|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-697 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 1082.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 1 MALSYLRPWASLLLVDMALL-ALLQGSPGNLLPLGLPGLWLEGTLR--------LGGLWGLLAVGGLLGRVGTFPPLLCL 71
Cdd:TIGR00958 1 AALAYLLPWFSLLLVDWALLrDLLQGIFGLLLPFEKGLYVLWLEGTlrlgvlwlGALGILLNKAGGLLAAVKPLVAALCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 72 ATPLFFSLRALVGGTMSSPAVRVASASWVWLLADYKAAALGWAVWAVLSPPGAREKEA--GQEKNKSLMWQLLRLSRPDL 149
Cdd:TIGR00958 81 ATPSLSSLRALAFWEALDPAVRVALGLWSWFVWSYGAALPAAALWAVLSSAGASEKEAeqGQSETADLLFRLLGLSGRDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 150 PFLMVAFFFLAWAVLGETLIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRGGSFLFTMSRINLRIRERL 229
Cdd:TIGR00958 161 PWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 230 FSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKV 309
Cdd:TIGR00958 241 FRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 310 YNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQV 389
Cdd:TIGR00958 321 FGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 390 LILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKVFCYIDRKPNLPQPGTLAPSRLEGRVE 469
Cdd:TIGR00958 401 LVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 470 FQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLV 549
Cdd:TIGR00958 481 FQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 550 GQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLI 629
Cdd:TIGR00958 561 GQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLI 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528078492 630 LDEATSALDSQCEQALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVE---HSQLREDQDVYAHLV 697
Cdd:TIGR00958 641 LDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEmgtHKQLMEDQGCYKHLV 711
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
132-703 |
1.93e-168 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 495.45 E-value: 1.93e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 132 EKNKSLMWQLLRLSRPDLPFLMVAFFFLAWAVLGETLIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRG 211
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 212 GSFLFTMSRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPR 291
Cdd:COG1132 83 YLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 292 LTFLSLLDLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDL 371
Cdd:COG1132 163 LALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 372 ERALYLAIRRVMALGMQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKVFCYIDRKP 451
Cdd:COG1132 243 LSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 452 NLPQP-GTLAPSRLEGRVEFQDVTFSYPsrP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLD 530
Cdd:COG1132 323 EIPDPpGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 531 GQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVG 610
Cdd:COG1132 401 GVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 611 QKQRLAIARALVRNPRVLILDEATSALDSQCEQALQA--WRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVE---HSQ 685
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEalERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEqgtHEE 560
|
570
....*....|....*...
gi 528078492 686 LREDQDVYAHLVQQRLEA 703
Cdd:COG1132 561 LLARGGLYARLYRLQFGE 578
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
155-443 |
4.14e-157 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 455.26 E-value: 4.14e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 155 AFFFLAWAVLGETLIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRGGSFLFTMSRINLRIRERLFSSLL 234
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 235 RQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRH 314
Cdd:cd18590 81 QQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 315 QAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQVLILNC 394
Cdd:cd18590 161 QKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYC 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 528078492 395 GVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18590 241 GRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
118-701 |
7.04e-128 |
|
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: 395.36 E-value: 7.04e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 118 VLSPPGAREKEAGQEKNKSLMWQLLRLSRPDLPFLMVAFFFLAwaVLGeTLIPHYSGRVID--ILGSDFDP-*SFASAIF 194
Cdd:COG2274 127 LLEPTPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLIN--LLA-LATPLFTQVVIDrvLPNQDLSTlWVLAIGLL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 195 FMCLFSVGSSLSagcRGGSFLFTMSRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSsDTSKMSRWLpynANILLRS 274
Cdd:COG2274 204 LALLFEGLLRLL---RSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFL---TGSLLTA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 275 LVK----VIGLyCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPR-HQAVLTEIQDATAKAGQVVrEAVGGLQTVRSFGAEE 349
Cdd:COG2274 277 LLDllfvLIFL-IVLFFYSPPLALVVLLLIPLYVLLGLLFQPRlRRLSREESEASAKRQSLLV-ETLRGIETIKALGAES 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 350 QEVSRYKEALERCRQLwwrrDLERALYLAIRRVMALGMQ----VLILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRN 425
Cdd:COG2274 355 RFRRRWENLLAKYLNA----RFKLRRLSNLLSTLSGLLQqlatVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQ 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 426 LVYMYGDMLSNVGAAEKVFCYIDRKP-NLPQPGTLAPSRLEGRVEFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGP 504
Cdd:COG2274 431 LIGLLQRFQDAKIALERLDDILDLPPeREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGR 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 505 NGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAAC 584
Cdd:COG2274 510 SGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAG 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 585 ADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCE----QALQAWRskGDRTVLVIA 660
Cdd:COG2274 590 LHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEaiilENLRRLL--KGRTVIIIA 667
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 528078492 661 HRLHTVQNVDQVLVLKQGQLVE---HSQLREDQDVYAHLVQQRL 701
Cdd:COG2274 668 HRLSTIRLADRIIVLDKGRIVEdgtHEELLARKGLYAELVQQQL 711
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
457-680 |
6.15e-120 |
|
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: 357.55 E-value: 6.15e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 457 GTLAPSRLEGRVEFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQ 536
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 537 YDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLA 616
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 617 IARALVRNPRVLILDEATSALDS----QCEQALQAWRSkgDRTVLVIAHRLHTVQNVDQVLVLKQGQL 680
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAeseqQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
190-696 |
2.22e-118 |
|
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: 366.35 E-value: 2.22e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 190 ASAIFFMCLFSVGSSLSAG-CRGGSFLFtMSRINLR----IRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWL 264
Cdd:TIGR02203 50 RSVLWWVPLVVIGLAVLRGiCSFVSTYL-LSWVSNKvvrdIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 265 PYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRS 344
Cdd:TIGR02203 129 TDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 345 FGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMA-LGMQVLILNCGVQQiLAGEVTRGGLLSFLLYQEEVGDYV 423
Cdd:TIGR02203 209 FGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIAsLALAVVLFIALFQA-QAGSLTAGDFTAFITAMIALIRPL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 424 RNLVYMYGDMLSNVGAAEKVFCYIDRKPNlPQPGTLAPSRLEGRVEFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVG 503
Cdd:TIGR02203 288 KSLTNVNAPMQRGLAAAESLFTLLDSPPE-KDTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 504 PNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYG-LKDCEDAQVMAAVRA 582
Cdd:TIGR02203 366 RSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGrTEQADRAEIERALAA 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 583 ACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQAW--RSKGDRTVLVIA 660
Cdd:TIGR02203 446 AYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAAleRLMQGRTTLVIA 525
|
490 500 510
....*....|....*....|....*....|....*....
gi 528078492 661 HRLHTVQNVDQVLVLKQGQLVE---HSQLREDQDVYAHL 696
Cdd:TIGR02203 526 HRLSTIEKADRIVVMDDGRIVErgtHNELLARNGLYAQL 564
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
468-699 |
2.37e-105 |
|
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: 320.64 E-value: 2.37e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRV 627
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 628 LILDEATSALDSQCEQALQAW--RSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVE---HSQLREDQDVYAHLVQQ 699
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEAldRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEqgtHDELMAQKGVYAKLVKA 237
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
155-443 |
7.02e-101 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 311.01 E-value: 7.02e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 155 AFFFLAWAVLGETLIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRGGSFLFTMSRINLRIRERLFSSLL 234
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 235 RQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRH 314
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 315 QAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQVLILNC 394
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 528078492 395 GVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18572 241 GGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
120-703 |
2.97e-91 |
|
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: 296.35 E-value: 2.97e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 120 SPPGAREKEAGQEKNKSLMWQLLRLSRPDLPFLMVAFFFLAWAVL-GETLIPHYSGRVIDILGSDFDP*SFASAIFFMCL 198
Cdd:COG5265 2 PSARAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLlAAALALVVPPLLKDAIDALLSGAAALLVVPVGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 199 FSVGSSlsagcRGGSFLFT------MSRINLRIRERL----FSSLLRQDLGFFQENKTGELN---SRLSSDTSKMSRWLP 265
Cdd:COG5265 82 LAYGLL-----RLLSVLFGelrdalFARVTQRAVRRLalevFRHLHALSLRFHLERQTGGLSrdiERGTKGIEFLLRFLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 266 YNANILLRSLVKVIGLycFMLQVSPRLTFLSLLDLPLTIA-----AEKVYNPRHQAVLTEiQDATAKAgqvvreaVGGL- 339
Cdd:COG5265 157 FNILPTLLEIALVAGI--LLVKYDWWFALITLVTVVLYIAftvvvTEWRTKFRREMNEAD-SEANTRA-------VDSLl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 340 --QTVRSFGAEEQEVSRYKEALERcrqlwwrrdLERAlylAIRRVMALGM----QVLILNCGV--------QQILAGEVT 405
Cdd:COG5265 227 nyETVKYFGNEAREARRYDEALAR---------YERA---AVKSQTSLALlnfgQALIIALGLtammlmaaQGVVAGTMT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 406 RGGL-------------LSFL--LYQEevgdyVRN-LVymygDMlsnvgaaEKVFCYIDRKPNL---PQPGTLAPSrlEG 466
Cdd:COG5265 295 VGDFvlvnayliqlyipLNFLgfVYRE-----IRQaLA----DM-------ERMFDLLDQPPEVadaPDAPPLVVG--GG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 467 RVEFQDVTFSYpsRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQV 546
Cdd:COG5265 357 EVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAI 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 547 VLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPR 626
Cdd:COG5265 435 GIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPP 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 627 VLILDEATSALDSQCEQALQ-AWR--SKGdRTVLVIAHRLHTVQNVDQVLVLKQGQLVE---HSQLREDQDVYAHL--VQ 698
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQaALRevARG-RTTLVIAHRLSTIVDADEILVLEAGRIVErgtHAELLAQGGLYAQMwaRQ 593
|
....*
gi 528078492 699 QRLEA 703
Cdd:COG5265 594 QEEEE 598
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
468-696 |
5.57e-89 |
|
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: 277.96 E-value: 5.57e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:cd03251 1 VEFKNVTFRYPGDG-PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRV 627
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 628 LILDEATSALDSQCEQALQAWRSK--GDRTVLVIAHRLHTVQNVDQVLVLKQGQLVE---HSQLREDQDVYAHL 696
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERlmKNRTTFVIAHRLSTIENADRIVVLEDGKIVErgtHEELLAQGGVYAKL 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
219-690 |
8.15e-89 |
|
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: 288.58 E-value: 8.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 219 SRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKM----SRWLPYnaniLLRSLVKVIGLYCFMLQVSPRLTF 294
Cdd:COG4988 87 ARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALdgyfARYLPQ----LFLAALVPLLILVAVFPLDWLSGL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 295 LSLLDLPLT--------IAAEKVyNPRHQAVLTEIqdatakAGQVVrEAVGGLQTVRSFGAEEQEVSRYKEALERcrqlw 366
Cdd:COG4988 163 ILLVTAPLIplfmilvgKGAAKA-SRRQWRALARL------SGHFL-DRLRGLTTLKLFGRAKAEAERIAEASED----- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 367 WRRDLERALYLAIRR------VMALGMQVLILNCGVQqILAGEVTRGGLLSFLL-----YQEevgdyVRNLVYMYGDMLS 435
Cdd:COG4988 230 FRKRTMKVLRVAFLSsavlefFASLSIALVAVYIGFR-LLGGSLTLFAALFVLLlapefFLP-----LRDLGSFYHARAN 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 436 NVGAAEKVFCYIDRKPNLPQPGTLAPSRLEG-RVEFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAA 514
Cdd:COG4988 304 GIAAAEKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGG--RPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 515 PLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPD 594
Cdd:COG4988 382 LLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPD 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 595 GIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQAL-QAWRS-KGDRTVLVIAHRLHTVQNVDQV 672
Cdd:COG4988 462 GLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEIlQALRRlAKGRTVILITHRLALLAQADRI 541
|
490 500
....*....|....*....|.
gi 528078492 673 LVLKQGQLVE---HSQLREDQ 690
Cdd:COG4988 542 LVLDDGRIVEqgtHEELLAKN 562
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
155-443 |
2.66e-87 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 275.73 E-value: 2.66e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 155 AFFFLAWAVLGETLIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRGGSFLFTMSRINLRIRERLFSSLL 234
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 235 RQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRH 314
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 315 QAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQVLILNC 394
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 528078492 395 GVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18784 241 GGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
223-696 |
2.48e-85 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 279.98 E-value: 2.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 223 LRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPL 302
Cdd:PRK11176 98 MTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 303 TIAAEKVYNPRHQAVLTEIQDA----TAKAGQVVReavgGLQTVRSFGAEEQEVSRYKEALERCRQLwwrrdleralyla 378
Cdd:PRK11176 178 VSIAIRVVSKRFRNISKNMQNTmgqvTTSAEQMLK----GHKEVLIFGGQEVETKRFDKVSNRMRQQ------------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 379 irrvmalGMQVL----ILNCGVQQI--LAgevtrgglLSFLLYQEEVGDYVRNL-------VY--MYGDM-----LSNV- 437
Cdd:PRK11176 241 -------GMKMVsassISDPIIQLIasLA--------LAFVLYAASFPSVMDTLtagtitvVFssMIALMrplksLTNVn 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 438 -------GAAEKVFCYIDRKPNLPQpGTLAPSRLEGRVEFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGPNGSGKS 510
Cdd:PRK11176 306 aqfqrgmAACQTLFAILDLEQEKDE-GKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKS 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 511 TVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLKD-CEDAQVMAAVRAACADDFI 589
Cdd:PRK11176 384 TIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEqYSREQIEEAARMAYAMDFI 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 590 GEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQAWRS--KGDRTVLVIAHRLHTVQ 667
Cdd:PRK11176 464 NKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDelQKNRTSLVIAHRLSTIE 543
|
490 500 510
....*....|....*....|....*....|..
gi 528078492 668 NVDQVLVLKQGQLVE---HSQLREDQDVYAHL 696
Cdd:PRK11176 544 KADEILVVEDGEIVErgtHAELLAQNGVYAQL 575
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
466-688 |
3.42e-85 |
|
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: 267.94 E-value: 3.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 466 GRVEFQDVTFSYpsRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQ 545
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 546 VVLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNP 625
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 626 RVLILDEATSALDSQCEQALQA--WRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVE---HSQLRE 688
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEalEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEegtHDELLA 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
468-699 |
4.40e-84 |
|
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: 265.25 E-value: 4.40e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPsrP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRV 627
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 628 LILDEATSALDSQCEQALQAW--RSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVE---HSQLREDQDVYAHLVQQ 699
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAAlrDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVErgtHEELLAKGGLYAEMWKA 235
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
155-443 |
9.55e-84 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 266.35 E-value: 9.55e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 155 AFFFLAWAVLGETLIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRGGSFLFTMSRINLRIRERLFSSLL 234
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 235 RQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRH 314
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 315 QAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQVLILNC 394
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 528078492 395 GVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18557 241 GGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
208-702 |
2.30e-78 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 264.68 E-value: 2.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 208 GCRGGSFLFTMSRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSsDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQ 287
Cdd:TIGR01846 197 GLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVR-ELEQIRNFLTGSALTVVLDLLFVVVFLAVMFF 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 288 VSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALerCRQLWW 367
Cdd:TIGR01846 276 YSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQL--AAYVAA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 368 RRDLERALYLA---IRRVMALGMqVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDmLSNVGAAEKVF 444
Cdd:TIGR01846 354 SFRVTNLGNIAgqaIELIQKLTF-AILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQD-FQQTGIALERL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 445 CYIDRKPNLPQP-GTLAPSRLEGRVEFQDVTFSY-PSRP*kPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQP 522
Cdd:TIGR01846 432 GDILNSPTEPRSaGLAALPELRGAITFENIRFRYaPDSP--EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTP 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 523 TGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGE 602
Cdd:TIGR01846 510 QHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGE 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 603 KGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQAWRSK--GDRTVLVIAHRLHTVQNVDQVLVLKQGQL 680
Cdd:TIGR01846 590 KGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREicRGRTVIIIAHRLSTVRACDRIIVLEKGQI 669
|
490 500
....*....|....*....|....*
gi 528078492 681 VE---HSQLREDQDVYAHLVQQRLE 702
Cdd:TIGR01846 670 AEsgrHEELLALQGLYARLWQQQSG 694
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
468-679 |
8.50e-74 |
|
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: 235.74 E-value: 8.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSGSVKDNIayglkdcedaqvmaavraacaddfigempdgihteigekgsqLAVGQKQRLAIARALVRNPRV 627
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 628 LILDEATSALDSQCE----QALQAWRskGDRTVLVIAHRLHTVQNVDQVLVLKQGQ 679
Cdd:cd03228 118 LILDEATSALDPETEalilEALRALA--KGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
224-699 |
9.03e-74 |
|
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: 248.91 E-value: 9.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 224 RIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMsrwlpynANILLR-------SLVKVIGLYCFMLQVSPRL---- 292
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDAL-------DNLYLRvllpllvALLVILAAVAFLAFFSPALalvl 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 293 ---TFLSLLDLPLTIAAekvynpRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERcrqlWWRR 369
Cdd:COG4987 162 algLLLAGLLLPLLAAR------LGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEAR----LAAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 370 DLERALYLAIRR-VMALGMQ-----VLILncGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:COG4987 232 QRRLARLSALAQaLLQLAAGlavvaVLWL--AAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 444 FCYIDRKPNLPQPGTLAPSRLEGRVEFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPT 523
Cdd:COG4987 310 NELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 524 GGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEK 603
Cdd:COG4987 389 SGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEG 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 604 GSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQA--WRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLV 681
Cdd:COG4987 469 GRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAdlLEALAGRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
490 500
....*....|....*....|.
gi 528078492 682 E---HSQLREDQDVYAHLVQQ 699
Cdd:COG4987 549 EqgtHEELLAQNGRYRQLYQR 569
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
466-681 |
2.07e-69 |
|
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: 225.93 E-value: 2.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 466 GRVEFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQ 545
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 546 VVLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNP 625
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 626 RVLILDEATSALDSQCE----QALQAWRskGDRTVLVIAHRLHTVQNVDQVLVLKQGQLV 681
Cdd:cd03245 160 PILLLDEPTSAMDMNSEerlkERLRQLL--GDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
468-698 |
2.61e-67 |
|
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: 221.21 E-value: 2.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYpsRP*KP-VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQV 546
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 547 VLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPR 626
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 627 VLILDEATSALDSQCEQALQAWRSK--GDRTVLVIAHRLHTVQNVDQVLVLKQGQLVE---HSQLREDQDVYAHLVQ 698
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDicAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEqgsHDELLAENGLYAYLYQ 235
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
466-682 |
2.27e-66 |
|
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: 218.13 E-value: 2.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 466 GRVEFQDVTFSYpsRP-*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHR 544
Cdd:cd03244 1 GDIEFKNVSLRY--RPnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVGQEPVLFSGSVKDNIAyGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRN 624
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD-PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 625 PRVLILDEATSALDSQCEQALQ-AWRSK-GDRTVLVIAHRLHTVQNVDQVLVLKQGQLVE 682
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQkTIREAfKDCTVLTIAHRLDTIIDSDRILVLDKGRVVE 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
332-682 |
9.20e-66 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 227.92 E-value: 9.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 332 VREAVGGLQTVRSF---GAEEQEVSRYKEALERCrQL----WWrrdlerALYLAIRRVMALGMQVLILNCGVQQILAGEV 404
Cdd:PRK13657 198 VSDAIGNVSVVQSYnriEAETQALRDIADNLLAA-QMpvlsWW------ALASVLNRAASTITMLAILVLGAALVQKGQL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 405 TRGGLLSF-----LLYQ--EEVGDYVrNLVYM-------YGDMLSNVGAAEKvfcyidrKPNLPQPGtlapsRLEGRVEF 470
Cdd:PRK13657 271 RVGEVVAFvgfatLLIGrlDQVVAFI-NQVFMaapkleeFFEVEDAVPDVRD-------PPGAIDLG-----RVKGAVEF 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 471 QDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVG 550
Cdd:PRK13657 338 DDVSFSYDNS--RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVF 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 551 QEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLIL 630
Cdd:PRK13657 416 QDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILIL 495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 631 DEATSALDSQCE----QALQAWRSkgDRTVLVIAHRLHTVQNVDQVLVLKQGQLVE 682
Cdd:PRK13657 496 DEATSALDVETEakvkAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
225-675 |
1.21e-64 |
|
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: 223.32 E-value: 1.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 225 IRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKM----SRWLP--YNANILLRSLVKVIglycfmLQVSPRLTFLSLL 298
Cdd:TIGR02857 79 LRERLLEAVAALGPRWLQGRPSGELATLALEGVEALdgyfARYLPqlVLAVIVPLAILAAV------FPQDWISGLILLL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 299 DLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQlwwrRDLE--RALY 376
Cdd:TIGR02857 153 TAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRE----RTMRvlRIAF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 377 L---AIRRVMALGMQVLILNCGVQqILAGEVT-RGGLLSFLLyQEEVGDYVRNLVYMYGDMLSNVGAAEKVFCYIDRKPN 452
Cdd:TIGR02857 229 LssaVLELFATLSVALVAVYIGFR-LLAGDLDlATGLFVLLL-APEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 453 LPQPGTLAPSRLEGRVEFQDVTFSYPSRP*kPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQ 532
Cdd:TIGR02857 307 PLAGKAPVTAAPASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 533 PLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQK 612
Cdd:TIGR02857 385 PLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQA 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 613 QRLAIARALVRNPRVLILDEATSALDSQCEQALQA--WRSKGDRTVLVIAHRLHTVQNVDQVLVL 675
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEalRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
152-416 |
1.75e-64 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 214.81 E-value: 1.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 152 LMVAFFFLAWAVLGETLIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRGGSFLF--TMSRINLRIRERL 229
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLnhTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 230 FSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKV 309
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 310 YNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQV 389
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260
....*....|....*....|....*..
gi 528078492 390 LILNCGVQQILAGEVTRGGLLSFLLYQ 416
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLF 267
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
224-701 |
1.19e-62 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 219.59 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 224 RIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLT 303
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 304 IAAEKVYN----P---RHQAVLTEIQDAtakagqvVREAVGGL-------QTVRsFGAEEQEVSR--YKEALERCRqlww 367
Cdd:PRK10790 179 LVVMVIYQrystPivrRVRAYLADINDG-------FNEVINGMsviqqfrQQAR-FGERMGEASRshYMARMQTLR---- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 368 rrdLERALylaIRRVMALgMQVLILnCGVQQIL----AGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:PRK10790 247 ---LDGFL---LRPLLSL-FSALIL-CGLLMLFgfsaSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 444 FCYIDRkpnlPQPGTLAPSRL--EGRVEFQDVTFSYpsRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQ 521
Cdd:PRK10790 319 FELMDG----PRQQYGNDDRPlqSGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 522 PTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGlKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIG 601
Cdd:PRK10790 393 LTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG-RDISEEQVWQALETVQLAELARSLPDGLYTPLG 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 602 EKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQ-AWRSKGDRTVL-VIAHRLHTVQNVDQVLVLKQGQ 679
Cdd:PRK10790 472 EQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQqALAAVREHTTLvVIAHRLSTIVEADTILVLHRGQ 551
|
490 500
....*....|....*....|....*
gi 528078492 680 LVE---HSQLREDQDVYAHLVQQRL 701
Cdd:PRK10790 552 AVEqgtHQQLLAAQGRYWQMYQLQL 576
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
157-443 |
1.70e-59 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 202.32 E-value: 1.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 157 FFLAWAVLGETLIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRGGSFLFTMSRINLRIRERLFSSLLRQ 236
Cdd:cd18589 3 GLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 237 DLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQA 316
Cdd:cd18589 83 EIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 317 VLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQVLILNCGV 396
Cdd:cd18589 163 LAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 528078492 397 QQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18589 243 QLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
454-700 |
1.50e-58 |
|
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: 207.68 E-value: 1.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 454 PQPGTLAPSRLEGRVEFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQP 533
Cdd:COG4618 317 AEPERMPLPRPKGRLSVENLTVVPPGSK-RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 534 LVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAyGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQ 613
Cdd:COG4618 396 LSQWDREELGRHIGYLPQDVELFDGTIAENIA-RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 614 RLAIARALVRNPRVLILDEATSALDSQCEQAL----QAWRSKGdRTVLVIAHRLHTVQNVDQVLVLKQGQlVEHSQLREd 689
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALaaaiRALKARG-ATVVVITHRPSLLAAVDKLLVLRDGR-VQAFGPRD- 551
|
250
....*....|.
gi 528078492 690 qDVYAHLVQQR 700
Cdd:COG4618 552 -EVLARLARPA 561
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
238-697 |
2.29e-58 |
|
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: 209.98 E-value: 2.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 238 LGFFQENKTGELNSRLSsDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAV 317
Cdd:TIGR01193 244 MSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 318 LTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQVLILNCGVQ 397
Cdd:TIGR01193 323 NHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAY 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 398 QILAGEVTRGGLLSFLLyqeevgdyvrnLVYMYGDMLSNVgaaekvfcyIDRKPNLpQPGTLAPSRLE------------ 465
Cdd:TIGR01193 403 LVMRGKLTLGQLITFNA-----------LLSYFLTPLENI---------INLQPKL-QAARVANNRLNevylvdsefink 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 466 ----------GRVEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLV 535
Cdd:TIGR01193 462 kkrtelnnlnGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 536 QYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLKD-CEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQR 614
Cdd:TIGR01193 540 DIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKEnVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQR 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 615 LAIARALVRNPRVLILDEATSALDSQCEQA-LQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVE---HSQLREDQ 690
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEKKiVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEqgsHDELLDRN 699
|
....*..
gi 528078492 691 DVYAHLV 697
Cdd:TIGR01193 700 GFYASLI 706
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
142-701 |
2.53e-58 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 209.43 E-value: 2.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 142 LRLSRPDLpfLMVAFFFLAWAVLGeTLIPHYSGRVIDilgsDFDP*SFASAIFFMCLFSVGSSLSAGcrggSFLFTMSRI 221
Cdd:TIGR03797 131 LRGARRDL--LAILAMGLLGTLLG-MLVPIATGILIG----TAIPDADRSLLVQIALALLAAAVGAA----AFQLAQSLA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 222 NLRIRERLFSS--------LLRQDLGFFQENKTGELNSRLSSdTSKMSRWLpynANILLRSLVKVI-GLYCF--MLQVSP 290
Cdd:TIGR03797 200 VLRLETRMDASlqaavwdrLLRLPVSFFRQYSTGDLASRAMG-ISQIRRIL---SGSTLTTLLSGIfALLNLglMFYYSW 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 291 RLTFLSLLDLPLTIA---AEKVYNPRHQAVLTEIQDATAkaGQVVrEAVGGLQTVRSFGAEEQEVSRYkeALERCRQLWW 367
Cdd:TIGR03797 276 KLALVAVALALVAIAvtlVLGLLQVRKERRLLELSGKIS--GLTV-QLINGISKLRVAGAENRAFARW--AKLFSRQRKL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 368 RRDLER-ALYLAIRRVM--ALGMQVLILNCGvQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKVf 444
Cdd:TIGR03797 351 ELSAQRiENLLTVFNAVlpVLTSAALFAAAI-SLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERA- 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 445 cyidrKPNLPQP-----GTLAPSRLEGRVEFQDVTFSY-PSRP*kPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQN 518
Cdd:TIGR03797 429 -----KPILEALpevdeAKTDPGKLSGAIEVDRVTFRYrPDGP--LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLG 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 519 LYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDfIGEMPDGIHT 598
Cdd:TIGR03797 502 FETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAED-IRAMPMGMHT 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 599 EIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQG 678
Cdd:TIGR03797 581 VISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAG 660
|
570 580
....*....|....*....|....*.
gi 528078492 679 QLVE---HSQLREDQDVYAHLVQQRL 701
Cdd:TIGR03797 661 RVVQqgtYDELMAREGLFAQLARRQL 686
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
214-703 |
8.33e-57 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 203.02 E-value: 8.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 214 FLFTMS-RINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFM-LQVSPR 291
Cdd:PRK10789 59 LLFGASyQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 292 LTFLSLLDLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKE-ALERCRQlwwrrd 370
Cdd:PRK10789 139 LTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAAdAEDTGKK------ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 371 lerALYLAirRV---------MALGM-QVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAA 440
Cdd:PRK10789 213 ---NMRVA--RIdarfdptiyIAIGMaNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAY 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 441 EKVFCYIDRKPNLpQPGTLAPSRLEGRVEFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLY 520
Cdd:PRK10789 288 SRIRAMLAEAPVV-KDGSEPVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 521 QPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEI 600
Cdd:PRK10789 366 DVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEV 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 601 GEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCE----QALQAWRSKgdRTVLVIAHRLHTVQNVDQVLVLK 676
Cdd:PRK10789 446 GERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEhqilHNLRQWGEG--RTVIISAHRLSALTEASEILVMQ 523
|
490 500 510
....*....|....*....|....*....|....
gi 528078492 677 QGQLVE---HSQLRED----QDVYAHlvqQRLEA 703
Cdd:PRK10789 524 HGHIAQrgnHDQLAQQsgwyRDMYRY---QQLEA 554
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
483-703 |
2.14e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 196.60 E-value: 2.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTvaapLQNL------YQptgGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLF 556
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTS----LLNAllgflpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 557 SGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSA 636
Cdd:PRK11174 436 HGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 637 LDSQCEQAL-----QAWRSKgdrTVLVIAHRLHTVQNVDQVLVLKQGQLVE---HSQLREDQDVYAHLVQQRLEA 703
Cdd:PRK11174 516 LDAHSEQLVmqalnAASRRQ---TTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAELSQAGGLFATLLAHRQEE 587
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
220-663 |
2.34e-49 |
|
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: 181.40 E-value: 2.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 220 RINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMsrwlpynANILLRSLVKVIG---LYCFMLQVSPRLTFLS 296
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDAL-------QDLYVRVIVPAGValvVGAAAVAAIAVLSVPA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 297 LLDLPLTIAAEKVYNPRHQAVLTEIQDATAKAG-----QVVREAVGGLQTVRSFGAEEQEVSRYKEALERC-----RQLW 366
Cdd:TIGR02868 156 ALILAAGLLLAGFVAPLVSLRAARAAEQALARLrgelaAQLTDALDGAAELVASGALPAALAQVEEADRELtraerRAAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 367 WRRdLERALYLAIRRVMALGMQVLilncGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKVFCY 446
Cdd:TIGR02868 236 ATA-LGAALTLLAAGLAVLGALWA----GGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 447 IDRKP-----NLPQPGTLAPSrlEGRVEFQDVTFSYPSRP*kPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQ 521
Cdd:TIGR02868 311 LDAAGpvaegSAPAAGAVGLG--KPTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 522 PTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIG 601
Cdd:TIGR02868 387 PLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLG 466
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 602 EKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQAWRSKGD--RTVLVIAHRL 663
Cdd:TIGR02868 467 EGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALsgRTVVLITHHL 530
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
152-443 |
2.04e-48 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 171.96 E-value: 2.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 152 LMVAFFFLAWAVLGETLIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRGGSFLFTMSRINLRIRERLFS 231
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 232 SLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYN 311
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 312 PRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQVLI 391
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 528078492 392 LNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
225-698 |
1.88e-47 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 181.77 E-value: 1.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 225 IRERLFSSLLRQDLGFFQENKT--GELNSRLSSDTSKMSRWLPYN----ANILLRSLVKVIGLYCFMLQVSPRLTFLSLL 298
Cdd:PTZ00265 901 MKRRLFENILYQEISFFDQDKHapGLLSAHINRDVHLLKTGLVNNivifTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFI 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 299 DLPL-----TIAAEK------VYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWW 367
Cdd:PTZ00265 981 FMRVfairaRLTANKdvekkeINQPGTVFAYNSDDEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQK 1060
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 368 RRDLERALYLAIRRVMALGMQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKVFCYI 447
Cdd:PTZ00265 1061 RKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLI 1140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 448 DRKPNLP--QPGTLA---PSRLEGRVEFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLY-- 520
Cdd:PTZ00265 1141 IRKSNIDvrDNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdl 1220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 521 ----------QPTG------------------------------------------GQLLLDGQPLVQYDHHYLHRQVVL 548
Cdd:PTZ00265 1221 kndhhivfknEHTNdmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSI 1300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 549 VGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVL 628
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 629 ILDEATSALDSQCEQALQAW----RSKGDRTVLVIAHRLHTVQNVDQVLVL----KQGQLVE----HSQLREDQD-VYAH 695
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTivdiKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQahgtHEELLSVQDgVYKK 1460
|
...
gi 528078492 696 LVQ 698
Cdd:PTZ00265 1461 YVK 1463
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
155-443 |
3.18e-47 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 168.85 E-value: 3.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 155 AFFFLAWAVLGETLIPHYSGRVIDILGSDFDP*SFAS------AIFFMCLFSVGSSLSAGcrgGSFLFTMS--RINLRIR 226
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGlslktfALALLGVFVVGAAANFG---RVYLLRIAgeRIVARLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 227 ERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAA 306
Cdd:cd18573 78 KRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 307 EKVYNpRHQAVLT-EIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMAL 385
Cdd:cd18573 158 AVFYG-RYVRKLSkQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGN 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 386 GMQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18573 237 LSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
224-698 |
4.36e-47 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 180.56 E-value: 4.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 224 RIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPrLTFLSLLDLPLT 303
Cdd:PLN03232 984 RLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVST-ISLWAIMPLLIL 1062
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 304 IAAEKVYnprHQAVLTEIQ--DATAKAGQVVR--EAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRrDLERALYLAI 379
Cdd:PLN03232 1063 FYAAYLY---YQSTSREVRrlDSVTRSPIYAQfgEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLA-NTSSNRWLTI 1138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 380 RRVMALGMQVL------ILNCGVQQILAGEVTRGGLLsfLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKVFCYIDRKPNL 453
Cdd:PLN03232 1139 RLETLGGVMIWltatfaVLRNGNAENQAGFASTMGLL--LSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEA 1216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 454 P------QPGTLAPSRleGRVEFQDVTFSY-PSRP*kPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQ 526
Cdd:PLN03232 1217 TaiiennRPVSGWPSR--GSIKFEDVHLRYrPGLP--PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGR 1292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 527 LLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAyGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQ 606
Cdd:PLN03232 1293 IMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID-PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGEN 1371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 607 LAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQAWRSKGDR--TVLVIAHRLHTVQNVDQVLVLKQGQLVEHS 684
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKscTMLVIAHRLNTIIDCDKILVLSSGQVLEYD 1451
|
490
....*....|....*...
gi 528078492 685 Q----LREDQDVYAHLVQ 698
Cdd:PLN03232 1452 SpqelLSRDTSAFFRMVH 1469
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
155-443 |
5.23e-47 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 168.20 E-value: 5.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 155 AFFFLAWAVLGETLIPHYSGRVIDILGSDFDP*SFAS------AIFFMCLFSVGSSLSAGCRggSFLFTMS--RINLRIR 226
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEAlralnqAVLILLGVVLIGSIATFLR--SWLFTLAgeRVVARLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 227 ERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAA 306
Cdd:cd18780 79 KRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 307 EKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALG 386
Cdd:cd18780 159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 387 MQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18780 239 AIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
468-681 |
2.01e-45 |
|
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: 161.73 E-value: 2.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPsrP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPV--LFSGSVKDNIAYGLK--DCEDAQVMAAVRAACA----DDFIGEMPdgihteigekgSQLAVGQKQRLAIAR 619
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPEnlGLPREEIRERVEEALElvglEHLADRPP-----------HELSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 620 ALVRNPRVLILDEATSALD--SQCE--QALQAWRSKGdRTVLVIAHRLHTV-QNVDQVLVLKQGQLV 681
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDprGRREllELLKRLNKEG-KTVIIVTHDLDLVaELADRVIVLDDGRIV 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
224-700 |
8.34e-45 |
|
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: 173.59 E-value: 8.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 224 RIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPrltFLSLLDLPLT 303
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATP---IAAVIIPPLG 1115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 304 IA---AEKVY--NPRHQAVLTEIQDATAKAGqvVREAVGGLQTVRSFgaEEQEVSRYKEALERCRQlwwrrdlERALYLA 378
Cdd:TIGR00957 1116 LLyffVQRFYvaSSRQLKRLESVSRSPVYSH--FNETLLGVSVIRAF--EEQERFIHQSDLKVDEN-------QKAYYPS 1184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 379 I--RRVMALGMQvLILNCGVQ-QILAGEVTRGGLLSFLL-----YQEEVGDYVRNLVYMYGDMLSNVGAAEKVFCYIDRK 450
Cdd:TIGR00957 1185 IvaNRWLAVRLE-CVGNCIVLfAALFAVISRHSLSAGLVglsvsYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETE 1263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 451 PNLPQ--PGTLAPSRL--EGRVEFQDVTFSYpsRP-*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGG 525
Cdd:TIGR00957 1264 KEAPWqiQETAPPSGWppRGRVEFRNYCLRY--REdLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEG 1341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 526 QLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAyGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGS 605
Cdd:TIGR00957 1342 EIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGE 1420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 606 QLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQAW-RSK-GDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEH 683
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTiRTQfEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEF 1500
|
490
....*....|....*..
gi 528078492 684 sqlredqDVYAHLVQQR 700
Cdd:TIGR00957 1501 -------GAPSNLLQQR 1510
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
345-683 |
2.81e-44 |
|
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: 166.62 E-value: 2.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 345 FGAEEQEVSRyKEALERCRQLWWRRDLERALY-------------LAIRRVMALGMQVLILN--------CGVQQILA-- 401
Cdd:COG1123 107 EALENLGLSR-AEARARVLELLEAVGLERRLDryphqlsggqrqrVAIAMALALDPDLLIADepttaldvTTQAEILDll 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 402 GEVTRGGLLSFLL---YQEEVGDYVRNLVYMYGDMLSNVGAAEKVFCYIDRKPNLPQPGTLAPSRLEGR------VEFQD 472
Cdd:COG1123 186 RELQRERGTTVLLithDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAaaaeplLEVRN 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 473 VTFSYPSRP*KPV--LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDH---HYLHRQVV 547
Cdd:COG1123 266 LSKRYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQ 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPV--LFSG-SVKDNIAYGLK---DCEDAQVMAAVRAACAD-----DFIGEMPdgihteigekgSQLAVGQKQRLA 616
Cdd:COG1123 346 MVFQDPYssLNPRmTVGDIIAEPLRlhgLLSRAERRERVAELLERvglppDLADRYP-----------HELSGGQRQRVA 414
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 617 IARALVRNPRVLILDEATSALD--SQCE--QALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH 683
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDvsVQAQilNLLRDLQRELGLTYLFISHDLAVVRYIaDRVAVMYDGRIVED 486
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
469-680 |
4.02e-44 |
|
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: 156.22 E-value: 4.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVL 548
Cdd:cd03246 2 EVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 549 VGQEPVLFSGSVKDNIayglkdcedaqvmaavraacaddfigempdgihteigekgsqLAVGQKQRLAIARALVRNPRVL 628
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 629 ILDEATSALDSQCEQAL-QAWRS--KGDRTVLVIAHRLHTVQNVDQVLVLKQGQL 680
Cdd:cd03246 119 VLDEPNSHLDVEGERALnQAIAAlkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
466-683 |
7.47e-44 |
|
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: 156.80 E-value: 7.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 466 GRVEFQDVTFSY-PSRP*kPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHR 544
Cdd:cd03369 5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVGQEPVLFSGSVKDNI-AYGLKDceDAQVMAAVRaacaddfigempdgihteIGEKGSQLAVGQKQRLAIARALVR 623
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 624 NPRVLILDEATSALDSQCEQALQ-AWRSK-GDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEH 683
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQkTIREEfTNSTILTIAHRLRTIIDYDKILVMDAGEVKEY 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
486-635 |
1.01e-43 |
|
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: 154.34 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSG-SVKDNI 564
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528078492 565 AYGLKDCEDAQVMAAVRAACADDFIGeMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATS 635
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
439-699 |
1.10e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 165.77 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 439 AAEKVFCYIDRKPNLPQPGTLAPSRLEGRVEFQDVTFSYPSRP*kPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQN 518
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 519 LYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIgEMPDGIHT 598
Cdd:PRK11160 389 AWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLL-EDDKGLNA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 599 EIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCE-QALQAWRSKG-DRTVLVIAHRLHTVQNVDQVLVLK 676
Cdd:PRK11160 468 WLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETErQILELLAEHAqNKTVLMITHRLTGLEQFDRICVMD 547
|
250 260
....*....|....*....|....*.
gi 528078492 677 QGQLVE---HSQLREDQDVYAHLVQQ 699
Cdd:PRK11160 548 NGQIIEqgtHQELLAQQGRYYQLKQR 573
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
468-679 |
4.05e-43 |
|
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: 154.55 E-value: 4.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*--KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLlldgqplvqydhhYLHRQ 545
Cdd:cd03250 1 ISVEDASFTWDSGEQetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 546 VVLVGQEPVLFSGSVKDNIAYGLKdcEDAQ-VMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRN 624
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP--FDEErYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528078492 625 PRVLILDEATSALDSQCEQALqaWRS------KGDRTVLVIAHRLHTVQNVDQVLVLKQGQ 679
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHI--FENcilgllLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
469-680 |
4.17e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 154.59 E-value: 4.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVL 548
Cdd:COG4619 2 ELEGLSFRVGG---KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 549 VGQEPVLFSGSVKDNIAY-----GLKDCEDAQVMAAVRAACADDFIgempdgiHTEIgekgSQLAVGQKQRLAIARALVR 623
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDIL-------DKPV----ERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 624 NPRVLILDEATSALDSQ----CEQALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQL 680
Cdd:COG4619 148 QPDVLLLDEPTSALDPEntrrVEELLREYLAEEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
469-703 |
4.10e-42 |
|
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: 153.09 E-value: 4.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLhRQVVL 548
Cdd:COG4555 3 EVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 549 VGQEPVLFSG-SVKDNI-----AYGLKDCEDAQVMAAVraacADDFigEMPDGIHTEIGEkgsqLAVGQKQRLAIARALV 622
Cdd:COG4555 79 LPDERGLYDRlTVRENIryfaeLYGLFDEELKKRIEEL----IELL--GLEEFLDRRVGE----LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 623 RNPRVLILDEATSALD--SQCE--QALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLredQDVYAHLV 697
Cdd:COG4555 149 HDPKVLLLDEPTNGLDvmARRLlrEILRALKKEG-KTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSL---DELREEIG 224
|
....*.
gi 528078492 698 QQRLEA 703
Cdd:COG4555 225 EENLED 230
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
469-679 |
9.09e-42 |
|
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: 151.08 E-value: 9.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVL 548
Cdd:cd03225 1 ELKNLSFSYPDGA-RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 549 VGQEP--VLFSGSVKDNIAYGLK-DCEDAQVMAAVRAACADDFigEMPDGIHTEIgekgSQLAVGQKQRLAIARALVRNP 625
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLEnLGLPEEEIEERVEEALELV--GLEGLRDRSP----FTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 626 RVLILDEATSALDSQCEQALQAW----RSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQ 679
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELlkklKAEG-KTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
180-689 |
4.22e-41 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 162.12 E-value: 4.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 180 LGSDFDP*SFASAIFFMCLFsVGSSLSAGCRGgsflFTMSRINLRIRERLFSSLLRQDlGFFQENKTGelnSRLSSDtsk 259
Cdd:PTZ00265 92 LGENVNDIIFSLVLIGIFQF-ILSFISSFCMD----VVTTKILKTLKLEFLKSVFYQD-GQFHDNNPG---SKLTSD--- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 260 MSRWLP-YNANILLRSLV------KVIGLYCFMLQVSPRLTFLSLLDLPL-----TIAAEKVYNPRHQAVLTEIQDATak 327
Cdd:PTZ00265 160 LDFYLEqVNAGIGTKFITiftyasAFLGLYIWSLFKNARLTLCITCVFPLiyicgVICNKKVKINKKTSLLYNNNTMS-- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 328 agqVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMAL---------GMQVLILNCGVQQ 398
Cdd:PTZ00265 238 ---IIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILasyafgfwyGTRIIISDLSNQQ 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 399 ------------ILAGEVTRGGLLSFLLyqEEVGDYVRNLvymygdmlsnvGAAEKVFCYIDRKPNLP--QPGTLAPSRl 464
Cdd:PTZ00265 315 pnndfhggsvisILLGVLISMFMLTIIL--PNITEYMKSL-----------EATNSLYEIINRKPLVEnnDDGKKLKDI- 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 465 eGRVEFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLL-DGQPLVQYDHHYLH 543
Cdd:PTZ00265 381 -KKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWR 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 544 RQVVLVGQEPVLFSGSVKDNIAYGLKDCEDAQVMA------------------AVRAACAD------------------- 586
Cdd:PTZ00265 460 SKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLEALSnyynedgndsqenknkrnSCRAKCAGdlndmsnttdsneliemrk 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 587 --------------------DFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQ 646
Cdd:PTZ00265 540 nyqtikdsevvdvskkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 528078492 647 A----WRSKGDRTVLVIAHRLHTVQNVDQVLVL---KQGQLVEHSQLRED 689
Cdd:PTZ00265 620 KtinnLKGNENRITIIIAHRLSTIRYANTIFVLsnrERGSTVDVDIIGED 669
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
168-443 |
8.98e-41 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 150.71 E-value: 8.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 168 LIPHYSGRVIDILGSDFDP*SFAS-AIFFMCLFSVGSSLSAGcrgGSFLFTMS--RINLRIRERLFSSLLRQDLGFFQEN 244
Cdd:cd18576 14 VFPLLAGQLIDAALGGGDTASLNQiALLLLGLFLLQAVFSFF---RIYLFARVgeRVVADLRKDLYRHLQRLPLSFFHER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 245 KTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLTEIQDA 324
Cdd:cd18576 91 RVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 325 TAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQVLILNCGVQQILAGEV 404
Cdd:cd18576 171 LAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGEL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 528078492 405 TRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18576 251 TAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
468-685 |
1.40e-39 |
|
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: 145.40 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLY-----QPTGGQLLLDGQPL--VQYDHH 540
Cdd:cd03260 1 IELRDLNVYYGD---KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 541 YLHRQVVLVGQEPVLFSGSVKDNIAYGLK-------DCEDAQVMAAVRAACADDfigEMPDGIHteigekGSQLAVGQKQ 613
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgiklkEELDERVEEALRKAALWD---EVKDRLH------ALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 614 RLAIARALVRNPRVLILDEATSALD----SQCEQALQawRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQ 685
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDpistAKIEELIA--ELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGP 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
468-683 |
3.41e-39 |
|
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: 144.19 E-value: 3.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*K-PVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHH---YLH 543
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 544 RQVVLVGQE------PVLfsgSVKDNIAYGLKDCEDAQVMAAVRAACADDFIG-EMPDGIhteIGEKGSQLAVGQKQRLA 616
Cdd:cd03257 82 KEIQMVFQDpmsslnPRM---TIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvGLPEEV---LNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 617 IARALVRNPRVLILDEATSALDS----QCEQALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH 683
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVsvqaQILDLLKKLQEELGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEE 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
468-702 |
1.80e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 142.51 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQyDHHYLHRQVV 547
Cdd:COG1131 1 IEVRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSG-SVKDNIAY--GLKDCEDAQVMAAVRAACaDDFigempdGIHTEIGEKGSQLAVGQKQRLAIARALVRN 624
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFfaRLYGLPRKEARERIDELL-ELF------GLTDAADRKVGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 625 PRVLILDEATSALD--SQCE--QALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH---SQLREDQ--DVYA 694
Cdd:COG1131 150 PELLILDEPTSGLDpeARRElwELLRELAAEG-KTVLLSTHYLEEAERLcDRVAIIDKGRIVADgtpDELKARLleDVFL 228
|
....*...
gi 528078492 695 HLVQQRLE 702
Cdd:COG1131 229 ELTGEEAR 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
467-681 |
3.48e-38 |
|
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: 142.49 E-value: 3.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 467 RVEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQV 546
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 547 VLVGQEPVL-FSGSVKDNIAYG------LKDCEDAQVMAAVRAACADdfigempdgihTEIGEKG----SQLAVGQKQRL 615
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGryphlgLFGRPSAEDREAVEEALER-----------TGLEHLAdrpvDELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528078492 616 AIARALVRNPRVLILDEATSALD--SQCE--QALQAWRSKGDRTVLVIAHRL-HTVQNVDQVLVLKQGQLV 681
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDlaHQLEvlELLRRLARERGRTVVMVLHDLnLAARYADRLVLLKDGRIV 217
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
155-443 |
5.18e-38 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 143.01 E-value: 5.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 155 AFFFLAWAVLGETLIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRggsFLFTMS---RINLRIRERLFS 231
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALR---FYLVSWlgeRVVADLRKAVFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 232 SLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYN 311
Cdd:cd18575 78 HLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 312 PRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQVLI 391
Cdd:cd18575 158 RRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 528078492 392 LNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18575 238 LWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
211-698 |
1.00e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 151.81 E-value: 1.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 211 GGSFLFTMSRINL--RIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQV 288
Cdd:PLN03130 972 LNSYWLIMSSLYAakRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIV 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 289 SPrLTFLSLLDLPLTIAAEKVYnprHQAVLTEIQ--DATAKAGQVVR--EAVGGLQTVRSFGAEEQEVSRYKEALE-RCR 363
Cdd:PLN03130 1052 ST-ISLWAIMPLLVLFYGAYLY---YQSTAREVKrlDSITRSPVYAQfgEALNGLSTIRAYKAYDRMAEINGRSMDnNIR 1127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 364 QLWWRRDLERalYLAIRrVMALG--MQVLILNCGV--------QQILAGevTRGGLLSFLLYQEEVGDYVRNLVYMYGDM 433
Cdd:PLN03130 1128 FTLVNMSSNR--WLAIR-LETLGglMIWLTASFAVmqngraenQAAFAS--TMGLLLSYALNITSLLTAVLRLASLAENS 1202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 434 LSNVgaaEKVFCYIDRKP--------NLPQPGTlaPSrlEGRVEFQDVTFSY-PSRP*kPVLKGLTFTLHPGKVTALVGP 504
Cdd:PLN03130 1203 LNAV---ERVGTYIDLPSeaplvienNRPPPGW--PS--SGSIKFEDVVLRYrPELP--PVLHGLSFEISPSEKVGIVGR 1273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 505 NGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKDNIAyGLKDCEDAQVMAAVRAAC 584
Cdd:PLN03130 1274 TGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD-PFNEHNDADLWESLERAH 1352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 585 ADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQawrsKGDR------TVLV 658
Cdd:PLN03130 1353 LKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQ----KTIReefkscTMLI 1428
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 528078492 659 IAHRLHTVQNVDQVLVLKQGQLVEHSQ----LREDQDVYAHLVQ 698
Cdd:PLN03130 1429 IAHRLNTIIDCDRILVLDAGRVVEFDTpenlLSNEGSAFSKMVQ 1472
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
464-698 |
1.08e-37 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 141.20 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 464 LEGRVEFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLH 543
Cdd:cd03288 16 LGGEIKIHDLCVRYENN-LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 544 RQVVLVGQEPVLFSGSVKDNIAYGLKdCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVR 623
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 624 NPRVLILDEATSALDSQCEQALQ--AWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEH----SQLREDQDVYAHLV 697
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQkvVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECdtpeNLLAQEDGVFASLV 253
|
.
gi 528078492 698 Q 698
Cdd:cd03288 254 R 254
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
468-683 |
3.26e-36 |
|
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: 136.47 E-value: 3.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*-KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQV 546
Cdd:COG1124 2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 547 VLVGQEPvlfSGS------VKDNIAYGLKDCEDAQVMAAVRAACAD-----DFIGEMPdgihteigekgSQLAVGQKQRL 615
Cdd:COG1124 82 QMVFQDP---YASlhprhtVDRILAEPLRIHGLPDREERIAELLEQvglppSFLDRYP-----------HQLSGGQRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528078492 616 AIARALVRNPRVLILDEATSALD--SQCE--QALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH 683
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDvsVQAEilNLLKDLREERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEE 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
468-675 |
4.49e-36 |
|
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: 135.29 E-value: 4.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSR-P*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQydhhyLHRQV 546
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 547 VLVGQEPVLFS-GSVKDNIAYGLK--DCEDAQVMAAVRAACA----DDFIGEMPdgihteigekgSQLAVGQKQRLAIAR 619
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElqGVPKAEARERAEELLElvglSGFENAYP-----------HQLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 620 ALVRNPRVLILDEATSALDSQCEQALQA-----WRSKGdRTVLVIAHRLH-TVQNVDQVLVL 675
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEelldiWRETG-KTVLLVTHDIDeAVFLADRVVVL 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
469-679 |
8.20e-36 |
|
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: 132.37 E-value: 8.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVL 548
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 549 VGQepvlFSGsvkdniayglkdcedaqvmaavraacaddfigempdgihteigekgsqlavGQKQRLAIARALVRNPRVL 628
Cdd:cd00267 78 VPQ----LSG---------------------------------------------------GQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 629 ILDEATSALDS----QCEQALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQ 679
Cdd:cd00267 103 LLDEPTSGLDPasreRLLELLRELAEEG-RTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
468-680 |
1.71e-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: 132.14 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQyDHHYLHRQVV 547
Cdd:cd03230 1 IEVRNLSKRYGK---KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSG-SVKDNIAYglkdcedaqvmaavraacaddfigempdgihteigekgSQlavGQKQRLAIARALVRNPR 626
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL--------------------------------------SG---GMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 627 VLILDEATSALD----SQCEQALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQL 680
Cdd:cd03230 116 LLILDEPTSGLDpesrREFWELLRELKKEG-KTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
468-688 |
2.06e-35 |
|
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: 140.81 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTG---GQLLLDGQPLVQYDHHYLHR 544
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVGQEP--VLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIgempdGIHTEIGEKGSQLAVGQKQRLAIARALV 622
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAV-----GLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528078492 623 RNPRVLILDEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTV-QNVDQVLVLKQGQLVEHSQLRE 688
Cdd:COG1123 159 LDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEE 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
468-681 |
3.40e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 134.35 E-value: 3.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEP-VLFSGS-VKDNIAYGLKD-CEDAQVMaavraacaDDFIGEMPDGIHTE-IGEKGSQ-LAVGQKQRLAIARALV 622
Cdd:PRK13632 87 IIFQNPdNQFIGAtVEDDIAFGLENkKVPPKKM--------KDIIDDLAKKVGMEdYLDKEPQnLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528078492 623 RNPRVLILDEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLV 681
Cdd:PRK13632 159 LNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
468-682 |
6.33e-35 |
|
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: 130.51 E-value: 6.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHyLHRQVV 547
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSGSVKDNIayglkdcedaqvmaavraacaddfigempdgihteigekGSQLAVGQKQRLAIARALVRNPRV 627
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 628 LILDEATSALDSQCEQAL--QAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVE 682
Cdd:cd03247 120 VLLDEPTVGLDPITERQLlsLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
468-684 |
1.72e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.75 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKST-VAAPLqNLYQPTGGQLLLDGQPLVQYDHH--YLHR 544
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTlLKAIL-GLLPPTSGTVRLFGKPPRRARRRigYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVGQEPVlfsgSVKDNIAYGL----------KDCEDAQVMAAVRAACADDFIgempdgiHTEIGEkgsqLAVGQKQR 614
Cdd:COG1121 83 RAEVDWDFPI----TVRDVVLMGRygrrglfrrpSRADREAVDEALERVGLEDLA-------DRPIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 615 LAIARALVRNPRVLILDEATSALDSQCEQA----LQAWRSKGdRTVLVIAHRLHTV-QNVDQVLVLKQGQLVEHS 684
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEAlyelLRELRREG-KTILVVTHDLGAVrEYFDRVLLLNRGLVAHGP 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
468-688 |
2.14e-34 |
|
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: 131.16 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*K-PVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYL---H 543
Cdd:cd03258 2 IELKNVSKVFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 544 RQVVLVGQEPVLFSG-SVKDNIAYGLkdcEDAQVMAAVRAACADD---FIGempdgihteIGEKG----SQLAVGQKQRL 615
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPL---EIAGVPKAEIEERVLElleLVG---------LEDKAdaypAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 616 AIARALVRNPRVLILDEATSALDSQCEQA----LQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLRE 688
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSilalLRDINRELGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEE 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
469-681 |
3.36e-34 |
|
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: 128.71 E-value: 3.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVL 548
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 549 VgqepvlfsgsvkdniayglkdcedAQVMAAVRAAC-ADDFIGEMPDgihteigekgsqlavGQKQRLAIARALVRNPRV 627
Cdd:cd03214 78 V------------------------PQALELLGLAHlADRPFNELSG---------------GERQRVLLARALAQEPPI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 628 LILDEATSALD--SQCE--QALQAWRSKGDRTVLVIAHRL-HTVQNVDQVLVLKQGQLV 681
Cdd:cd03214 119 LLLDEPTSHLDiaHQIEllELLRRLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
468-681 |
3.39e-34 |
|
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: 127.93 E-value: 3.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPlvqydhhylhrqvv 547
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 lvgqepVLFSgSVKDNIAYGLkdcedaqvmaavraacaddfigEMpdgIHteigekgsQLAVGQKQRLAIARALVRNPRV 627
Cdd:cd03216 64 ------VSFA-SPRDARRAGI----------------------AM---VY--------QLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 628 LILDEATSALDSQCEQAL----QAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:cd03216 104 LILDEPTAALTPAEVERLfkviRRLRAQG-VAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
468-688 |
5.19e-34 |
|
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: 131.01 E-value: 5.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 -LVGQEP--VLFSGSVKDNIAYGLkdcEDAQV----MAAvRAACADDFIGeMPDGIHTEigekGSQLAVGQKQRLAIARA 620
Cdd:TIGR04520 80 gMVFQNPdnQFVGATVEDDVAFGL---ENLGVpreeMRK-RVDEALKLVG-MEDFRDRE----PHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 621 LVRNPRVLILDEATSALDSQCE----QALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEHSQLRE 688
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRkevlETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPRE 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
462-703 |
8.26e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 130.21 E-value: 8.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 462 SRLEGRVEFQDVTFSYPSRP-*KPVLKGLTFTLHPGKVTALVGPNGSGKST----VAaplqNLYQPTGGQLLLDGQPLVQ 536
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTllrlIA----GLEKPTSGEVLVDGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 537 ydhhyLHRQVVLVGQEPVLF---SgsVKDNIAYGLkdcEDAQVMAAVRAACADDFIGEMpdgihteiGEKG------SQL 607
Cdd:COG1116 78 -----PGPDRGVVFQEPALLpwlT--VLDNVALGL---ELRGVPKAERRERARELLELV--------GLAGfedaypHQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 608 AVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQA-----WRSKGdRTVLVIAHrlhtvqNV-------DQVLVL 675
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDellrlWQETG-KTVLFVTH------DVdeavflaDRVVVL 212
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 528078492 676 KQ--GQLVE----------HSQLREDQDvYAHLVQQRLEA 703
Cdd:COG1116 213 SArpGRIVEeidvdlprprDRELRTSPE-FAALRAEILDL 251
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
469-678 |
1.40e-33 |
|
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: 128.03 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQydhhyLHRQVVL 548
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 549 VGQEPVL---FSGSVKDNIAYGL------------KDCEDA-QVMAAVraacaddfigEMPDGIHTEIGEkgsqLAVGQK 612
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLyghkglfrrlskADKAKVdEALERV----------GLSELADRQIGE----LSGGQQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528078492 613 QRLAIARALVRNPRVLILDEATSALDSQCEQA----LQAWRSKGdRTVLVIAHRLHTVQN-VDQVLVLKQG 678
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDiyelLRELRREG-MTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
468-685 |
9.02e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 126.31 E-value: 9.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*K-PVLKGLTFTLHPGKVTALVGPNGSGKSTvaapLQN----LYQPTGGQLLLDGQPLVQYDHHYL 542
Cdd:COG1136 5 LELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKST----LLNilggLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 543 ----HRQVVLVGQEPVLFSG-SVKDNIAYGLkdcEDAQVMAAVRAACADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAI 617
Cdd:COG1136 81 arlrRRHIGFVFQFFNLLPElTALENVALPL---LLAGVSRKERRERARELLERV--GLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 618 ARALVRNPRVLILDEATSALDSQ-CEQ---ALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEHSQ 685
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKtGEEvleLLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
468-682 |
2.19e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 126.67 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:PRK13635 6 IRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEP-VLFSGS-VKDNIAYGLKDC----EDAQ--VMAAVRAACADDFIGEMPdgihteigekgSQLAVGQKQRLAIAR 619
Cdd:PRK13635 85 MVFQNPdNQFVGAtVQDDVAFGLENIgvprEEMVerVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 620 ALVRNPRVLILDEATSALDSQCEQ----ALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVE 682
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRRevleTVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
152-443 |
2.55e-32 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 126.77 E-value: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 152 LMVAFFFLAWAVLGETLIPHYSGRVIDILGSDFDP*sfaSAIFFMCLFSVGSSLsagCRG-GSFL--FTMSRINLRI--- 225
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDL----EALLLVPLAIIGLFL---LRGlASYLqtYLMAYVGQRVvrd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 226 -RERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTI 304
Cdd:cd18552 74 lRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 305 AAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMA 384
Cdd:cd18552 154 LPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 385 LGMQVLILNCGVQQILAGEVTRGGLLSF-----LLYQEevgdyVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18552 234 AIAIALVLWYGGYQVISGELTPGEFISFitallLLYQP-----IKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
468-683 |
3.03e-32 |
|
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: 124.17 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHylHRQVV 547
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSG-SVKDNIAYGLKDcedAQVMAAVRAACADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPR 626
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKL---RGVPKAEIRARVRELLELV--GLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 627 VLILDEATSALDSQCEQALQA-----WRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEH 683
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREelkelQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
468-679 |
7.77e-32 |
|
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: 121.91 E-value: 7.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPsrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYL-HRQV 546
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPpLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 547 V-LVGQEPVLFSG-SVKDNIAYGLKDcedaqvmaavraacaddfigempdgihteigekgsqlavGQKQRLAIARALVRN 624
Cdd:cd03229 78 IgMVFQDFALFPHlTVLENIALGLSG---------------------------------------GQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528078492 625 PRVLILDEATSALDSQCEQALQA-----WRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQ 679
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRAllkslQAQLG-ITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
468-680 |
1.19e-31 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 122.60 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*K-PVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDH----HYL 542
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 543 HRQVVLVGQEPVLFSG-SVKDNIAYGLkdcEDAQVMAAVRAACADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARAL 621
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPL---LLAGVPKKERRERAEELLERV--GLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528078492 622 VRNPRVLILDEATSALDSQCEQA----LQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQL 680
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEvmelLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
467-677 |
5.60e-31 |
|
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: 120.28 E-value: 5.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 467 RVEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVaapLQ---NLYQPTGGQLLLDGQPLVQYDHHYlH 543
Cdd:COG4133 2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTL---LRilaGLLPPSAGEVLWNGEPIRDAREDY-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 544 RQVVLVGQEPVLFSG-SVKDNIA-----YGLkDCEDAQVMAAVRAAcaddfigempdGIHTEIGEKGSQLAVGQKQRLAI 617
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 618 ARALVRNPRVLILDEATSALDSQ----CEQALQAWRSKGdRTVLVIAHRLHTVQNvDQVLVLKQ 677
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAgvalLAELIAAHLARG-GAVLLTTHQPLELAA-ARVLDLGD 204
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
472-681 |
9.89e-31 |
|
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: 119.67 E-value: 9.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 472 DVTFSYpsRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDhhyLHRQVVLVGQ 551
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 552 EP--VLFSGSVKDNIAYGLKDCED--AQVMAAVRAACADDFIGEMPdgiHTeigekgsqLAVGQKQRLAIARALVRNPRV 627
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAgnEQAETVLKDLDLYALKERHP---LS--------LSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 628 LILDEATSALDSQCEQALQAW---RSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELireLAAQGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
152-415 |
1.20e-30 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 122.15 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 152 LMVAFFFLAWAVLGETLIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRGGSFLFTMSRINLRIRERLFS 231
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 232 SLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYN 311
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 312 PRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQVLI 391
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260
....*....|....*....|....
gi 528078492 392 LNCGVQQILAGEVTRGGLLSFLLY 415
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISY 264
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
468-688 |
2.27e-30 |
|
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: 119.53 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQP---LVQYDHHYLHR 544
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVGQEPVLFSG-SVKDNIAYGL----KDCE---DAQVMAAVRAACADDFIGEMPdgihteigekgSQLAVGQKQRLA 616
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLrehtRLSEeeiREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 617 IARALVRNPRVLILDEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLRE 688
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEE 223
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
174-411 |
2.58e-30 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 121.43 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 174 GRVIDILGS----DFDP*SFASAIFFMCLFSVGssLSAGCRGGSFLFTMS------RINLRIRERLFSSLLRQDLGFFQE 243
Cdd:cd18577 23 GDLFDAFTDfgsgESSPDEFLDDVNKYALYFVY--LGIGSFVLSYIQTACwtitgeRQARRIRKRYLKALLRQDIAWFDK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 244 NKTGELNSRLSSDTSK----MSRWLPynanILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLT 319
Cdd:cd18577 101 NGAGELTSRLTSDTNLiqdgIGEKLG----LLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 320 EIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQVLILNCGVQQI 399
Cdd:cd18577 177 KEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLV 256
|
250
....*....|..
gi 528078492 400 LAGEVTRGGLLS 411
Cdd:cd18577 257 RDGEISPGDVLT 268
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
468-682 |
4.58e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.75 E-value: 4.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYD-HHYLHRQV 546
Cdd:COG1129 5 LEMRGISKSFGGVK---ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 547 VLVGQEPVLFSG-SVKDNIA-------YGLKDceDAQVMAAVRAACAddfigEMpdGIHTEIGEKGSQLAVGQKQRLAIA 618
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFlgreprrGGLID--WRAMRRRARELLA-----RL--GLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 619 RALVRNPRVLILDEATSALDSQcE-----QALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVE 682
Cdd:COG1129 153 RALSRDARVLILDEPTASLTER-EverlfRIIRRLKAQG-VAIIYISHRLDEVFEIaDRVTVLRDGRLVG 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
468-688 |
6.30e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.45 E-value: 6.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEP-VLFSG-SVKDNIAYGLKDCEDAQVMAAVRAACADDFIGeMPDGIHTEigekGSQLAVGQKQRLAIARALVRNP 625
Cdd:PRK13650 85 MVFQNPdNQFVGaTVEDDVAFGLENKGIPHEEMKERVNEALELVG-MQDFKERE----PARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 626 RVLILDEATSALDSQCEQAL----QAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEHSQLRE 688
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELiktiKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRE 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
468-685 |
7.78e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 117.46 E-value: 7.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPsrP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVaapLQNLY---QPTGGQLLLDGQPLVQYDHH---Y 541
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTL---LKLLYgeeRPTSGQVLVNGQDLSRLKRReipY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 542 LHRQVVLVGQE-PVLFSGSVKDNIAYGLK--DCEDAQVMAAVRAACA----DDFIGEMPDgihteigekgsQLAVGQKQR 614
Cdd:COG2884 77 LRRRIGVVFQDfRLLPDRTVYENVALPLRvtGKSRKEIRRRVREVLDlvglSDKAKALPH-----------ELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 615 LAIARALVRNPRVLILDEATSALDSqcEQALQAWR------SKGdRTVLVIAHRLHTVQNVDQ-VLVLKQGQLVEHSQ 685
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDP--ETSWEIMElleeinRRG-TTVLIATHDLELVDRMPKrVLELEDGRLVRDEA 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
468-683 |
9.78e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 120.57 E-value: 9.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*K-PVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLH--- 543
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 544 RQVVLVGQEPVLFSG-SVKDNIAYGLkdcEDAQVMAAVRAACAD---DFIGempdgihteIGEKG----SQLAVGQKQRL 615
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENVALPL---EIAGVPKAEIRKRVAellELVG---------LSDKAdaypSQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528078492 616 AIARALVRNPRVLILDEATSALDSQCEQA----LQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH 683
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSildlLKDINRELGLTIVLITHEMDVVRRIcDRVAVLENGRIVEQ 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
468-691 |
1.38e-29 |
|
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: 117.39 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVaapLQN---LYQPTGGQLLLDGQPLVQYDHHYLHR 544
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVL---LKLiigLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVG---QEPVLFSG-SVKDNIAYGLK---DCEDAQVMAAVRAACA----DDFIGEMPdgihteigekgSQLAVGQKQ 613
Cdd:COG1127 80 LRRRIGmlfQGGALFDSlTVFENVAFPLRehtDLSEAEIRELVLEKLElvglPGAADKMP-----------SELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 614 RLAIARALVRNPRVLILDEATSALD-----------SQCEQALQAwrskgdrTVLVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDpitsavideliRELRDELGL-------TSVVVTHDLDSAFAIaDRVAVLADGKII 221
|
250
....*....|...
gi 528078492 682 EH---SQLREDQD 691
Cdd:COG1127 222 AEgtpEELLASDD 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
468-646 |
1.73e-29 |
|
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: 116.95 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHylHRQVV 547
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSG-SVKDNIAYGL------KDCEDAQVMAAVRAACADDFIGEMPDgihteigekgsQLAVGQKQRLAIARA 620
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGLrlkklpKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARA 144
|
170 180
....*....|....*....|....*.
gi 528078492 621 LVRNPRVLILDEATSALDSQCEQALQ 646
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQ 170
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
142-405 |
6.35e-29 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 117.55 E-value: 6.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 142 LRLSRPDLPFLMVAFFFlawAVLGETLIPHYS---GRVIDILGSDFDP*SFASAIFFMCLF---SVGSSLSAGCRGGSFL 215
Cdd:cd18578 1 LKLNKPEWPLLLLGLIG---AIIAGAVFPVFAilfSKLISVFSLPDDDELRSEANFWALMFlvlAIVAGIAYFLQGYLFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 216 FTMSRINLRIRERLFSSLLRQDLGFF--QENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLT 293
Cdd:cd18578 78 IAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 294 FLSLLDLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLER 373
Cdd:cd18578 158 LVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALIS 237
|
250 260 270
....*....|....*....|....*....|..
gi 528078492 374 ALYLAIRRVMALGMQVLILNCGVQQILAGEVT 405
Cdd:cd18578 238 GLGFGLSQSLTFFAYALAFWYGGRLVANGEYT 269
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
468-688 |
1.34e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.05 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQP---TGGQLLLDGQPLVQYDHHYLHR 544
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVGQEP-VLFSG-SVKDNIAYGLkdcEDAQV-----MAAVRAACADdfIGeMPDGIHTEigekGSQLAVGQKQRLAI 617
Cdd:PRK13640 85 KVGIVFQNPdNQFVGaTVGDDVAFGL---ENRAVprpemIKIVRDVLAD--VG-MLDYIDSE----PANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 618 ARALVRNPRVLILDEATSALD-SQCEQALQAWR---SKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEHSQLRE 688
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDpAGKEQILKLIRklkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
426-688 |
2.10e-28 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 122.58 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 426 LVYMYGDMLSNVGAAEKVFCYIDRKPN--LPQ----------------------------PGTLAPSRLE-GRVEFQDVT 474
Cdd:PTZ00243 1236 LVRQVATVEADMNSVERLLYYTDEVPHedMPEldeevdalerrtgmaadvtgtvviepasPTSAAPHPVQaGSLVFEGVQ 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 475 FSYpsRP*KP-VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEP 553
Cdd:PTZ00243 1316 MRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDP 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 554 VLFSGSVKDNIAYGLkDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLIL-DE 632
Cdd:PTZ00243 1394 VLFDGTVRQNVDPFL-EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDE 1472
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 633 ATSALDSQCEQALQA--WRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEHSQLRE 688
Cdd:PTZ00243 1473 ATANIDPALDRQIQAtvMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRE 1530
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
468-638 |
3.91e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 116.35 E-value: 3.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKST----VAaplqNLYQPTGGQLLLDGQPLvqydhHYL- 542
Cdd:COG3842 6 LELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTllrmIA----GFETPDSGRILLDGRDV-----TGLp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 543 --HRQVVLVGQEPVLFSG-SVKDNIAYGLKdcedaqvMAAVRAACADDFIGEMPDgiHTEIGEKG----SQLAVGQKQRL 615
Cdd:COG3842 74 peKRNVGMVFQDYALFPHlTVAENVAFGLR-------MRGVPKAEIRARVAELLE--LVGLEGLAdrypHQLSGGQQQRV 144
|
170 180
....*....|....*....|...
gi 528078492 616 AIARALVRNPRVLILDEATSALD 638
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALD 167
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
458-683 |
4.03e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.59 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 458 TLAPSRLEGRVEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVaapLQNL--------YQPTGGQLLL 529
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGD---KQALKDINLDIPENKVTALIGPSGCGKSTL---LRCLnrmndlipGARVEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 530 DGQPLvqYDHHY----LHRQVVLVGQEPVLFSGSVKDNIAYGLKDCE-------DAQVMAAVR-AACADdfigEMPDGIH 597
Cdd:COG1117 76 DGEDI--YDPDVdvveLRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGikskselDEIVEESLRkAALWD----EVKDRLK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 598 teigEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALD----SQCEQALQawRSKGDRTVLVIAHRLHTVQNV-DQV 672
Cdd:COG1117 150 ----KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELIL--ELKKDYTIVIVTHNMQQAARVsDYT 223
|
250
....*....|.
gi 528078492 673 LVLKQGQLVEH 683
Cdd:COG1117 224 AFFYLGELVEF 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
468-682 |
5.42e-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: 111.93 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPlVQYDHHYLHRQVV 547
Cdd:cd03268 1 LKTNDLTKTYGK---KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-YQKNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVgQEPVLFSG-SVKDNI-----AYGLKDCEDAQVMAAVraacaddfigempdGIHTEIGEKGSQLAVGQKQRLAIARAL 621
Cdd:cd03268 77 LI-EAPGFYPNlTARENLrllarLLGIRKKRIDEVLDVV--------------GLKDSAKKKVKGFSLGMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 622 VRNPRVLILDEATSALD----SQCEQALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVE 682
Cdd:cd03268 142 LGNPDLLILDEPTNGLDpdgiKELRELILSLRDQG-ITVLISSHLLSEIQKVaDRIGIINKGKLIE 206
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
485-692 |
6.96e-28 |
|
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: 112.53 E-value: 6.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHylhrQVVLVG-----QEPVLFSG- 558
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH----EIARLGigrtfQIPRLFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 SVKDNIA--------YGLKDCEDAQVMAAVRAACAD--DFIGeMPDGIHTEIGEkgsqLAVGQKQRLAIARALVRNPRVL 628
Cdd:cd03219 91 TVLENVMvaaqartgSGLLLARARREEREARERAEEllERVG-LADLADRPAGE----LSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 629 ILDEATSALDSQCEQAL----QAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH---SQLREDQDV 692
Cdd:cd03219 166 LLDEPAAGLNPEETEELaeliRELRERG-ITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEgtpDEVRNNPRV 236
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
468-682 |
3.12e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.38 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*KpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPV-LFSGS-VKDNIAYGLKDcedaqvmaavRAACADDFIGEMPDGIhTEIG------EKGSQLAVGQKQRLAIAR 619
Cdd:PRK13648 87 IVFQNPDnQFVGSiVKYDVAFGLEN----------HAVPYDEMHRRVSEAL-KQVDmleradYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 620 ALVRNPRVLILDEATSALDSQCEQAL----QAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVE 682
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLldlvRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYK 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
462-682 |
5.16e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 110.90 E-value: 5.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 462 SRLEGRVEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTG-----GQLLLDGQPLVQ 536
Cdd:PRK14258 2 SKLIPAIKVNNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 537 --YDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLK------DCE-DAQVMAAVRAAcaddfigEMPDGIHTEIGEKGSQL 607
Cdd:PRK14258 79 rrVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpKLEiDDIVESALKDA-------DLWDEIKHKIHKSALDL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 608 AVGQKQRLAIARALVRNPRVLILDEATSALDS----QCEQALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVL------KQ 677
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFfkgnenRI 231
|
....*
gi 528078492 678 GQLVE 682
Cdd:PRK14258 232 GQLVE 236
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
468-695 |
5.28e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 112.93 E-value: 5.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKST----VAAplqnLYQPTGGQLLLDGQpLVQYDHHYLH 543
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTllriIAG----LETPDSGRIVLNGR-DLFTNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 544 RQVVLVGQEPVLFSG-SVKDNIAYGLKdceDAQVMAAVRAACADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALV 622
Cdd:COG1118 75 RRVGFVFQHYALFPHmTVAENIAFGLR---VRPPSKAEIRARVEELLELV--QLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 623 RNPRVLILDEATSALDSQCEQALQAWrskgdrtvLViahRLHTVQNV----------------DQVLVLKQGQLVehsQL 686
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRW--------LR---RLHDELGGttvfvthdqeealelaDRVVVMNQGRIE---QV 215
|
....*....
gi 528078492 687 REDQDVYAH 695
Cdd:COG1118 216 GTPDEVYDR 224
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
152-415 |
6.82e-27 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 111.35 E-value: 6.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 152 LMVAFFFLAWAVLGETLIPHYSGRVIDILGS-DFDP*SFASAIFFMCLFSVgssLSAGCRGGS--FLFTMSR-INLRIRE 227
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAgTLTASQLLRYALLILLLAL---LIGIFRFLWryLIFGASRrIEYDLRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 228 RLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAE 307
Cdd:cd18541 78 DLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 308 KVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALercrqlwwRRDLERALYLAirRVMAL-- 385
Cdd:cd18541 158 YRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLN--------EEYVEKNLRLA--RVDALff 227
|
250 260 270
....*....|....*....|....*....|....*...
gi 528078492 386 -------GM-QVLILNCGVQQILAGEVTRGGLLSFLLY 415
Cdd:cd18541 228 pliglliGLsFLIVLWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
467-688 |
1.05e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.35 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 467 RVEFQDVTFSYPSrp*kpV--LKGLTFTLHPGKVTALVGPNGSGKSTvaapLQN----LYQPTGGQLLLDGQPLVQYD-H 539
Cdd:COG3845 5 ALELRGITKRFGG-----VvaNDDVSLTVRPGEIHALLGENGAGKST----LMKilygLYQPDSGEILIDGKPVRIRSpR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 540 HYLHRQVVLVGQEPVLFSG-SVKDNIAYGLKDCEDAQV-MAAVRA---ACADDFigempdGIHTEIGEKGSQLAVGQKQR 614
Cdd:COG3845 76 DAIALGIGMVHQHFMLVPNlTVAENIVLGLEPTKGGRLdRKAARArirELSERY------GLDVDPDAKVEDLSVGEQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 615 LAIARALVRNPRVLILDEATSALDSQcE-----QALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLRE 688
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLTPQ-EadelfEILRRLAAEG-KSIIFITHKLREVMAIaDRVTVLRRGKVVGTVDTAE 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
484-689 |
1.97e-26 |
|
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: 107.91 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 484 PVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHY-LHRQVVLVGQEPVLFSG-SVK 561
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 562 DNI---AYGLKDCEDAQVMAAVRAAcaddF--IGEMPDgihteigEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSA 636
Cdd:cd03224 94 ENLllgAYARRRAKRKARLERVYEL----FprLKERRK-------QLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528078492 637 LD----SQCEQALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH---SQLRED 689
Cdd:cd03224 163 LApkivEEIFEAIRELRDEG-VTILLVEQNARFALEIaDRAYVLERGRVVLEgtaAELLAD 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
468-683 |
1.99e-26 |
|
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: 107.66 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGkVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQyDHHYLHRQVV 547
Cdd:cd03264 1 LQLENLTKRYGK---KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSG-SVKDNIAY--GLKDCEDAQVMAAVRAACADDfigempdGIHTEIGEKGSQLAVGQKQRLAIARALVRN 624
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiaWLKGIPSKEVKARVDEVLELV-------NLGDRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 625 PRVLILDEATSALDSqcEQALqAWRS-----KGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH 683
Cdd:cd03264 149 PSILIVDEPTAGLDP--EERI-RFRNllselGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFE 210
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
159-414 |
2.72e-26 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 109.56 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 159 LAWAVLGeTLIPHYSGRVIDIL-------GSDFDP*SFASAIFFMCLFSVGSSLSAGCRggSFLFTMS-RINLRIRERLF 230
Cdd:cd18574 6 LAAALVN-IQIPLLLGDLVNVIsrslketNGDFIEDLKKPALKLLGLYLLQSLLTFAYI--SLLSVVGeRVAARLRNDLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 231 SSLLRQDLGFFQENKTGELNSRLSSD------TSKMSrwlpynANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTI 304
Cdd:cd18574 83 SSLLRQDIAFFDTHRTGELVNRLTADvqefksSFKQC------VSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 305 AAEKVY-----NPRHQAvlteiQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAI 379
Cdd:cd18574 157 LVGTLYgsflrKLSRRA-----QAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGL 231
|
250 260 270
....*....|....*....|....*....|....*
gi 528078492 380 RRVMALGMQVLILNCGVQQILAGEVTRGGLLSFLL 414
Cdd:cd18574 232 SNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
495-681 |
4.27e-26 |
|
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: 106.61 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 495 PGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLV----QYDHHYLHRQVVLVGQEPVLFSG-SVKDNIAYGLK 569
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdsrkKINLPPQQRKIGLVFQQYALFPHlNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 570 DCEDAqvmaaVRAACADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALD----SQCEQAL 645
Cdd:cd03297 102 RKRNR-----EDRISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDralrLQLLPEL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 528078492 646 QAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:cd03297 175 KQIKKNLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQ 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
484-681 |
4.53e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 112.84 E-value: 4.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 484 PVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHR-QVVLVGQEPVLFSG-SVK 561
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 562 DNIAYGL-KDCEDAQVMAAVRAACaddfigempdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALD-- 638
Cdd:PRK15439 105 ENILFGLpKRQASMQKMKQLLAAL----------GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpa 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 528078492 639 --SQCEQALQAWRSKGDRTVLvIAHRLHTV-QNVDQVLVLKQGQLV 681
Cdd:PRK15439 175 etERLFSRIRELLAQGVGIVF-ISHKLPEIrQLADRISVMRDGTIA 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
468-695 |
8.10e-26 |
|
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: 106.65 E-value: 8.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*kpvLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQydHHYLHRQVV 547
Cdd:cd03296 3 IEVRNVSKRFGDFVA---LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD--VPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSG-SVKDNIAYGL----------KDCEDAQVMAAVRAACADDFIGEMPdgihteigekgSQLAVGQKQRLA 616
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLrvkprserppEAEIRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 617 IARALVRNPRVLILDEATSALDSQCEQALQAW-RSKGDR----TVLVIAHRLHTVQNVDQVLVLKQGQlVEhsQLREDQD 691
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWlRRLHDElhvtTVFVTHDQEEALEVADRVVVMNKGR-IE--QVGTPDE 223
|
....
gi 528078492 692 VYAH 695
Cdd:cd03296 224 VYDH 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
468-695 |
8.47e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 108.67 E-value: 8.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYP------SRP*KPV--LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDH 539
Cdd:COG4608 8 LEVRDLKKHFPvrgglfGRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 540 HYL---HRQVVLVGQEPvlfSGS------VKDNIAYGLK--------DCED--AQVMAAV--RAACADDFigemPdgiHt 598
Cdd:COG4608 88 RELrplRRRMQMVFQDP---YASlnprmtVGDIIAEPLRihglaskaERRErvAELLELVglRPEHADRY----P---H- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 599 eigekgsQLAVGQKQRLAIARALVRNPRVLILDEATSALD-SQceQA--------LQAwrsKGDRTVLVIAHRLHTVQNV 669
Cdd:COG4608 157 -------EFSGGQRQRIGIARALALNPKLIVCDEPVSALDvSI--QAqvlnlledLQD---ELGLTYLFISHDLSVVRHI 224
|
250 260
....*....|....*....|....*..
gi 528078492 670 -DQVLVLKQGQLVEHSqlrEDQDVYAH 695
Cdd:COG4608 225 sDRVAVMYLGKIVEIA---PRDELYAR 248
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
152-415 |
8.86e-26 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 107.90 E-value: 8.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 152 LMVAFFFLAWAVLGETLIPHYSGRVIDILGSDfdp*SFASAIFFMCLFSVGSSLSAGcrGGSFLFTMS--RINLRIRERL 229
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAG---GSSGGLLALLVALFLLQAVLSA--LSSYLLGRTgeRVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 230 FSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKV 309
Cdd:cd18551 76 WRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 310 YNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCrqlwWRRDLERALYLA-IRRVMALGMQ 388
Cdd:cd18551 156 LGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERL----YRAGLKAAKIEAlIGPLMGLAVQ 231
|
250 260 270
....*....|....*....|....*....|
gi 528078492 389 ---VLILNCGVQQILAGEVTRGGLLSFLLY 415
Cdd:cd18551 232 lalLVVLGVGGARVASGALTVGTLVAFLLY 261
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
460-683 |
1.11e-25 |
|
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: 111.70 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 460 APSRLEGRvefqDVTFSYP------SRP*KPV--LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLyQPTGGQLLLDG 531
Cdd:COG4172 272 APPLLEAR----DLKVWFPikrglfRRTVGHVkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 532 QPLVQYDHHYL-----HRQVVLvgQEPvlFSG-----SVKDNIAYGLK----DCEDAQVMAAVRAACADdfIGEMPDGIH 597
Cdd:COG4172 347 QDLDGLSRRALrplrrRMQVVF--QDP--FGSlsprmTVGQIIAEGLRvhgpGLSAAERRARVAEALEE--VGLDPAARH 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 598 TEIGEkgsqLAVGQKQRLAIARALVRNPRVLILDEATSALDS--QCE-----QALQAwrsKGDRTVLVIAHRLHTVQNV- 669
Cdd:COG4172 421 RYPHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVsvQAQildllRDLQR---EHGLAYLFISHDLAVVRALa 493
|
250
....*....|....
gi 528078492 670 DQVLVLKQGQLVEH 683
Cdd:COG4172 494 HRVMVMKDGKVVEQ 507
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
485-692 |
1.37e-25 |
|
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: 106.28 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTvaapLQNL----YQPTGGQLLLDGQPLVQYDHHylhrQVVLVG-----QEPVL 555
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTT----LFNLitgfYRPTSGRILFDGRDITGLPPH----RIARLGiartfQNPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 556 FSG-SVKDNIA--------YGLKDC---------EDAQVMAAVRAACadDFIgempdGIHTEIGEKGSQLAVGQKQRLAI 617
Cdd:COG0411 91 FPElTVLENVLvaaharlgRGLLAAllrlprarrEEREARERAEELL--ERV-----GLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 618 ARALVRNPRVLILDEATSALDSQcE-----QALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH---SQLRE 688
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPE-EteelaELIRRLRDERGITILLIEHDMDLVMGLaDRIVVLDFGRVIAEgtpAEVRA 242
|
....
gi 528078492 689 DQDV 692
Cdd:COG0411 243 DPRV 246
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
474-681 |
2.41e-25 |
|
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: 104.76 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 474 TFSYPSRP*KpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEP 553
Cdd:cd03266 10 RFRDVKKTVQ-AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 554 VLFSGSVKDNIAY--GLKDCEDAQVMAAVraacaDDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILD 631
Cdd:cd03266 89 LYDRLTARENLEYfaGLYGLKGDELTARL-----EELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 632 EATSALDSQCEQAL----QAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:cd03266 162 EPTTGLDVMATRALrefiRQLRALG-KCILFSTHIMQEVERLcDRVVVLHRGRVV 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
468-638 |
3.05e-25 |
|
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: 104.15 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQ--YDHHYLHRQ 545
Cdd:cd03262 1 IEIKNLHKSFGD---FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 546 VVLVGQEPVLFSG-SVKDNIAYGL-------KDCEDAQVMAAVRAACADDFIGEMPdgihteigekgSQLAVGQKQRLAI 617
Cdd:cd03262 78 VGMVFQQFNLFPHlTVLENITLAPikvkgmsKAEAEERALELLEKVGLADKADAYP-----------AQLSGGQQQRVAI 146
|
170 180
....*....|....*....|.
gi 528078492 618 ARALVRNPRVLILDEATSALD 638
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALD 167
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
468-646 |
3.58e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 108.11 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHylHRQVV 547
Cdd:PRK09452 15 VELRGISKSFDG---KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSG-SVKDNIAYGLKdCE-------DAQVMAAVRAACADDFIGEMPdgihteigekgSQLAVGQKQRLAIAR 619
Cdd:PRK09452 90 TVFQSYALFPHmTVFENVAFGLR-MQktpaaeiTPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIAR 157
|
170 180
....*....|....*....|....*..
gi 528078492 620 ALVRNPRVLILDEATSALDSQCEQALQ 646
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQ 184
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
466-638 |
4.25e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 107.08 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 466 GRVEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKST----VAAplqnLYQPTGGQLLLDGQpLVQyDHHY 541
Cdd:COG3839 2 ASLELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTllrmIAG----LEDPTSGEILIGGR-DVT-DLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 542 LHRQVVLVGQEPVLF-SGSVKDNIAYGLK--DCEDAQVMAAVRAACA----DDFIGEMPdgihteigekgSQLAVGQKQR 614
Cdd:COG3839 73 KDRNIAMVFQSYALYpHMTVYENIAFPLKlrKVPKAEIDRRVREAAEllglEDLLDRKP-----------KQLSGGQRQR 141
|
170 180
....*....|....*....|....
gi 528078492 615 LAIARALVRNPRVLILDEATSALD 638
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLD 165
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
468-681 |
5.60e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.20 E-value: 5.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEP--VLFSGSVKDNIAYGLKDCE------DAQVMAAVRAACADDFIGEMPdgihteigekgSQLAVGQKQRLAIAR 619
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNMGldkdevERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 620 ALVRNPRVLILDEATSALDSQCEQALQA--WR-SKGDRTVLVIAHRLH-TVQNVDQVLVLKQGQLV 681
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEilDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVL 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
479-681 |
5.68e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.47 E-value: 5.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 479 SRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQV-VLVGQEPVLFS 557
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRaVLPQHSSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 558 GSVKDNIAYGLKD--CEDAQVMAAVRAACADdfigempdgihTEIGEKGS----QLAVGQKQRLAIARALVR------NP 625
Cdd:PRK13548 91 FTVEEVVAMGRAPhgLSRAEDDALVAAALAQ-----------VDLAHLAGrdypQLSGGEQQRVQLARVLAQlwepdgPP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528078492 626 RVLILDEATSALD-SQCEQALQAWRSKGDR---TVLVIAHRLH-TVQNVDQVLVLKQGQLV 681
Cdd:PRK13548 160 RWLLLDEPTSALDlAHQHHVLRLARQLAHErglAVIVVLHDLNlAARYADRIVLLHQGRLV 220
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
479-701 |
5.74e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 104.92 E-value: 5.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 479 SRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPvlfSG 558
Cdd:COG4167 22 RRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDP---NT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 SVKDNIAYG------LK---DCEDAQVMAAVRAACAddFIGEMPDgiHTEIGEKgsQLAVGQKQRLAIARALVRNPRVLI 629
Cdd:COG4167 99 SLNPRLNIGqileepLRlntDLTAEEREERIFATLR--LVGLLPE--HANFYPH--MLSSGQKQRVALARALILQPKIII 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 630 LDEATSALD----SQC-----EqaLQawRSKGDRTVLViAHRLHTVQNV-DQVLVLKQGQLVEHSQLREdqdVYA---HL 696
Cdd:COG4167 173 ADEALAALDmsvrSQIinlmlE--LQ--EKLGISYIYV-SQHLGIVKHIsDKVLVMHQGEVVEYGKTAE---VFAnpqHE 244
|
....*
gi 528078492 697 VQQRL 701
Cdd:COG4167 245 VTKRL 249
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
485-688 |
6.83e-25 |
|
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: 103.95 E-value: 6.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHylHRQVVLVGQEPVLFSG-SVKDN 563
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 564 IAYGLK--DCEDAQVMAAVRAacaddfIGEMPdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQC 641
Cdd:cd03299 92 IAYGLKkrKVDKKEIERKVLE------IAEML-GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 528078492 642 EQA----LQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLRE 688
Cdd:cd03299 165 KEKlreeLKKIRKEFGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEE 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
483-681 |
7.04e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 104.33 E-value: 7.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSG-SVK 561
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 562 DNIAYG----------LKDcEDAQVmaaVRAACADDFIGEMPDgihteigEKGSQLAVGQKQRLAIARALVRNPRVLILD 631
Cdd:PRK11231 95 ELVAYGrspwlslwgrLSA-EDNAR---VNQAMEQTRINHLAD-------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 632 EATSALD--SQCE--QALQAWRSKGdRTVLVIAHRLHTV-QNVDQVLVLKQGQLV 681
Cdd:PRK11231 164 EPTTYLDinHQVElmRLMRELNTQG-KTVVTVLHDLNQAsRYCDHLVVLANGHVM 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
483-699 |
7.48e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.02 E-value: 7.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYqPTGGQLLLDGQPLVQYDHHYL---HRQVVLVGQEPvlFSG- 558
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP--NSSl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 ----SVKDNIAYGL----KDCEDAQVMAAVRAACADdfIGEMPDGIHTEIGEkgsqLAVGQKQRLAIARALVRNPRVLIL 630
Cdd:PRK15134 376 nprlNVLQIIEEGLrvhqPTLSAAQREQQVIAVMEE--VGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 631 DEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLredQDVYAHLVQQ 699
Cdd:PRK15134 450 DEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHDLHVVRALcHQVIVLRQGEVVEQGDC---ERVFAAPQQE 520
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
468-683 |
7.66e-25 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 103.54 E-value: 7.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHH--YLHRQ 545
Cdd:COG1126 2 IEIENLHKSFGD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 546 VVLVGQEPVLFSG-SVKDNIAYGL-----KDCEDAQVMAA-----VRAAcadDFIGEMPdgihteigekgSQLAVGQKQR 614
Cdd:COG1126 79 VGMVFQQFNLFPHlTVLENVTLAPikvkkMSKAEAEERAMellerVGLA---DKADAYP-----------AQLSGGQQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 615 LAIARALVRNPRVLILDEATSALD----SQCEQALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH 683
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDpelvGEVLDVMRDLAKEG-MTMVVVTHEMGFAREVaDRVVFMDGGRIVEE 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
468-688 |
1.38e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.00 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLvQYDHHYL--HRQ 545
Cdd:PRK13639 2 LETRDLKYSYPDGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLleVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 546 VV-LVGQEP--VLFSGSVKDNIAYG------LKDCEDAQVMAAVRAACADDFIGEMPdgiHteigekgsQLAVGQKQRLA 616
Cdd:PRK13639 79 TVgIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPP---H--------HLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 617 IARALVRNPRVLILDEATSALD----SQCEQALQAWRSKGdRTVLVIAHRLHTVQ-NVDQVLVLKQGQLVEHSQLRE 688
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDpmgaSQIMKLLYDLNKEG-ITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKE 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
468-688 |
1.61e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPlVQYDHH---YLHR 544
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP-IDYSRKglmKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVGQEP--VLFSGSVKDNIAYG---LKDCEDaQVMAAVRAACADDFIGEMPDgihteigEKGSQLAVGQKQRLAIAR 619
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGavnLKLPED-EVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 620 ALVRNPRVLILDEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQ-NVDQVLVLKQGQLVEHSQLRE 688
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
480-682 |
1.97e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 103.23 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 480 RP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYD---HHYLHRQVVLVGQEP--- 553
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 554 VLFSGSVKDNIAYGLKDCEDaqVMAAVRAACADDFIGEMpdGIHTEIGEK-GSQLAVGQKQRLAIARALVRNPRVLILDE 632
Cdd:PRK10419 102 VNPRKTVREIIREPLRHLLS--LDKAERLARASEMLRAV--DLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 633 ATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNVDQ-VLVLKQGQLVE 682
Cdd:PRK10419 178 AVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQrVMVMDNGQIVE 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
468-682 |
2.60e-24 |
|
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: 104.36 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*K-PVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQP---TGGQLLLDGQPLVQYDH---- 539
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 540 HYLHRQVVLVGQE------PVLfsgSVKDNIAYGLK---DCEDAQVMAAVRAA-------CADDFIGEMPdgiHteigek 603
Cdd:COG0444 82 KIRGREIQMIFQDpmtslnPVM---TVGDQIAEPLRihgGLSKAEARERAIELlervglpDPERRLDRYP---H------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 604 gsQLAVGQKQRLAIARALVRNPRVLILDEATSALD-SqcEQA-----LQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLK 676
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALDvT--IQAqilnlLKDLQRELGLAILFITHDLGVVAEIaDRVAVMY 225
|
....*.
gi 528078492 677 QGQLVE 682
Cdd:COG0444 226 AGRIVE 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
468-682 |
3.56e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.50 E-value: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYP-SRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYL---H 543
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 544 RQVVLVGQEPVLFSG-SVKDNIAYGLKdcedaqvMAAVRAACADDFIGEMPDGIhtEIGEKG----SQLAVGQKQRLAIA 618
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALPLE-------LAGTPKAEIKARVTELLELV--GLSDKAdrypAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 619 RALVRNPRVLILDEATSALDSQCEQALQAWRSKGDR----TVLVIAHRLHTVQNV-DQVLVLKQGQLVE 682
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRelglTIVLITHEMDVVKRIcDRVAVIDAGRLVE 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
189-688 |
4.80e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 108.52 E-value: 4.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 189 FASAIFFmclfsvGSSLSAGCRGGSFLfTMSRINLRIRERLFSSLLRQDLGFFQEnktgelnSRLSSDTSKMSRWLPYNA 268
Cdd:PLN03232 343 YAFLIFF------GVTFGVLCESQYFQ-NVGRVGFRLRSTLVAAIFHKSLRLTHE-------ARKNFASGKVTNMITTDA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 269 NILLRSLVKVIGLYC--FMLQVSPRLTFLSL--------LDLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGG 338
Cdd:PLN03232 409 NALQQIAEQLHGLWSapFRIIVSMVLLYQQLgvaslfgsLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILAS 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 339 LQTVRSFGAEEQEVSRYKEAleRCRQLWWRRDLEraLYLAIRRVM--ALGMQVLILNCGVQQILAGEVTRG-GLLSFLLY 415
Cdd:PLN03232 489 MDTVKCYAWEKSFESRIQGI--RNEELSWFRKAQ--LLSAFNSFIlnSIPVVVTLVSFGVFVLLGGDLTPArAFTSLSLF 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 416 QeevgdYVRNLVYMYGDMLSNVGAA-------EKVFCYIDR--KPNLP-QPGTLAPSRLEGrvefqdvTFSYPSRP*KPV 485
Cdd:PLN03232 565 A-----VLRSPLNMLPNLLSQVVNAnvslqriEELLLSEERilAQNPPlQPGAPAISIKNG-------YFSWDSKTSKPT 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGK-STVAAPLQNLYQPTGGQLLLDGQplvqydhhylhrqVVLVGQEPVLFSGSVKDNI 564
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAETSSVVIRGS-------------VAYVPQVSWIFNATVRENI 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 565 AYGlKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCeqA 644
Cdd:PLN03232 700 LFG-SDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV--A 776
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 528078492 645 LQAWRS------KGDRTVLViAHRLHTVQNVDQVLVLKQGQLVEHSQLRE 688
Cdd:PLN03232 777 HQVFDScmkdelKGKTRVLV-TNQLHFLPLMDRIILVSEGMIKEEGTFAE 825
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
467-683 |
7.22e-24 |
|
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: 99.55 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 467 RVEFQDVTFSYPSRP*---KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPL--QNLYQPTGGQLLLDGQPLvqyDHHY 541
Cdd:cd03213 3 TLSFRNLTVTVKSSPSksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 542 LHRQVVLVGQEPVLFSG-SVKDNIAYglkdcedaqvmaavrAACAddfigempdgihteigekgSQLAVGQKQRLAIARA 620
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLMF---------------AAKL-------------------RGLSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 621 LVRNPRVLILDEATSALDS-QCEQALQAWR--SKGDRTVLVIAHRLHT--VQNVDQVLVLKQGQLVEH 683
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSsSALQVMSLLRrlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYF 193
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
468-680 |
1.55e-23 |
|
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: 99.40 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPsrP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHH---YLHR 544
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVGQEPVLFSG-SVKDNIAYGLKDCEDAQVMAAVRAACADDFIGempdgIHTEIGEKGSQLAVGQKQRLAIARALVR 623
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEVTGVPPREIRKRVPAALELVG-----LSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 624 NPRVLILDEATSALDSQceqalQAWR--------SKGDRTVLVIAHRLHTVQNVD-QVLVLKQGQL 680
Cdd:cd03292 154 SPTILIADEPTGNLDPD-----TTWEimnllkkiNKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
153-415 |
1.70e-23 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 101.43 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 153 MVAFFFLAWAVLGETLIPHY-SGRVID----ILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRGGSFLFTMSRINLRIRE 227
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYlTKILIDdvliQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 228 RLFSSLLRQDLGFFQENKTGELNSRLSSDTSK----MSRWLPYnaniLLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLT 303
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRlqdfLSDGLPD----FLTNILMIIGIGVVLFSLNWKLALLVLIPVPLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 304 IAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLwwRRDLERaLYLAIRRVM 383
Cdd:cd18563 157 VWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDA--NIRAEK-LWATFFPLL 233
|
250 260 270
....*....|....*....|....*....|....*
gi 528078492 384 ALGMQ---VLILNCGVQQILAGEVTRGGLLSFLLY 415
Cdd:cd18563 234 TFLTSlgtLIVWYFGGRQVLSGTMTLGTLVAFLSY 268
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
468-681 |
2.15e-23 |
|
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: 99.12 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPlVQYDHHYLHRQVV 547
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS-IRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSG-SVKDNIAY-----GLKDCEDAQVMAAVRAACaddfigEMPDGIHTEIGekgsQLAVGQKQRLAIARAL 621
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLRVL------GLTDKANKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 622 VRNPRVLILDEATSALDSQCEQALqaW----RSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAI--WdlilEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLR 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
468-682 |
2.34e-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: 98.87 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQplvqyDHHYL---HR 544
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR-----DVTDLppkDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVGQEPVLFSG-SVKDNIAYGLK------DCEDAQVMAAVRAAcaddfigempdGIHTEIGEKGSQLAVGQKQRLAI 617
Cdd:cd03301 73 DIAMVFQNYALYPHmTVYDNIAFGLKlrkvpkDEIDERVREVAELL-----------QIEHLLDRKPKQLSGGQRQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 618 ARALVRNPRVLILDEATSALDSQCEQALQAWRSK-----GDRTVLVIAHRLHTVQNVDQVLVLKQGQLVE 682
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqqrlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
468-688 |
2.57e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.55 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEP--VLFSGSVKDNIAYGLKDC----ED--AQVMAAVRAACADDFIGEMPdgihteigekgSQLAVGQKQRLAIAR 619
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQgiprEEmiKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528078492 620 ALVRNPRVLILDEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEHSQLRE 688
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSE 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
484-692 |
3.34e-23 |
|
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: 98.90 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 484 PVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYD-HHYLHRQVVLVGQEPVLFSG-SVK 561
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIGYVPEGRRIFPSlTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 562 DNI---AYGLKDCEDAqvmAAVRAACADDFigemPdgihtEIGEKGSQLAV----GQKQRLAIARALVRNPRVLILDEAT 634
Cdd:COG0410 97 ENLllgAYARRDRAEV---RADLERVYELF----P-----RLKERRRQRAGtlsgGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 635 SALD----SQCEQALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH---SQLREDQDV 692
Cdd:COG0410 165 LGLAplivEEIFEIIRRLNREG-VTILLVEQNARFALEIaDRAYVLERGRIVLEgtaAELLADPEV 229
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
152-443 |
3.51e-23 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 100.25 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 152 LMVAFFFLAWAVLGETLIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRggsfLFTMSRINLRI----RE 227
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLR----RYLAGRLSLGVehdlRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 228 RLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYnANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAE 307
Cdd:cd18543 77 DLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 308 KVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGM 387
Cdd:cd18543 156 RRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 388 QVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18543 236 LAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
488-692 |
3.56e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.29 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 488 GLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQ-VVLVGQEPVLFSG-------- 558
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgVVRTFQHVRLFREmtvienll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 -----SVKDNIAYGL---KDCEDAQVMAAVRAACADDFIGeMPDGIHTEIGekgsQLAVGQKQRLAIARALVRNPRVLIL 630
Cdd:PRK11300 103 vaqhqQLKTGLFSGLlktPAFRRAESEALDRAATWLERVG-LLEHANRQAG----NLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 631 DEATSALDSQCEQALQA----WRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH---SQLREDQDV 692
Cdd:PRK11300 178 DEPAAGLNPKETKELDEliaeLRNEHNVTVLLIEHDMKLVMGIsDRIYVVNQGTPLANgtpEEIRNNPDV 247
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
468-682 |
4.09e-23 |
|
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: 98.91 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:cd03295 1 IEFENVTKRYGGG--KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSG-SVKDNIAY--GLKDCEDAQvmaavRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRN 624
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIALvpKLLKWPKEK-----IRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528078492 625 PRVLILDEATSALDSQCEQALQA----WRSKGDRTVLVIAHRL-HTVQNVDQVLVLKQGQLVE 682
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEefkrLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQ 216
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
485-691 |
4.70e-23 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 98.37 E-value: 4.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYL-HRQVVLVGQEPVLFSG-SVKD 562
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPRlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 563 NIAYGlkdcedaqvMAAVRAACA--DDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALD-- 638
Cdd:TIGR03410 95 NLLTG---------LAALPRRSRkiPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQps 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 639 --SQCEQALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVeHSQLREDQD 691
Cdd:TIGR03410 166 iiKDIGRVIRRLRAEGGMAILLVEQYLDFARELaDRYYVMERGRVV-ASGAGDELD 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
468-681 |
7.42e-23 |
|
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: 98.23 E-value: 7.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVaapLQ----NLYQPTGGQLLLDGQPLVQYD----- 538
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTL---LSlitgDLPPTYGNDVRLFGERRGGEDvwelr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 539 ----------HHYLH-----RQVVLVGqepvlFSGSVkdniayGL-KDCEDAQVMAAVR-------AACADDFIGEMpdg 595
Cdd:COG1119 78 kriglvspalQLRFPrdetvLDVVLSG-----FFDSI------GLyREPTDEQRERAREllellglAHLADRPFGTL--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 596 ihteigekgSQlavGQKQRLAIARALVRNPRVLILDEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTV-QNVD 670
Cdd:COG1119 144 ---------SQ---GEQRRVLIARALVKDPELLILDEPTAGLDlgarELLLALLDKLAAEGAPTLVLVTHHVEEIpPGIT 211
|
250
....*....|.
gi 528078492 671 QVLVLKQGQLV 681
Cdd:COG1119 212 HVLLLKDGRVV 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
485-688 |
7.81e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.45 E-value: 7.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQ-----PTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEP-VLFSG 558
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 SVKDNIAYGLK----DCEDAQVMAAVRAACADdfiGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEAT 634
Cdd:PRK14247 98 SIFENVALGLKlnrlVKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 635 SALDSQCEQALQA--WRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLRE 688
Cdd:PRK14247 175 ANLDPENTAKIESlfLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTRE 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
483-669 |
8.56e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.48 E-value: 8.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLFSGSVKD 562
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 563 NIAYGLKDCEDAQVMAAVRAACAdDFigEMPDgihtEIGEKG-SQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQc 641
Cdd:PRK10247 100 NLIFPWQIRNQQPDPAIFLDDLE-RF--ALPD----TILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES- 171
|
170 180
....*....|....*....|....*...
gi 528078492 642 eqalqawrskGDRTVLVIAHRLHTVQNV 669
Cdd:PRK10247 172 ----------NKHNVNEIIHRYVREQNI 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
468-681 |
1.18e-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: 96.58 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHH------- 540
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNrigylpe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 541 ----YLHRQVvlvgQEPVLFSGSVKdniayGLKDcEDAqvmaavrAACADDFIGEMpdgihtEIGEKGS----QLAVGQK 612
Cdd:cd03269 78 erglYPKMKV----IDQLVYLAQLK-----GLKK-EEA-------RRRIDEWLERL------ELSEYANkrveELSKGNQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 613 QRLAIARALVRNPRVLILDEATSALD----SQCEQALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:cd03269 135 QKVQFIAAVIHDPELLILDEPFSGLDpvnvELLKDVIRELARAG-KTVILSTHQMELVEELcDRVLLLNKGRAV 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
453-695 |
1.43e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 100.29 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 453 LPQPGTLAPSRLEGRVEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQ 532
Cdd:PRK11607 5 IPRPQAKTRKALTPLLEIRNLTKSFDG---QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 533 PLVQYDHHylHRQVVLVGQEPVLFSG-SVKDNIAYGLKdcEDAQVMAAVRAAcaddfIGEMPDGIHTE--IGEKGSQLAV 609
Cdd:PRK11607 82 DLSHVPPY--QRPINMMFQSYALFPHmTVEQNIAFGLK--QDKLPKAEIASR-----VNEMLGLVHMQefAKRKPHQLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 610 GQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQ-----AWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVehs 684
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQlevvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV--- 229
|
250
....*....|.
gi 528078492 685 QLREDQDVYAH 695
Cdd:PRK11607 230 QIGEPEEIYEH 240
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
471-681 |
1.55e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 97.49 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 471 QDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYL--HR---- 544
Cdd:COG4559 5 ENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarRRavlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 ------------QVVLVGQEPVLFSGSVKDNIAyglkdcedAQVMAAVraacaddfigempdGIHTEIGEKGSQLAVGQK 612
Cdd:COG4559 82 qhsslafpftveEVVALGRAPHGSSAAQDRQIV--------REALALV--------------GLAHLAGRSYQTLSGGEQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 613 QRLAIARALV-------RNPRVLILDEATSALD----SQCEQALQAWRSKGdRTVLVIAHRLH-TVQNVDQVLVLKQGQL 680
Cdd:COG4559 140 QRVQLARVLAqlwepvdGGPRWLFLDEPTSALDlahqHAVLRLARQLARRG-GGVVAVLHDLNlAAQYADRILLLHQGRL 218
|
.
gi 528078492 681 V 681
Cdd:COG4559 219 V 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
468-691 |
1.85e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 96.70 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLV--QYDHHYLHRQ 545
Cdd:PRK09493 2 IEFKNVSKHFGP---TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 546 VVLVGQEPVLFSG-SVKDNIAYGlkdceDAQVMAAVRAAC---ADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARAL 621
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFG-----PLRVRGASKEEAekqARELLAKV--GLAERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528078492 622 VRNPRVLILDEATSALDSQCEQ-ALQAWRSKGDR--TVLVIAHRLHTVQNVDQVLVlkqgqLVEHSQLREDQD 691
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHeVLKVMQDLAEEgmTMVIVTHEIGFAEKVASRLI-----FIDKGRIAEDGD 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
469-683 |
2.09e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 96.36 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPSRP*kpvlkgLTFTLH--PGKVTALVGPNGSGKSTvaapLQNL----YQPTGGQLLLDGQPLVQYDHHyl 542
Cdd:COG3840 3 RLDDLTYRYGDFP-------LRFDLTiaAGERVAILGPSGAGKST----LLNLiagfLPPDSGRILWNGQDLTALPPA-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 543 HRQVVLVGQEPVLFSG-SVKDNIAYGLK------DCEDAQVMAAVRAACADDFIGEMPdgihteigekgSQLAVGQKQRL 615
Cdd:COG3840 70 ERPVSMLFQENNLFPHlTVAQNIGLGLRpglkltAEQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528078492 616 AIARALVRNPRVLILDEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH 683
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHDPEDAARIaDRVLLVADGRIAAD 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
483-682 |
3.03e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 96.65 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQ------PTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVLF 556
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 557 SG-SVKDNIAYGLKD--CEDAQVMAAVRAACADDfIGEMPDgIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEA 633
Cdd:PRK14246 103 PHlSIYDNIAYPLKShgIKEKREIKKIVEECLRK-VGLWKE-VYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 528078492 634 TSALDSQCEQALQAWRS--KGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVE 682
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITelKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVE 232
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
472-685 |
3.41e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.00 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 472 DVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLvQYDHH---YLHRQVVL 548
Cdd:PRK13638 6 DLWFRYQD---EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 549 VGQEP--VLFSGSVKDNIAYGLKDCEDAQVMAAVRaacADDFIgEMPDGIHTEigEKGSQ-LAVGQKQRLAIARALVRNP 625
Cdd:PRK13638 82 VFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRR---VDEAL-TLVDAQHFR--HQPIQcLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 626 RVLILDEATSALD----SQCEQALQAWRSKGDRtVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQ 685
Cdd:PRK13638 156 RYLLLDEPTAGLDpagrTQMIAIIRRIVAQGNH-VIISSHDIDLIYEIsDAVYVLRQGQILTHGA 219
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
486-682 |
3.50e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 96.78 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPV----------- 554
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 555 LFSGSVKDNIAYGLKDCEDaQVMAAVRAacaddfIGEMPDgihtEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEAT 634
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREK-QIIETLRQ------VGLLPD----HASYYPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 528078492 635 SALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVE 682
Cdd:PRK15112 178 ASLDmsmrSQLINLMLELQEKQGISYIYVTQHLGMMKHIsDQVLVMHQGEVVE 230
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
469-661 |
4.62e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.47 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYP-SRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDhhyLHRQVV 547
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG---ADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LvgQEPVLFSG-SVKDNIAYGLKDcedAQVMAAVRAACADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPR 626
Cdd:COG4525 82 F--QKDALLPWlNVLDNVAFGLRL---RGVPKAERRARAEELLALV--GLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 528078492 627 VLILDEATSALDSQC-EQA----LQAWRSKGdRTVLVIAH 661
Cdd:COG4525 155 FLLMDEPFGALDALTrEQMqellLDVWQRTG-KGVFLITH 193
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
474-682 |
8.29e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 94.52 E-value: 8.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 474 TFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQ--PLV------QYDhhylhrq 545
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsSLLglgggfNPE------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 546 vvLVGQEPVLFSGSVkdniaYGLKDCEDAQVMaavraacadDFIGEMpdgihTEIGEKGSQ----LAVGQKQRLAIARAL 621
Cdd:cd03220 99 --LTGRENIYLNGRL-----LGLSRKEIDEKI---------DEIIEF-----SELGDFIDLpvktYSSGMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 622 VRNPRVLILDEATSALDS----QCEQALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVE 682
Cdd:cd03220 158 ALEPDILLIDEVLAVGDAafqeKCQRRLRELLKQG-KTVILVSHDPSSIKRLcDRALVLEKGKIRF 222
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
152-415 |
1.05e-21 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 95.92 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 152 LMVAFFFLAWAVLGETLIPHYSGRVID--ILGSDFDP*SFASAIFFMCLFSVGSSLSagcrggSFLFTMS------RINL 223
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDdyIVPGQGDLQGLLLLALLYLGLLLLSFLL------QYLQTYLlqklgqRIIY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 224 RIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWlpYNANI--LLRSLVKVIGLYCFMLQVSPRLTFLSLLDLP 301
Cdd:cd18544 75 DLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNEL--FTSGLvtLIGDLLLLIGILIAMFLLNWRLALISLLVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 302 LTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRrdlERALYLAIRR 381
Cdd:cd18544 153 LLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLK---SIKLFALFRP 229
|
250 260 270
....*....|....*....|....*....|....*...
gi 528078492 382 VM----ALGMqVLILNCGVQQILAGEVTRGGLLSFLLY 415
Cdd:cd18544 230 LVellsSLAL-ALVLWYGGGQVLSGAVTLGVLYAFIQY 266
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
490-682 |
1.42e-21 |
|
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: 95.02 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 490 TFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYL----HRQVVLVGQEPVLFSG-SVKDNI 564
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 565 AYGLkdcEDAQVMAAVRAACADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALD----SQ 640
Cdd:cd03294 124 AFGL---EVQGVPRAEREERAAEALELV--GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 528078492 641 CEQALQAWRSKGDRTVLVIAHRL-HTVQNVDQVLVLKQGQLVE 682
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQ 241
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
469-681 |
1.58e-21 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 94.17 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLH---RQ 545
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 546 VVLVGQEPVLFSG-SVKDNIAYGLkdcedAQVMAAVRA--------------ACADDFigempdGIHTEIGEKGSQLAVG 610
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGR-----LGRRSTWRSlfglfpkeekqralAALERV------GLLDKAYQRADQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 611 QKQRLAIARALVRNPRVLILDEATSALDSQ-CEQALQAWRSKG---DRTVLViahRLHTVQ----NVDQVLVLKQGQLV 681
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPAsSRQVMDLLKRINreeGITVIV---SLHQVDlareYADRIVGLKDGRIV 224
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
152-443 |
1.64e-21 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 95.55 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 152 LMVAFFFLAWAVLGETLIPHYSGRVIDIL------GSDFDP*SFASAIFFMCLFSVGSSLSagcrggSFL--FTMSRI-- 221
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIieglggGGGVDFSGLLRILLLLLGLYLLSALF------SYLqnRLMARVsq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 222 --NLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLD 299
Cdd:cd18547 75 rtVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 300 LPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWrrdleRALYLA- 378
Cdd:cd18547 155 VPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASF-----KAQFYSg 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 379 -----IRRVMALGmQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18547 230 llmpiMNFINNLG-YVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
483-692 |
1.66e-21 |
|
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: 93.76 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYD-HHYLHRQVVLVGQEPVLFSG-SV 560
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 561 KDNIAYGLkdcEDAQVMAAVRAACADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQ 640
Cdd:cd03218 93 EENILAVL---EIRGLSKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 641 CEQALQA----WRSKGdRTVLVIAHRLH-TVQNVDQVLVLKQGQLVEH---SQLREDQDV 692
Cdd:cd03218 168 AVQDIQKiikiLKDRG-IGVLITDHNVReTLSITDRAYIIYEGKVLAEgtpEEIAANELV 226
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
483-682 |
1.80e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.98 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNL--YQPTGGQLLLDGQPLVQYD-HHYLHRQVVLVGQEPVLFSG- 558
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSpDERARAGIFLAFQYPVEIPGv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 SVKD--NIAYGLKDCEDAQVMAAVRAAC--------ADDFigempdgIHTEIGEKGSQlavGQKQRLAIARALVRNPRVL 628
Cdd:COG0396 93 SVSNflRTALNARRGEELSAREFLKLLKekmkelglDEDF-------LDRYVNEGFSG---GEKKRNEILQMLLLEPKLA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528078492 629 ILDEATSALD-------SqceQALQAWRSKgDRTVLVIAH--RLHTVQNVDQVLVLKQGQLVE 682
Cdd:COG0396 163 ILDETDSGLDidalrivA---EGVNKLRSP-DRGILIITHyqRILDYIKPDFVHVLVDGRIVK 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
483-688 |
2.62e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.69 E-value: 2.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNL--YQP---TGGQLLLDGQPLV--QYDHHYLHRQVVLVGQEPVL 555
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYspRTDTVDLRKEIGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 556 FSGSVKDNIAYGL-----KDCE--DAQVMAAVRAACADDfigEMPDGIH-TEIGEKGsqlavGQKQRLAIARALVRNPRV 627
Cdd:PRK14239 98 FPMSIYENVVYGLrlkgiKDKQvlDEAVEKSLKGASIWD---EVKDRLHdSALGLSG-----GQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 628 LILDEATSALD----SQCEQALqaWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLRE 688
Cdd:PRK14239 170 ILLDEPTSALDpisaGKIEETL--LGLKDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYNDTKQ 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
468-681 |
3.52e-21 |
|
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: 92.56 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*KpvlkgLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQplvqyDHHYL---HR 544
Cdd:cd03298 1 VRLDKIRFSYGEQPMH-----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV-----DVTAAppaDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVGQEPVLFSG-SVKDNIAYGLK-----DCEDAQVMAAVraacaddfIGEMpdGIHTEIGEKGSQLAVGQKQRLAIA 618
Cdd:cd03298 71 PVSMLFQENNLFAHlTVEQNVGLGLSpglklTAEDRQAIEVA--------LARV--GLAGLEKRLPGELSGGERQRVALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 619 RALVRNPRVLILDEATSALDSQCEQALQAWRSKGDR----TVLVIAHRLHTVQNVDQ-VLVLKQGQLV 681
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAetkmTVLMVTHQPEDAKRLAQrVVFLDNGRIA 208
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
486-683 |
4.09e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.03 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHY---LHRQVVLVGQEPVlfsGS--- 559
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNPY---GSlnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 560 ---VKDNIAYGLKDceDAQVMAAVRAACADDFIGEMpdGIHTEIGEKGSQL-AVGQKQRLAIARALVRNPRVLILDEATS 635
Cdd:PRK11308 108 rkkVGQILEEPLLI--NTSLSAAERREKALAMMAKV--GLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 636 ALDSQCeQA--------LQawRSKGDRTVLvIAHRLHTVQNV-DQVLVLKQGQLVEH 683
Cdd:PRK11308 184 ALDVSV-QAqvlnlmmdLQ--QELGLSYVF-ISHDLSVVEHIaDEVMVMYLGRCVEK 236
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
447-679 |
6.57e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.19 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 447 IDRKPNLPQPGTLAPSRLEGRVEFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQ 526
Cdd:COG4178 342 LEAADALPEAASRIETSEDGALALEDLTLRTPDG--RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGR 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 527 LLLDGqplvqydhhylHRQVVLVGQEPVLFSGSVKDNIAYGLKDCE--DAQVMAAVRAACADDFIGEMpdgihTEIGEKG 604
Cdd:COG4178 420 IARPA-----------GARVLFLPQRPYLPLGTLREALLYPATAEAfsDAELREALEAVGLGHLAERL-----DEEADWD 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 605 SQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQAL-QAWRSK-GDRTVLVIAHRLHTVQNVDQVLVLKQGQ 679
Cdd:COG4178 484 QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALyQLLREElPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
152-443 |
1.26e-20 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 92.96 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 152 LMVAFFFLAWAVLGETLIPHYSGRVID-ILGSDFDP*SFA----------SAIFFMCLFSVGSSLSAGcrGGSFLFTM-- 218
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDdVLGDKPLPGLLGlapllgpdplALLLLAAAALVGIALLRG--LASYAGTYlt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 219 ----SRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTF 294
Cdd:cd18564 79 alvgQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 295 LSLLDLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWR-RDLER 373
Cdd:cd18564 159 IALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRaARLQA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 374 ALYLAIRRVMALGMqVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18564 239 LLSPVVDVLVAVGT-ALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
220-415 |
1.46e-20 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 93.01 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 220 RINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLD 299
Cdd:cd18565 84 RVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 300 LPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAI 379
Cdd:cd18565 164 VPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPV 243
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 528078492 380 RRVMALGMQVLILNCGVQQILAG------EVTRGGLLSFLLY 415
Cdd:cd18565 244 IRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFY 285
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
152-415 |
3.25e-20 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 91.44 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 152 LMVAFFFLAWAVLGETLIPHYSGRVIDILgsdFDP*SFASAIFFMCLFSVGS-SLSAGCRGGSFLFtMSRINLR----IR 226
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLV---TIGSKSLGLLLGLALLLLGAyLLRALLNFLRIYL-NHVAEQKvvadLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 227 ERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAA 306
Cdd:cd18778 77 SDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 307 EKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERcrqlwWRRDLERALYL------AIR 380
Cdd:cd18778 157 AWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRR-----YRKAQLRAMKLwaifhpLME 231
|
250 260 270
....*....|....*....|....*....|....*
gi 528078492 381 RVMALGMqVLILNCGVQQILAGEVTRGGLLSFLLY 415
Cdd:cd18778 232 FLTSLGT-VLVLGFGGRLVLAGELTIGDLVAFLLY 265
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
469-693 |
3.93e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.21 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPSrp*kpV--LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPlVQYDH--HYLHR 544
Cdd:PRK11288 6 SFDGIGKTFPG-----VkaLDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-MRFASttAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVGQE----PVLfsgSVKDNI-------AYGLKDCEDAQVMAAVRAAcaddfigEMpdGIHTEIGEKGSQLAVGQKQ 613
Cdd:PRK11288 80 GVAIIYQElhlvPEM---TVAENLylgqlphKGGIVNRRLLNYEAREQLE-------HL--GVDIDPDTPLKYLSIGQRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 614 RLAIARALVRNPRVLILDEATSALDSQCEQAL----QAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVE------ 682
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSAREIEQLfrviRELRAEG-RVILYVSHRMEEIFALcDAITVFKDGRYVAtfddma 226
|
250 260
....*....|....*....|
gi 528078492 683 ---HSQL------REDQDVY 693
Cdd:PRK11288 227 qvdRDQLvqamvgREIGDIY 246
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
189-682 |
4.16e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 95.96 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 189 FASAIFfmclfsVGSSLSAGCRGGSFLFTMsRINLRIRERLFSSLLRQDLGFFQEnktgelnSRLSSDTSKMSRWLPYNA 268
Cdd:PLN03130 343 YAFSIF------VGVVLGVLCEAQYFQNVM-RVGFRLRSTLVAAVFRKSLRLTHE-------GRKKFTSGKITNLMTTDA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 269 NIL--------------LRSLVKVIGLYcfmLQVSPRLTFLSLLdLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVRE 334
Cdd:PLN03130 409 EALqqicqqlhtlwsapFRIIIAMVLLY---QQLGVASLIGSLM-LVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNE 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 335 AVGGLQTVRSFGAEEQEVSRYKEAleRCRQLWWRRdleRALYLAIRRVMALG---MQVLILNCGVQQILAGEVTRG-GLL 410
Cdd:PLN03130 485 VLAAMDTVKCYAWENSFQSKVQTV--RDDELSWFR---KAQLLSAFNSFILNsipVLVTVVSFGVFTLLGGDLTPArAFT 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 411 SFLLYQeevgdYVRNLVYMYGDMLSNVGAA-------EKVFCYIDR--KPNLP-QPGTLAPSrlegrveFQDVTFSYPSR 480
Cdd:PLN03130 560 SLSLFA-----VLRFPLFMLPNLITQAVNAnvslkrlEELLLAEERvlLPNPPlEPGLPAIS-------IKNGYFSWDSK 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 481 P*KPVLKGLTFTLHPGKVTALVGPNGSGK-STVAAPLQNLYQPTGGQLLLDGQplvqydhhylhrqVVLVGQEPVLFSGS 559
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRGT-------------VAYVPQVSWIFNAT 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 560 VKDNIAYGLkDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDS 639
Cdd:PLN03130 695 VRDNILFGS-PFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 528078492 640 QCEQALQAWRSKGD---RTVLVIAHRLHTVQNVDQVLVLKQGQLVE 682
Cdd:PLN03130 774 HVGRQVFDKCIKDElrgKTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
193-698 |
6.90e-20 |
|
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: 94.98 E-value: 6.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 193 IFFMCLFSVGSSLSAGC-RGGSFLFTMSRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANIL 271
Cdd:TIGR01271 927 IFYIYVGTADSVLALGFfRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDF 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 272 LRSLVKVIGLYCFMLQVSPrLTFLSLLDLPLTIAAEKVYNPRHQAVLTEIQ-DATAKAGQVVREAVGGLQTVRSFGAEEQ 350
Cdd:TIGR01271 1007 IQLTLIVLGAIFVVSVLQP-YIFIAAIPVAVIFIMLRAYFLRTSQQLKQLEsEARSPIFSHLITSLKGLWTIRAFGRQSY 1085
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 351 EVSRYKEALERCRQLWWrrdleraLYLAIRR--VMALGM-------QVLILNCGVQQILAGEVtrGGLLSFLLYQEEVGD 421
Cdd:TIGR01271 1086 FETLFHKALNLHTANWF-------LYLSTLRwfQMRIDIifvfffiAVTFIAIGTNQDGEGEV--GIILTLAMNILSTLQ 1156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 422 YVRNLVYMYGDMLSNVgaaEKVFCYIDRKPNLPQP----GTLAPSRL--------------EGRVEFQDVTFSYPSrP*K 483
Cdd:TIGR01271 1157 WAVNSSIDVDGLMRSV---SRVFKFIDLPQEEPRPsgggGKYQLSTVlvienphaqkcwpsGGQMDVQGLTAKYTE-AGR 1232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 484 PVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQpTGGQLLLDGqplVQYDHHYLH---RQVVLVGQEPVLFSGSV 560
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG---VSWNSVTLQtwrKAFGVIPQKVFIFSGTF 1308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 561 KDNIAyGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQ 640
Cdd:TIGR01271 1309 RKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV 1387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 641 CEQALQAW--RSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEHSQLREDQDVYAHLVQ 698
Cdd:TIGR01271 1388 TLQIIRKTlkQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
481-678 |
7.25e-20 |
|
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: 88.93 E-value: 7.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 481 P*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLL----LDGQPLVQYDHHYLHRQVVLVGQEPVLF 556
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 557 SGSVKDNIAYGlkDCEDAQVMAAVRAACA-DDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATS 635
Cdd:cd03290 92 NATVEENITFG--SPFNKQRYKAVTDACSlQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 528078492 636 ALDSQC-----EQALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQG 678
Cdd:cd03290 170 ALDIHLsdhlmQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
491-688 |
8.51e-20 |
|
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: 91.70 E-value: 8.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 491 FTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDH-HYL---HRQVVLVGQEPVLFSG-SVKDNIA 565
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARgIFLpphRRRIGYVFQEARLFPHlSVRGNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 566 YGLKDCEDAQvmaavRAACADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQA- 644
Cdd:COG4148 100 YGRKRAPRAE-----RRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEi 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 528078492 645 ---LQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLRE 688
Cdd:COG4148 173 lpyLERLRDELDIPILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAE 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
470-690 |
1.10e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 470 FQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGqplvqydhhylHRQVVLV 549
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 550 GQEPVLFSG-SVKDNIAYGLKdcEDAQVMAAVRAACAD----DFIGEMPDGIHTEIGEKG-------------------- 604
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDA--ELRALEAELEELEAKlaepDEDLERLAELQEEFEALGgweaearaeeilsglgfpee 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 605 ------SQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQC----EQALQAWRSkgdrTVLVIAH-R--LHTVqnVDQ 671
Cdd:COG0488 145 dldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKNYPG----TVLVVSHdRyfLDRV--ATR 218
|
250 260
....*....|....*....|....*....
gi 528078492 672 VLVLKQGQL----------VEHSQLREDQ 690
Cdd:COG0488 219 ILELDRGKLtlypgnysayLEQRAERLEQ 247
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
468-694 |
1.15e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.17 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLvqydhHYLHRQvv 547
Cdd:COG4152 2 LELKGLTKRFGD---KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-----DPEDRR-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVG---QEPVLFSG-SVKDNIAY--GLKDCEDAQVMAAvraacADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARAL 621
Cdd:COG4152 72 RIGylpEERGLYPKmKVGEQLVYlaRLKGLSKAEAKRR-----ADEWLERL--GLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 622 VRNPRVLILDEATSALD----SQCEQALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLREDQDVYA 694
Cdd:COG4152 145 LHDPELLILDEPFSGLDpvnvELLKDVIRELAAKG-TTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
485-700 |
1.34e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 88.65 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQL-----LLDG-QPLVQYDH--HYLHRQVVLVGQEPVLF 556
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKGliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 557 SG-SVKDNIAYG---LKDCEDAQVMAAVRAACAddfigempdgihtEIGEKGSQ------LAVGQKQRLAIARALVRNPR 626
Cdd:PRK11264 98 PHrTVLENIIEGpviVKGEPKEEATARARELLA-------------KVGLAGKEtsyprrLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 627 VLILDEATSALDSQ-CEQALQAWRSKGD--RTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLREdqdVYAHLVQQR 700
Cdd:PRK11264 165 VILFDEPTSALDPElVGEVLNTIRQLAQekRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKA---LFADPQQPR 239
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
476-675 |
1.71e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.90 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 476 SYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLlldgqplvqydHHYLHRQVVLVGQ---E 552
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 553 PVLFSGSVKDNIAYGL---------KDCED-AQVMAAVRAACADDFIGEmpdgihtEIGEkgsqLAVGQKQRLAIARALV 622
Cdd:NF040873 67 PDSLPLTVRDLVAMGRwarrglwrrLTRDDrAAVDDALERVGLADLAGR-------QLGE----LSGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 623 RNPRVLILDEATSALDSQCEQA----LQAWRSKGdRTVLVIAHRLHTVQNVDQVLVL 675
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERiialLAEEHARG-ATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
468-681 |
1.80e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.03 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPS-RP*K-PVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPL----VQYDHHY 541
Cdd:PRK13649 3 INLQNVSYTYQAgTPFEgRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 542 LHRQVVLVGQ--EPVLFSGSVKDNIAYGLKDC----EDAQVMAAVRAACAddfigempdGIHTEIGEKGS-QLAVGQKQR 614
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFgvsqEEAEALAREKLALV---------GISESLFEKNPfELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528078492 615 LAIARALVRNPRVLILDEATSALDSQCEQALQAWRSK---GDRTVLVIAHRLHTVQN-VDQVLVLKQGQLV 681
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKlhqSGMTIVLVTHLMDDVANyADFVYVLEKGKLV 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
479-677 |
3.63e-19 |
|
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: 86.39 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 479 SRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYlHRQVVLVGQEPVLFSG 558
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 -SVKDNIAYGLKDCEDAQVMAAVRAACADDFiGEMPDGihteigekgsQLAVGQKQRLAIARALVRNPRVLILDEATSAL 637
Cdd:cd03231 88 lSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 528078492 638 D----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQ 677
Cdd:cd03231 157 DkagvARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLGF 200
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
486-681 |
4.46e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.20 E-value: 4.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYqPTGGQLLLDGQPLVQYDHHYL-HRQVVLVGQEPVLFSGSVKDNI 564
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELaRHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 565 AYGLKDCEDAQVMAAVRAACADDFigEMPDGIHTEIgekgSQLAVGQKQRLAIARALVR-----NP--RVLILDEATSAL 637
Cdd:COG4138 91 ALHQPAGASSEAVEQLLAQLAEAL--GLEDKLSRPL----TQLSGGEWQRVRLAAVLLQvwptiNPegQLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 528078492 638 DSQCEQALQAWRSK----GdRTVLVIAHRL-HTVQNVDQVLVLKQGQLV 681
Cdd:COG4138 165 DVAQQAALDRLLRElcqqG-ITVVMSSHDLnHTLRHADRVWLLKQGKLV 212
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
152-443 |
4.77e-19 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 88.29 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 152 LMVAFFFLAWAVLGETLIPHYSGRVID--ILGSDFDP*SFASAIFFmcLFSVGSSLSAGCRGgsflFTMSRIN----LRI 225
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDeyIPNGDLSGLLIIALLFL--ALNLVNWVASRLRI----YLMAKVGqrilYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 226 RERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPyNANI-LLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTI 304
Cdd:cd18545 76 RQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLS-NGLInLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 305 AA----EKVYNPRHQAVLTEIQDATAKagqvVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWwrrdlERALYLA-- 378
Cdd:cd18545 155 LVvfllRRRARKAWQRVRKKISNLNAY----LHESISGIRVIQSFAREDENEEIFDELNRENRKAN-----MRAVRLNal 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 379 ----IRRVMALGMqVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18545 226 fwplVELISALGT-ALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
480-639 |
5.06e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.08 E-value: 5.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 480 RP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDH----HYL-HRQvvlvGQEPV 554
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeacHYLgHRN----AMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 555 LfsgSVKDNIAY--GLKDCEDAQVMAAVraacadDFIGeMPDGIHTEIGEkgsqLAVGQKQRLAIARALVRNPRVLILDE 632
Cdd:PRK13539 88 L---TVAENLEFwaAFLGGEELDIAAAL------EAVG-LAPLAHLPFGY----LSAGQKRRVALARLLVSNRPIWILDE 153
|
....*..
gi 528078492 633 ATSALDS 639
Cdd:PRK13539 154 PTAALDA 160
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
460-683 |
5.35e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 5.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 460 APSRLeGR--VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLdGQPLVQ- 536
Cdd:COG0488 307 PPERL-GKkvLELEGLSKSYGD---KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIg 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 537 Y---DHHYLHRqvvlvgqepvlfSGSVKDNIAYGLKDCEDAQvmaaVRAACAD-DFIGEMpdgIHTEIGEkgsqLAVGQK 612
Cdd:COG0488 382 YfdqHQEELDP------------DKTVLDELRDGAPGGTEQE----VRGYLGRfLFSGDD---AFKPVGV----LSGGEK 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 613 QRLAIARALVRNPRVLILDEATSALD----SQCEQALQAWrsKGdrTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH 683
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDietlEALEEALDDF--PG--TVLLVSHDRYFLDRVaTRILEFEDGGVREY 510
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
485-648 |
5.51e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.99 E-value: 5.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQplvqyDHHYLH---RQVVLVGQEPVLFSG-SV 560
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT-----DVSRLHardRKVGFVFQHYALFRHmTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 561 KDNIAYGLK----------DCEDAQVMAAVRAACADDFIGEMPdgihteigekgSQLAVGQKQRLAIARALVRNPRVLIL 630
Cdd:PRK10851 92 FDNIAFGLTvlprrerpnaAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLL 160
|
170
....*....|....*...
gi 528078492 631 DEATSALDSQCEQALQAW 648
Cdd:PRK10851 161 DEPFGALDAQVRKELRRW 178
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
468-700 |
5.83e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.67 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYP-------------------SRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVaapLQ---NLYQPTGG 525
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTL---LKliaGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 526 QLLLDGQ--PLV------QYDhhylhrqvvLVGQEPVLFSGSVkdniaYGLKDCEDAQVMAAVRaacadDFigempdgih 597
Cdd:COG1134 82 RVEVNGRvsALLelgagfHPE---------LTGRENIYLNGRL-----LGLSRKEIDEKFDEIV-----EF--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 598 TEIGEKGSQlAV-----GQKQRLAIARALVRNPRVLILDEATSALDSQ----CEQALQAWRSKGdRTVLVIAHRLHTVQN 668
Cdd:COG1134 134 AELGDFIDQ-PVktyssGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRESG-RTVIFVSHSMGAVRR 211
|
250 260 270
....*....|....*....|....*....|...
gi 528078492 669 V-DQVLVLKQGQLVEHSQLREDQDVYAHLVQQR 700
Cdd:COG1134 212 LcDRAIWLEKGRLVMDGDPEEVIAAYEALLAGR 244
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
468-688 |
8.53e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 8.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYpsRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEP--VLFSGSVKDNIAYG---LKDCEDA---QVMAAVRAACADDFIGEMPdgihteigekgSQLAVGQKQRLAIAR 619
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGpinLGLDEETvahRVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 620 ALVRNPRVLILDEATSALDSQCEQAL----QAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLRE 688
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELidflNDLPETYGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEE 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
468-688 |
1.08e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.14 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSY-PSRP-*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQY--DHHYLH 543
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 544 -RQVV-LVGQ--EPVLFSGSVKDNIAYGLK----DCEDAQvmaavraacADDFIGEMPDGIHTEIGEKGS-QLAVGQKQR 614
Cdd:PRK13646 83 vRKRIgMVFQfpESQLFEDTVEREIIFGPKnfkmNLDEVK---------NYAHRLLMDLGFSRDVMSQSPfQMSGGQMRK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 615 LAIARALVRNPRVLILDEATSALDSQCEQA----LQAWRSKGDRTVLVIAHRLHTV-QNVDQVLVLKQGQLVEHSQLRE 688
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQvmrlLKSLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKE 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
471-680 |
1.15e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.27 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 471 QDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLvqydhHYLHRQVVLVG 550
Cdd:PRK11247 16 NAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 551 QEPVLFS-GSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPdgihteigekgSQLAVGQKQRLAIARALVRNPRVLI 629
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 630 LDEATSALDSQCEQALQA-----WRSKGdRTVLVIAHRL-HTVQNVDQVLVLKQGQL 680
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDlieslWQQHG-FTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
449-681 |
1.23e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 90.99 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 449 RKPNLPQPGTLAPSRLEGRVEFQDVTFSYPSrp*kpvlkgltftlhpGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLL 528
Cdd:PTZ00243 655 RSAKTPKMKTDDFFELEPKVLLRDVSVSVPR----------------GKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 529 LDgqplvqydhhylhRQVVLVGQEPVLFSGSVKDNIAYglKDCEDAQVMA-AVRAACADDFIGEMPDGIHTEIGEKGSQL 607
Cdd:PTZ00243 719 AE-------------RSIAYVPQQAWIMNATVRGNILF--FDEEDAARLAdAVRVSQLEADLAQLGGGLETEIGEKGVNL 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 608 AVGQKQRLAIARALVRNPRVLILDEATSALDSQC------EQALQAWRSKgdrTVLVIAHRLHTVQNVDQVLVLKQGQLV 681
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgervveECFLGALAGK---TRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
447-682 |
2.31e-18 |
|
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: 90.00 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 447 IDRKPNLPQPGTlapsrlegRVEFQDVTFSYpSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQ 526
Cdd:TIGR00957 624 IERRTIKPGEGN--------SITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 527 LLLDGQplvqydhhylhrqVVLVGQEPVLFSGSVKDNIAYG--LKDCEDAQVMAAVrAACADDFIgeMPDGIHTEIGEKG 604
Cdd:TIGR00957 695 VHMKGS-------------VAYVPQQAWIQNDSLRENILFGkaLNEKYYQQVLEAC-ALLPDLEI--LPSGDRTEIGEKG 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 605 SQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQC-----EQALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQ 679
Cdd:TIGR00957 759 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgkhifEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGK 838
|
...
gi 528078492 680 LVE 682
Cdd:TIGR00957 839 ISE 841
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
468-695 |
2.45e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.08 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVqyDHHYLHRQVV 547
Cdd:PRK11432 7 VVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSG-SVKDNIAYGLK--DCEDAQVMAAVRAACA--------DDFIgempdgihteigekgSQLAVGQKQRLA 616
Cdd:PRK11432 82 MVFQSYALFPHmSLGENVGYGLKmlGVPKEERKQRVKEALElvdlagfeDRYV---------------DQISGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 617 IARALVRNPRVLILDEATSALDSQCEQALqawRSK-------GDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVehsQLRE 688
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDANLRRSM---REKirelqqqFNITSLYVTHDQSEAFAVsDTVIVMNKGKIM---QIGS 220
|
....*..
gi 528078492 689 DQDVYAH 695
Cdd:PRK11432 221 PQELYRQ 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
481-686 |
2.80e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.14 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 481 P*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLvqyDHHYLHRQVVLvGQEPVLFSGSV 560
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV---EGPGAERGVVF-QNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 561 KDNIAYGLkdcEDAQVMAAVRAACAddfiGEMPDGIHTEIGEKGS--QLAVGQKQRLAIARALVRNPRVLILDEATSALD 638
Cdd:PRK11248 88 QDNVAFGL---QLAGVEKMQRLEIA----HQMLKKVGLEGAEKRYiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 639 SQC-EQA----LQAWRSKGdRTVLVIAHRLHTVQNVDQVLVL---KQGQLVEHSQL 686
Cdd:PRK11248 161 AFTrEQMqtllLKLWQETG-KQVLLITHDIEEAVFMATELVLlspGPGRVVERLPL 215
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
136-682 |
3.36e-18 |
|
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: 88.32 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 136 SLMWQLLRLSRPdlPFLMVAFFFLAWAVLGETLIphysGRVIDILGSDFDP*S-----FASAIFFMCLFSVGSSLSAGCR 210
Cdd:COG4615 2 NLLRLLLRESRW--LLLLALLLGLLSGLANAGLI----ALINQALNATGAALArllllFAGLLVLLLLSRLASQLLLTRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 211 GGSFLFtmsrinlRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSR---WLPynanILLRSLVKVIGLYCFMLQ 287
Cdd:COG4615 76 GQHAVA-------RLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQafvRLP----ELLQSVALVLGCLAYLAW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 288 VSPRLTFLSLLDLPLTIAAekvynprHQAVLTEIQDATAKAGQVVREAVGGLQTVrSFGAEEQEVSR------YKEALER 361
Cdd:COG4615 145 LSPPLFLLTLVLLGLGVAG-------YRLLVRRARRHLRRAREAEDRLFKHFRAL-LEGFKELKLNRrrrrafFDEDLQP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 362 CRQLWwrRDLERALYLAIRRVMALGmQVLILncGVQqilagevtrgGLLSFLL------YQEEVGDYVRNLVYMYG---- 431
Cdd:COG4615 217 TAERY--RDLRIRADTIFALANNWG-NLLFF--ALI----------GLILFLLpalgwaDPAVLSGFVLVLLFLRGplsq 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 432 --DMLSNVGAAEKVFCYIDR--------KPNLPQPGTLAPSRLEGRVEFQDVTFSYPSRP*KP--VLKGLTFTLHPGKVT 499
Cdd:COG4615 282 lvGALPTLSRANVALRKIEElelalaaaEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 500 ALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPL--VQYDHhylHRQ---VVLvgQEPVLFsgsvkDNIaYGLKDCEDA 574
Cdd:COG4615 362 FIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtaDNREA---YRQlfsAVF--SDFHLF-----DRL-LGLDGEADP 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 575 QVmaavraacADDFIGEMpdgihtEIGEKGS---------QLAVGQKQRLAIARALVRNPRVLILDEATSALDSQ----- 640
Cdd:COG4615 431 AR--------ARELLERL------ELDHKVSvedgrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvf 496
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 528078492 641 CEQALQAWRSKGdRTVLVIAHRLHTVQNVDQVLVLKQGQLVE 682
Cdd:COG4615 497 YTELLPELKARG-KTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
486-682 |
3.39e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.40 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLH----RQVVLVGQEPVLFSG-SV 560
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 561 KDNIAYGLkdcEDAQVMAAVRAACADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALD-- 638
Cdd:PRK10070 124 LDNTAFGM---ELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDpl 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 528078492 639 --SQCEQALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVE 682
Cdd:PRK10070 199 irTEMQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQ 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
486-681 |
7.46e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.15 E-value: 7.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQplvQYDH--HYLHRQ--VVLVGQE-PVLFSGSV 560
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI---NYNKldHKLAAQlgIGIIYQElSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 561 KDNIAYG-----------LKDCEDAQVMAAVraacaddfigeMPD--GIHTEIGEKGSQLAVGQKQRLAIARALVRNPRV 627
Cdd:PRK09700 98 LENLYIGrhltkkvcgvnIIDWREMRVRAAM-----------MLLrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 628 LILDEATSAL-DSQCEQ---ALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:PRK09700 167 IIMDEPTSSLtNKEVDYlflIMNQLRKEG-TAIVYISHKLAEIRRIcDRYTVMKDGSSV 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
486-675 |
8.40e-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: 82.90 E-value: 8.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLvqyDHHYLHRQVVLvgQEPVLFSG-SVKDNI 564
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI---TEPGPDRMVVF--QNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 565 AYGLkDCEDAQVMAAVRAACADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQC--- 641
Cdd:TIGR01184 76 ALAV-DRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTrgn 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 528078492 642 --EQALQAWRSKGdRTVLVIAHrlhtvqNVDQVLVL 675
Cdd:TIGR01184 153 lqEELMQIWEEHR-VTVLMVTH------DVDEALLL 181
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
220-415 |
9.67e-18 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 84.42 E-value: 9.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 220 RINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLD 299
Cdd:cd18549 72 RIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFAL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 300 LPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERcrqlwwrrdleralYLAI 379
Cdd:cd18549 152 LPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDR--------------FLES 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 528078492 380 R----RVMAL---GM-------QVLILNCGVQQILAGEVTRGGLLSFLLY 415
Cdd:cd18549 218 KkkayKAMAYffsGMnfftnllNLVVLVAGGYFIIKGEITLGDLVAFLLY 267
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
486-681 |
9.84e-18 |
|
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: 82.42 E-value: 9.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQyDHHYLHRQVVLVGQEPVLfsgsvkDNIA 565
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV------DDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 566 YGLKDCEDAQVMAAVRAACADDFIGEMPDGIhtEIGEKGSQLAV----GQKQRLAIARALVRNPRVLILDEATSALDSQC 641
Cdd:cd03265 89 TGWENLYIHARLYGVPGAERRERIDELLDFV--GLLEAADRLVKtysgGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 528078492 642 EqaLQAWR------SKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:cd03265 167 R--AHVWEyieklkEEFGMTILLTTHYMEEAEQLcDRVAIIDHGRII 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
468-681 |
1.09e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.88 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 -LVGQEP-VLFSG-SVKDNIAYGLKD-C-EDAQVMAAVRAACADdfigempDGIHTEIGEKGSQLAVGQKQRLAIARALV 622
Cdd:PRK13644 80 gIVFQNPeTQFVGrTVEEDLAFGPENlClPPIEIRKRVDRALAE-------IGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528078492 623 RNPRVLILDEATSALDSQCEQA----LQAWRSKGdRTVLVIAHRLHTVQNVDQVLVLKQGQLV 681
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAvlerIKKLHEKG-KTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
459-682 |
1.21e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.61 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 459 LAPSRLEGRVEFQDVTFSYPSRP*---------KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGG---- 525
Cdd:PRK14271 1 MACERLGGQSGAADVDAAAPAMAAvnltlgfagKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrys 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 526 -QLLLDGQPLVQY-DHHYLHRQVVLVGQEPVLFSGSVKDNIAYGL---KDCEDAQVMAAVRAACADdfIGeMPDGIHTEI 600
Cdd:PRK14271 81 gDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVrahKLVPRKEFRGVAQARLTE--VG-LWDAVKDRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 601 GEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQAW-RSKGDR-TVLVIAHRLHTVQNV-DQVLVLKQ 677
Cdd:PRK14271 158 SDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFiRSLADRlTVIIVTHNLAQAARIsDRAALFFD 237
|
....*
gi 528078492 678 GQLVE 682
Cdd:PRK14271 238 GRLVE 242
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
478-695 |
1.53e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 84.37 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 478 PSRP*KPVlKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLH---RQVVLVGQEPv 554
Cdd:PRK15079 30 PPKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrSDIQMIFQDP- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 555 LFS----GSVKDNIAYGLK----DCEDAQVMAAVRAACADdfIGEMPDGIHTEIGEkgsqLAVGQKQRLAIARALVRNPR 626
Cdd:PRK15079 108 LASlnprMTIGEIIAEPLRtyhpKLSRQEVKDRVKAMMLK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 627 VLILDEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEhsqLREDQDVYAH 695
Cdd:PRK15079 182 LIICDEPVSALDvsiqAQVVNLLQQLQREMGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVE---LGTYDEVYHN 252
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
468-688 |
1.56e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 83.56 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSY-PSRP-*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLV--QYDHHYLH 543
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 544 RQVVLVGQEP--VLFSGSVKDNIAYGLKDC--EDAQVMAAVRAACA------DDFIGEMPdgihteigekgSQLAVGQKQ 613
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLglSEEEIENRVKRAMNivgldyEDYKDKSP-----------FELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 614 RLAIARALVRNPRVLILDEATSALDSQCEQAL----QAWRSKGDRTVLVIAHRLHTVQN-VDQVLVLKQGQLVEHSQLRE 688
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEIlnkiKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
468-688 |
1.60e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 83.73 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSY-PSRP*-KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHY---- 541
Cdd:PRK13641 3 IKFENVDYIYsPGTPMeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 542 LHRQVVLVGQ--EPVLFSGSVKDNIAYGLKD---CEDAQVMAAVRaacaddFIGEMpdGIHTEIGEKGS-QLAVGQKQRL 615
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgfSEDEAKEKALK------WLKKV--GLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 616 AIARALVRNPRVLILDEATSALDSQC-EQALQAWRS--KGDRTVLVIAHRLHTV-QNVDQVLVLKQGQLVEHSQLRE 688
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDyqKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKE 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
471-681 |
1.67e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.91 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 471 QDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVG 550
Cdd:PRK10575 15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 551 QE-PVLFSGSVKDNIA------------YGLKDCEdaQVMAAVRAACADDFIGEMPDgihteigekgsQLAVGQKQRLAI 617
Cdd:PRK10575 92 QQlPAAEGMTVRELVAigrypwhgalgrFGAADRE--KVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 618 ARALVRNPRVLILDEATSALD--SQCEQALQAWRSKGDRTVLVIAhRLHTV----QNVDQVLVLKQGQLV 681
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDiaHQVDVLALVHRLSQERGLTVIA-VLHDInmaaRYCDYLVALRGGEMI 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
469-692 |
2.30e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 86.32 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPS-RP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHR--- 544
Cdd:PRK10535 6 ELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 -QVVLVGQEPVLFSG-SVKDNIayglkdcEDAQVMAAV----RAACADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIA 618
Cdd:PRK10535 86 eHFGFIFQRYHLLSHlTAAQNV-------EVPAVYAGLerkqRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 619 RALVRNPRVLILDEATSALDSQCEQA----LQAWRSKGdRTVLVIAHRLHTVQNVDQVLVLKQGQLVEHSQLREDQDV 692
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEvmaiLHQLRDRG-HTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNV 233
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
475-681 |
2.32e-17 |
|
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: 82.00 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 475 FSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGqpLVQYDHH--YLHRQVVLVGQE 552
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRkkFLRRIGVVFGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 553 -------PVLFSGSVKDNIaYGLKDcedaqvmaaVRAACADDFIGEMPDgIHTEIGEKGSQLAVGQKQRLAIARALVRNP 625
Cdd:cd03267 104 tqlwwdlPVIDSFYLLAAI-YDLPP---------ARFKKRLDELSELLD-LEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528078492 626 RVLILDEATSALDSQCEQA----LQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENirnfLKEYNRERGTTVLLTSHYMKDIEALaRRVLVIDKGRLL 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
472-638 |
3.21e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 81.55 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 472 DVTFSYPSRP*kpvlkgLTFTLH--PGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQplvqyDHHYL---HRQV 546
Cdd:PRK10771 6 DITWLYHHLP-------MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppsRRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 547 VLVGQEPVLFSG-SVKDNIAYG------LKDCEDAQVMAAVRAACADDFIGEMPdgihteigekgSQLAVGQKQRLAIAR 619
Cdd:PRK10771 74 SMLFQENNLFSHlTVAQNIGLGlnpglkLNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALAR 142
|
170
....*....|....*....
gi 528078492 620 ALVRNPRVLILDEATSALD 638
Cdd:PRK10771 143 CLVREQPILLLDEPFSALD 161
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
485-686 |
3.77e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.40 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQ-----------------YDHHYLhrqvv 547
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakaelrnqklgfiYQFHHL----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 lvgqepvLFSGSVKDNIAYGLkdcedaqVMAAVRAACADDFIGEM--PDGIHTEIGEKGSQLAVGQKQRLAIARALVRNP 625
Cdd:PRK11629 99 -------LPDFTALENVAMPL-------LIGKKKPAEINSRALEMlaAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 626 RVLILDEATSALDSQCE----QALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEHSQL 686
Cdd:PRK11629 165 RLVLADEPTGNLDARNAdsifQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
468-688 |
4.58e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 82.38 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSY-PSRP-*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLV----QYDHHY 541
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 542 LHRQVVLVGQ--EPVLFSGSVKDNIAYGLKDC----EDAQVMAAvraacaddfigEMPD--GIHTEIGEKGS-QLAVGQK 612
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFgvseEDAKQKAR-----------EMIElvGLPEELLARSPfELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 613 QRLAIARALVRNPRVLILDEATSALDSQCEQAL-----QAWRSKGDRTVLViAHRLHTVQN-VDQVLVLKQGQLVEHSQL 686
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMmemfyKLHKEKGLTTVLV-THSMEDAARyADQIVVMHKGTVFLQGTP 230
|
..
gi 528078492 687 RE 688
Cdd:PRK13634 231 RE 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
479-640 |
5.68e-17 |
|
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: 79.71 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 479 SRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYlHRQVVLVGQEPVLFSG 558
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 -SVKDNIAYGLKDCEDAQVMA--AVRAACADDFigempdgIHTEIGekgsQLAVGQKQRLAIARALVRNPRVLILDEATS 635
Cdd:TIGR01189 88 lSALENLHFWAAIHGGAQRTIedALAAVGLTGF-------EDLPAA----QLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
....*
gi 528078492 636 ALDSQ 640
Cdd:TIGR01189 157 ALDKA 161
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
220-417 |
8.12e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 81.37 E-value: 8.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 220 RINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLD 299
Cdd:cd18550 69 GVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 300 LPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVRE--AVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLE-RALY 376
Cdd:cd18550 149 LPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAgRWFF 228
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 528078492 377 LAIRRVMALGmQVLILNCGVQQILAGEVTRGGLLSFLLYQE 417
Cdd:cd18550 229 AALGLFTAIG-PALVYWVGGLLVIGGGLTIGTLVAFTALLG 268
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
483-682 |
9.19e-17 |
|
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: 79.11 E-value: 9.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNL--YQPTGGQLLLDGQPLVQYDHHYLHRQVVLVG-QEPVLFSGs 559
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFLAfQYPPEIPG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 560 VKDNiayglkdcedaqvmaavraacadDFIGEMPDGihteigekgsqLAVGQKQRLAIARALVRNPRVLILDEATSALD- 638
Cdd:cd03217 92 VKNA-----------------------DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDi 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 528078492 639 ---SQCEQALQAWRSKGdRTVLVIAH--RLHTVQNVDQVLVLKQGQLVE 682
Cdd:cd03217 138 dalRLVAEVINKLREEG-KSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
468-675 |
1.10e-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: 77.96 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLlldgqplvqydHHYLHRQVV 547
Cdd:cd03223 1 IELENLSLATPDG--RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSGSVKDNIAYGLKDcedaqvmaavraacaddfigempdgihteigekgsQLAVGQKQRLAIARALVRNPRV 627
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPWDD-----------------------------------VLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 528078492 628 LILDEATSALDSQCEQAL-QAWRSKGdRTVLVIAHRLHTVQNVDQVLVL 675
Cdd:cd03223 113 VFLDEATSALDEESEDRLyQLLKELG-ITVISVGHRPSLWKFHDRVLDL 160
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
485-695 |
2.38e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.66 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLL-------DGQPLVQYDHHY---------LHRQVVL 548
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdKKNNHELITNPYskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 549 VGQEP--VLFSGSVKDNIAYG---LKDC-EDAQVMAA---VRAACADDFIGEMPDGihteigekgsqLAVGQKQRLAIAR 619
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFGpvaLGVKkSEAKKLAKfylNKMGLDDSYLERSPFG-----------LSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 620 ALVRNPRVLILDEATSALDSQCEQALQAW---RSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLRE---DQDV 692
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLildAKANNKTVFVITHTMEHVLEVaDEVIVMDKGKILKTGTPYEiftDQHI 269
|
...
gi 528078492 693 YAH 695
Cdd:PRK13631 270 INS 272
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
483-682 |
2.60e-16 |
|
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: 78.84 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPL--QNLYQPTGGQLLLDGQPLVQYD-HHYLHRQVVLVGQEPVLFSG- 558
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEpDERARAGLFLAFQYPEEIPGv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 SVKDNIAYGLKdcedaqvmaAVRAACADDFIgEMPDgIHTEIGEKGSQLAV---------------GQKQRLAIARALVR 623
Cdd:TIGR01978 93 SNLEFLRSALN---------ARRSARGEEPL-DLLD-FEKLLKEKLALLDMdeeflnrsvnegfsgGEKKRNEILQMALL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 624 NPRVLILDEATSALDSQ-----CEQaLQAWRSKgDRTVLVIAH--RLHTVQNVDQVLVLKQGQLVE 682
Cdd:TIGR01978 162 EPKLAILDEIDSGLDIDalkivAEG-INRLREP-DRSFLIITHyqRLLNYIKPDYVHVLLDGRIVK 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
485-681 |
2.80e-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: 78.47 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKST----VAAPLQNLYQpTGGQLLLDGQPLvqyDHHYLHRQVVLVGQEPVLFSG-S 559
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPR---KPDQFQKCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 560 VKDNIAYGL--------KDCEDAQVMAAVR-AACADDFIGempdgihteiGEKGSQLAVGQKQRLAIARALVRNPRVLIL 630
Cdd:cd03234 98 VRETLTYTAilrlprksSDAIRKKRVEDVLlRDLALTRIG----------GNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 631 DEATSALDSQceQALQAWR-----SKGDRTVLVIAH--RLHTVQNVDQVLVLKQGQLV 681
Cdd:cd03234 168 DEPTSGLDSF--TALNLVStlsqlARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
468-681 |
3.30e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.78 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSY-PSRP-*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLdGQPLV-----QYDHH 540
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVsstskQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 541 YLHRQVVLVGQEP--VLFSGSVKDNIAYGLKDC----EDAQVMAAVRAacaddfigEMPdGIHTEIGEKGS-QLAVGQKQ 613
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFgipkEKAEKIAAEKL--------EMV-GLADEFWEKSPfELSGGQMR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 614 RLAIARALVRNPRVLILDEATSALDSQCE-QALQAWRS--KGDRTVLVIAHRLHTVQN-VDQVLVLKQGQLV 681
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKARiEMMQLFESihQSGQTVVLVTHLMDDVADyADYVYLLEKGHII 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
489-681 |
3.83e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.44 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 489 LTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYqPTGGQLLLDGQPLVQYDHHYL-HRQVVLVGQEPVLFSGSVKDNIAYG 567
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 568 LKD-CEDAQVMAAVRAACadDFIGeMPDGIHTEIGekgsQLAVGQKQRLAIARALVR-----NP--RVLILDEATSALDS 639
Cdd:PRK03695 94 QPDkTRTEAVASALNEVA--EALG-LDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 528078492 640 QCEQAL----QAWRSKGdRTVLVIAHRL-HTVQNVDQVLVLKQGQLV 681
Cdd:PRK03695 167 AQQAALdrllSELCQQG-IAVVMSSHDLnHTLRHADRVWLLKQGKLL 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
476-632 |
3.87e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.53 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 476 SYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKST-----VaaplqNLYQPTGGQLLLDGQPLVQYDHH--------YL 542
Cdd:COG1137 12 SYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTtfymiV-----GLVKPDSGRIFLDGEDITHLPMHkrarlgigYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 543 hrqvvlvGQEPVLFSG-SVKDNIAYGLkdcEDAQVMAAVRAACADDFIGEMpdGIhTEIGE-KGSQLAVGQKQRLAIARA 620
Cdd:COG1137 84 -------PQEASIFRKlTVEDNILAVL---ELRKLSKKEREERLEELLEEF--GI-THLRKsKAYSLSGGERRRVEIARA 150
|
170
....*....|..
gi 528078492 621 LVRNPRVLILDE 632
Cdd:COG1137 151 LATNPKFILLDE 162
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
152-415 |
4.16e-16 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 79.46 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 152 LMVAFFFLAWAVLGETLIPHYSGRVID--ILGSDFDP*SFASAIFfmcLFSVGssLSAGCRGGSFLFTMS---RINLRIR 226
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDsgVRAGDLGVLLLAAAAY---LAVVL--AGWVAQRAQTRLTGRtgeRLLYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 227 ERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAA 306
Cdd:cd18546 76 LRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 307 EKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLwwRRDLER--ALYLAIRRVMA 384
Cdd:cd18546 156 TRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDA--RLRAQRlvAIYFPGVELLG 233
|
250 260 270
....*....|....*....|....*....|.
gi 528078492 385 LGMQVLILNCGVQQILAGEVTRGGLLSFLLY 415
Cdd:cd18546 234 NLATAAVLLVGAWRVAAGTLTVGVLVAFLLY 264
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
467-682 |
4.64e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 81.94 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 467 RVEFQDVTFSYPSRP*KpvLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYD-HHYLHrq 545
Cdd:PRK10522 322 TLELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQpEDYRK-- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 546 vvlvgqepvLFSGSVKDniaYGLKDcedaQVMA----AVRAACADDFIG--EMPDGIHTEIGE-KGSQLAVGQKQRLAIA 618
Cdd:PRK10522 398 ---------LFSAVFTD---FHLFD----QLLGpegkPANPALVEKWLErlKMAHKLELEDGRiSNLKLSKGQKKRLALL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 619 RALVRNPRVLILDEATSALDSQCEQA-----LQAWRSKGdRTVLVIAHRLHTVQNVDQVLVLKQGQLVE 682
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPHFRREfyqvlLPLLQEMG-KTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
486-669 |
4.83e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 78.67 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQ--PTG---GQLLLDGQPLvqYDHHY----LHRQVVLVGQEPVLF 556
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNL--YAPDVdpveVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 557 SGSVKDNIAYG-----LKDCEDAQVMAAVRAACADDfigEMPDgihtEIGEKGSQLAVGQKQRLAIARALVRNPRVLILD 631
Cdd:PRK14243 104 PKSIYDNIAYGaringYKGDMDELVERSLRQAALWD---EVKD----KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 528078492 632 EATSALDS----QCEQALQAWrsKGDRTVLVIAHRLHTVQNV 669
Cdd:PRK14243 177 EPCSALDPistlRIEELMHEL--KEQYTIIIVTHNMQQAARV 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
468-683 |
4.83e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.20 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:COG4604 2 IEIKNVSKRYGG---KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVLFSG-SVKDNIAYG--------LKDCEDAQVMAAVR----AACADDFIGEmpdgihteigekgsqLAVGQKQR 614
Cdd:COG4604 79 ILRQENHINSRlTVRELVAFGrfpyskgrLTAEDREIIDEAIAyldlEDLADRYLDE---------------LSGGQRQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 615 LAIARALVRNPRVLILDEATSALD-SQCEQALQAWRSKGD---RTVLVIAHRLhtvqNV-----DQVLVLKQGQLVEH 683
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMMKLLRRLADelgKTVVIVLHDI----NFascyaDHIVAMKDGRVVAQ 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
468-681 |
5.82e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.61 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHH---YLHR 544
Cdd:PRK10908 2 IRFEHVSKAYLG--GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVGQEP-VLFSGSVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGIHTEIgekgsQLAVGQKQRLAIARALVR 623
Cdd:PRK10908 80 QIGMIFQDHhLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPI-----QLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 624 NPRVLILDEATSALDSQCEQALQAWRSKGDR---TVLVIAHRLHTVQNVD-QVLVLKQGQLV 681
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
468-678 |
9.47e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.89 E-value: 9.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTfsypsrp*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:PRK09536 11 VEFGDTT----------VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEPVL-FSGSVKDNIAYG----------LKDCEDAQVMAAVRAACADDFIGEMPDgihteigekgsQLAVGQKQRLA 616
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMGrtphrsrfdtWTETDRAAVERAMERTGVAQFADRPVT-----------SLSGGERQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 617 IARALVRNPRVLILDEATSALD-SQCEQALQAWRSKGD--RTVLVIAHRLH-TVQNVDQVLVLKQG 678
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDiNHQVRTLELVRRLVDdgKTAVAAIHDLDlAARYCDELVLLADG 215
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
468-679 |
1.02e-15 |
|
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: 74.41 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTvaaplqnlyqptggqlLLDgqplvqydhhylhrqvV 547
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKST----------------LLK----------------L 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVGQEpVLFSGSVKdniayglkdcedaqVMAAVRaacaddfIGEMPdgihteigekgsQLAVGQKQRLAIARALVRNPRV 627
Cdd:cd03221 46 IAGEL-EPDEGIVT--------------WGSTVK-------IGYFE------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 628 LILDEATSALD----SQCEQALQAWRskgdRTVLVIAHRLHTVQNV-DQVLVLKQGQ 679
Cdd:cd03221 92 LLLDEPTNHLDlesiEALEEALKEYP----GTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
468-638 |
1.04e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.12 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRp*KPVLKGLTFTLHPGKVTALVGPNGSGKST----VAAplqnLYQPTGGQLLLDGQPLVQYDHHylH 543
Cdd:PRK11650 4 LKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTllrmVAG----LERITSGEIWIGGRVVNELEPA--D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 544 RQVVLVGQEPVLFSG-SVKDNIAYGLKD--CEDAQVMAAVRAACADDFIGEMPDgihteigEKGSQLAVGQKQRLAIARA 620
Cdd:PRK11650 76 RDIAMVFQNYALYPHmSVRENMAYGLKIrgMPKAEIEERVAEAARILELEPLLD-------RKPRELSGGQRQRVAMGRA 148
|
170
....*....|....*...
gi 528078492 621 LVRNPRVLILDEATSALD 638
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLD 166
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
217-427 |
1.54e-15 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 77.84 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 217 TMSRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYN-ANILLRSLVKVIGLyCFMLQVSPRLTFL 295
Cdd:cd18554 73 IANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGlMNIWLDMITIIIAI-CIMLVLNPKLTFV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 296 SLLDLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERAL 375
Cdd:cd18554 152 SLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAK 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 528078492 376 YLAIRRVMALGMQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLV 427
Cdd:cd18554 232 TFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLV 283
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
468-677 |
3.68e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.92 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV 547
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 L---VGQEPVLFSGSVKDNIAYGLKDCEDAQVMAAvraacaddfigempdgihteigeKGSQLAVGQKQRLAIARALVRN 624
Cdd:PRK09544 82 LpltVNRFLRLRPGTKKEDILPALKRVQAGHLIDA-----------------------PMQKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 625 PRVLILDEATSALDSQCEQAL----QAWRSKGDRTVLVIAHRLHTVQ-NVDQVLVLKQ 677
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHDLHLVMaKTDEVLCLNH 196
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
192-360 |
4.45e-15 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 76.55 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 192 AIFFMCLfSVGSSLSAGCRGGSFLFTMSRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANIL 271
Cdd:cd18558 62 AYYYLII-GAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 272 LRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQE 351
Cdd:cd18558 141 FQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKE 220
|
....*....
gi 528078492 352 VSRYKEALE 360
Cdd:cd18558 221 ETRYAQNLE 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
486-679 |
4.69e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.43 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYqPTG---GQLLLDGQPLVQY---DHHylHRQVVLVGQEPVLFSG- 558
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASnirDTE--RAGIAIIHQELALVKEl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 SVKDNIAYGlKDCEDAQVM--AAVRAACaDDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSA 636
Cdd:PRK13549 98 SVLENIFLG-NEITPGGIMdyDAMYLRA-QKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 528078492 637 L-DSQCEQAL---QAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQ 679
Cdd:PRK13549 174 LtESETAVLLdiiRDLKAHG-IACIYISHKLNEVKAIsDTICVIRDGR 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
443-681 |
5.10e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 443 VFCYIDRKPNLPQPGTLAP--SRLEGRVEFQdvtfsypsRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNlY 520
Cdd:TIGR00955 4 SWRNSDVFGRVAQDGSWKQlvSRLRGCFCRE--------RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 521 QPTG----GQLLLDGQPLVQYDHH----YLHRQVVLVG----QEPVLFSGSVKdniayglkdcEDAQVMAAVRAACADDF 588
Cdd:TIGR00955 75 SPKGvkgsGSVLLNGMPIDAKEMRaisaYVQQDDLFIPtltvREHLMFQAHLR----------MPRRVTKKEKRERVDEV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 589 IGEMP--DGIHTEIGEKGSQ--LAVGQKQRLAIARALVRNPRVLILDEATSALDS----QCEQALQAWRSKGdRTVLVIA 660
Cdd:TIGR00955 145 LQALGlrKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSfmaySVVQVLKGLAQKG-KTIICTI 223
|
250 260
....*....|....*....|...
gi 528078492 661 HR--LHTVQNVDQVLVLKQGQLV 681
Cdd:TIGR00955 224 HQpsSELFELFDKIILMAEGRVA 246
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
146-412 |
5.63e-15 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 76.09 E-value: 5.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 146 RPDLPFLMVAFFFLAwavLGETLIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRGGSFLFTMSRINLRI 225
Cdd:cd18782 1 RRALIEVLALSFVVQ---LLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 226 RERLFSSLLRQDLGFFQENKTGELNSRLsSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIA 305
Cdd:cd18782 78 GGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 306 AEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMAL 385
Cdd:cd18782 157 LTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNK 236
|
250 260
....*....|....*....|....*..
gi 528078492 386 GMQVLILNCGVQQILAGEVTRGGLLSF 412
Cdd:cd18782 237 LSSLLVLWVGAYLVLRGELTLGQLIAF 263
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
458-699 |
6.10e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.41 E-value: 6.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 458 TLAPSRLEGrvefQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQY 537
Cdd:PRK10253 2 TESVARLRG----EQLTLGYGK---YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 538 DHHYLHRQVVLVGQEPVLFSG-SVKDNIAYG-----------LKDCEDAqVMAAVRAAcaddfigempdGIHTEIGEKGS 605
Cdd:PRK10253 75 ASKEVARRIGLLAQNATTPGDiTVQELVARGryphqplftrwRKEDEEA-VTKAMQAT-----------GITHLADQSVD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 606 QLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQAWRSKGDR----TVLVIAHRLH-TVQNVDQVLVLKQGQL 680
Cdd:PRK10253 143 TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRekgyTLAAVLHDLNqACRYASHLIALREGKI 222
|
250
....*....|....*....
gi 528078492 681 VEHSQLREdqDVYAHLVQQ 699
Cdd:PRK10253 223 VAQGAPKE--IVTAELIER 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
483-701 |
8.61e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.82 E-value: 8.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVA-APLQNLYQP----TGGQLLLDGQPLVQYDHHYLHR----QVVLVGQEP 553
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 554 VLfSGSVKDNIAYGLkdcedAQVMAAVRAACADDFIGEMPD-----GIH---TEIGEKGSQLAVGQKQRLAIARALVRNP 625
Cdd:PRK15134 102 MV-SLNPLHTLEKQL-----YEVLSLHRGMRREAARGEILNcldrvGIRqaaKRLTDYPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 626 RVLILDEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLREDQDVYAHLVQQR 700
Cdd:PRK15134 176 ELLIADEPTTALDvsvqAQILQLLRELQQELNMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQNRAATLFSAPTHPYTQK 255
|
.
gi 528078492 701 L 701
Cdd:PRK15134 256 L 256
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
468-685 |
8.80e-15 |
|
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: 74.39 E-value: 8.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrP*KPV--LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDH----HY 541
Cdd:COG4181 9 IELRGLTKTVGT-GAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdaraRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 542 LHRQVVLVGQ-EPVLFSGSVKDNIAY-----GLKDCED--AQVMAAV----RAacaddfiGEMPdgihteigekgSQLAV 609
Cdd:COG4181 88 RARHVGFVFQsFQLLPTLTALENVMLplelaGRRDARAraRALLERVglghRL-------DHYP-----------AQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 610 GQKQRLAIARALVRNPRVLILDEATSALDS----QCEQALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEHSQ 685
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAatgeQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
483-683 |
1.09e-14 |
|
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: 77.42 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKS-TVAAPLQNLYQP---TGGQLLLDGQPLVQYDHHYLHR----QVVLVGQEPV 554
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 555 -----LFSgsVKDNIAYGLkdcedaQVMAAVRAACADDFIGEMPD--GIH---TEIGEKGSQLAVGQKQRLAIARALVRN 624
Cdd:COG4172 103 tslnpLHT--IGKQIAEVL------RLHRGLSGAAARARALELLErvGIPdpeRRLDAYPHQLSGGQRQRVMIAMALANE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 625 PRVLILDEATSALD--SQCE-----QALQAWRSKGdrtVLVIAHRLHTVQNV-DQVLVLKQGQLVEH 683
Cdd:COG4172 175 PDLLIADEPTTALDvtVQAQildllKDLQRELGMA---LLLITHDLGVVRRFaDRVAVMRQGEIVEQ 238
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
456-679 |
1.17e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.23 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 456 PGTLAPsrlegrVEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLV 535
Cdd:PRK13537 2 PMSVAP------IDFRNVEKRYGD---KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 536 QYDHHYLHRqvvlVGQEPVLfsgsvkDNIAYGLKDCEDAQVMA---AVRAACADDFIGEMPD--GIHTEIGEKGSQLAVG 610
Cdd:PRK13537 73 SRARHARQR----VGVVPQF------DNLDPDFTVRENLLVFGryfGLSAAAARALVPPLLEfaKLENKADAKVGELSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 611 QKQRLAIARALVRNPRVLILDEATSALDSQCE----QALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQ 679
Cdd:PRK13537 143 MKRRLTLARALVNDPDVLVLDEPTTGLDPQARhlmwERLRSLLARG-KTILLTTHFMEEAERLcDRLCVIEEGR 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
454-678 |
1.30e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.64 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 454 PQPGTLAPSRlegrVEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQP 533
Cdd:PRK13536 32 SIPGSMSTVA----IDLAGVSKSYGD---KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 534 lVQYDHHYLHRQVVLVGQEPVL-FSGSVKDNIA-----YGLKDCEDAQVMAAVRaacadDFIgempdGIHTEIGEKGSQL 607
Cdd:PRK13536 105 -VPARARLARARIGVVPQFDNLdLEFTVRENLLvfgryFGMSTREIEAVIPSLL-----EFA-----RLESKADARVSDL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 608 AVGQKQRLAIARALVRNPRVLILDEATSALDSQCE----QALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQG 678
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHARhliwERLRSLLARG-KTILLTTHFMEEAERLcDRLCVLEAG 248
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
468-688 |
3.02e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.58 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSY---PSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHR 544
Cdd:PRK13633 5 IKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVV-LVGQEP--VLFSGSVKDNIAYGLKDcedaqvmaavraacaddfIGEMPDGIHTEIGEKGSQ-------------LA 608
Cdd:PRK13633 85 NKAgMVFQNPdnQIVATIVEEDVAFGPEN------------------LGIPPEEIRERVDESLKKvgmyeyrrhaphlLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 609 VGQKQRLAIARALVRNPRVLILDEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEHS 684
Cdd:PRK13633 147 GGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
....
gi 528078492 685 QLRE 688
Cdd:PRK13633 227 TPKE 230
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
478-681 |
1.09e-13 |
|
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: 70.37 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 478 PSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTG---GQLLLDGQPLVQYDHHYlHRQVVLVGQE-- 552
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKY-PGEIIYVSEEdv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 553 --PVLfsgSVKDNIAYGLKdcedaqvmaavraACADDFIgempdgihteigeKGsqLAVGQKQRLAIARALVRNPRVLIL 630
Cdd:cd03233 94 hfPTL---TVRETLDFALR-------------CKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 631 DEATSALDS----QCEQALQawrskgdrtvlVIAHRLHTVQNV-------------DQVLVLKQGQLV 681
Cdd:cd03233 143 DNSTRGLDSstalEILKCIR-----------TMADVLKTTTFVslyqasdeiydlfDKVLVLYEGRQI 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
475-678 |
1.20e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 74.95 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 475 FSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQplvqydhhylhrqVVLVGQEPV 554
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 555 LFSGSVKDNIAYGLKdCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEAT 634
Cdd:TIGR01271 498 IMPGTIKDNIIFGLS-YDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 528078492 635 SALDSQCEQAL-QAWRSK--GDRTVLVIAHRLHTVQNVDQVLVLKQG 678
Cdd:TIGR01271 577 THLDVVTEKEIfESCLCKlmSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
189-412 |
1.35e-13 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 72.09 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 189 FASAIFFMCLFSVGSSLSAGcrggSFLFTMS-RINLRIRERLFSSLLRQDLGFFQENKTGELNSRLsSDTSKMSRWLPYN 267
Cdd:cd18570 44 ISIGLILLYLFQSLLSYIRS----YLLLKLSqKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISST 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 268 A-NILLRSLVKVIGLyCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFG 346
Cdd:cd18570 119 TiSLFLDLLMVIISG-IILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLN 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 347 AEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQVLILNCGVQQILAGEVTRGGLLSF 412
Cdd:cd18570 198 AEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAF 263
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
473-691 |
1.45e-13 |
|
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: 71.81 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 473 VTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQplvqydhhylhrqVVLVGQE 552
Cdd:cd03291 40 LFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 553 PVLFSGSVKDNIAYGLKdCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDE 632
Cdd:cd03291 107 SWIMPGTIKENIIFGVS-YDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 633 ATSALDSQCE-QALQAWRSK--GDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEHSQLREDQD 691
Cdd:cd03291 186 PFGYLDVFTEkEIFESCVCKlmANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
486-690 |
1.58e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.67 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYqPTG---GQLLLDGQPlVQY----DHHylHRQVVLVGQE----PV 554
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEV-CRFkdirDSE--ALGIVIIHQElaliPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 555 LfsgSVKDNI-------AYGLKDCED-----AQVMAAVRaacaddfIGEMPDGIHTEIGekgsqlaVGQKQRLAIARALV 622
Cdd:NF040905 93 L---SIAENIflgneraKRGVIDWNEtnrraRELLAKVG-------LDESPDTLVTDIG-------VGKQQLVEIAKALS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528078492 623 RNPRVLILDEATSALDSQCEQAL----QAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLREDQ 690
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALldllLELKAQG-ITSIIISHKLNEIRRVaDSITVLRDGRTIETLDCRADE 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
481-701 |
1.62e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.88 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 481 P*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQP----TGGQLLLDGQPLVQYDHHylHRQVVLVGQEPVLF 556
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR--GRKIATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 557 SGSVKDNIAYGLKDC-------EDAQVMAAVRAACADDfigempdgIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLI 629
Cdd:PRK10418 92 FNPLHTMHTHARETClalgkpaDDATLTAALEAVGLEN--------AARVLKLYPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 630 LDEATSALD--SQCE-----QALQAWRSKGdrtVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLREDQDVYAHLVQQRL 701
Cdd:PRK10418 164 ADEPTTDLDvvAQARildllESIVQKRALG---MLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNAPKHAVTRSL 240
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
485-688 |
1.83e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.03 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQ-----PTGGQLLLDGQPLVQYDHHYLH--RQVVLVGQEPVLFS 557
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIEvrREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 558 G-SVKDNIAYGLK--------DCEDAQVMAAVRAACaddfigeMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVL 628
Cdd:PRK14267 99 HlTIYDNVAIGVKlnglvkskKELDERVEWALKKAA-------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 629 ILDEATSALD----SQCEQALqaWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEHSQLRE 688
Cdd:PRK14267 172 LMDEPTANIDpvgtAKIEELL--FELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRK 234
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
470-678 |
1.97e-13 |
|
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: 69.19 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 470 FQDVTFSYPS-RP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVaapLQNLYQPT-----GGQLLLDGQPLVQYdhhyLH 543
Cdd:cd03232 6 WKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTL---LDVLAGRKtagviTGEILINGRPLDKN----FQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 544 RQVVLVGQEPVLFSGS-VKDNIAYGlkdcedaqvmAAVRAacaddfigempdgihteigekgsqLAVGQKQRLAIARALV 622
Cdd:cd03232 79 RSTGYVEQQDVHSPNLtVREALRFS----------ALLRG------------------------LSVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 623 RNPRVLILDEATSALDSQCE----QALQAWRSKGdRTVLVIAHRLHTV--QNVDQVLVLKQG 678
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAynivRFLKKLADSG-QAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
486-681 |
2.99e-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: 72.55 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYqPTG---GQLLLDGQPLVQYDHHYLHRQ-VVLVGQEPVLFSG-SV 560
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 561 KDNIAYGLKDCEDAQVMA------AVRAACADDFIGEMPDGIHTeigekgSQLAVGQKQRLAIARALVRNPRVLILDEAT 634
Cdd:TIGR02633 96 AENIFLGNEITLPGGRMAynamylRAKNLLRELQLDADNVTRPV------GDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 528078492 635 SAL-DSQCEQALQAWRSKGDRTV--LVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:TIGR02633 170 SSLtEKETEILLDIIRDLKAHGVacVYISHKLNEVKAVcDTICVIRDGQHV 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
480-682 |
5.21e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 5.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 480 RP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDhhylhRQVV------------ 547
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRS-----RQVIelseqsaaqmrh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 -------LVGQEPV-----LFSgsVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMPDGiHTEIGEKGSQLAVGQKQRL 615
Cdd:PRK10261 101 vrgadmaMIFQEPMtslnpVFT--VGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQRV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 616 AIARALVRNPRVLILDEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVE 682
Cdd:PRK10261 178 MIAMALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMGVIFITHDMGVVAEIaDRVLVMYQGEAVE 249
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
485-682 |
8.93e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.84 E-value: 8.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQ----------PLVQYDHHYLH---RQVVLVGQ 551
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgQLKVADKNQLRllrTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 552 EPVLFSG-SVKDNIAYGlkdceDAQVMAAVRAACADDFIGEMPD-GI-HTEIGEKGSQLAVGQKQRLAIARALVRNPRVL 628
Cdd:PRK10619 100 HFNLWSHmTVLENVMEA-----PIQVLGLSKQEARERAVKYLAKvGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 629 ILDEATSALD----SQCEQALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVE 682
Cdd:PRK10619 175 LFDEPTSALDpelvGEVLRIMQQLAEEG-KTMVVVTHEMGFARHVsSHVIFLHQGKIEE 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
466-698 |
1.00e-12 |
|
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: 69.11 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 466 GRVEFQDVTFSYpSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTV-AAPLQNLYqpTGGQLLLDG-----QPLVQYdh 539
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDGvswnsVPLQKW-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 540 hylHRQVVLVGQEPVLFSGSVKDNI-AYGlkDCEDAQVMAAVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIA 618
Cdd:cd03289 76 ---RKAFGVIPQKVFIFSGTFRKNLdPYG--KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 619 RALVRNPRVLILDEATSALDSQCEQALQAW--RSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLVEHSQLREDQDVYAHL 696
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTlkQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
..
gi 528078492 697 VQ 698
Cdd:cd03289 231 KQ 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
479-640 |
1.06e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.52 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 479 SRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYlHRQVVLVGQEPvlfsg 558
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHQP----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 SVKD--------NIAYGLKDCEDAQVMAAVRAAcaddfigempdgihteIGEKG------SQLAVGQKQRLAIARALVRN 624
Cdd:PRK13538 84 GIKTeltalenlRFYQRLHGPGDDEALWEALAQ----------------VGLAGfedvpvRQLSAGQQRRVALARLWLTR 147
|
170
....*....|....*.
gi 528078492 625 PRVLILDEATSALDSQ 640
Cdd:PRK13538 148 APLWILDEPFTAIDKQ 163
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
483-680 |
1.10e-12 |
|
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: 71.97 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPlVQYDHHYLHRQVVLVGQEPVLFSG-SVK 561
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD-IETNLDAVRQSLGMCPQHNILFHHlTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 562 DNIAYGL----KDCEDAQVmaAVRAACADdfigempDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSAL 637
Cdd:TIGR01257 1022 EHILFYAqlkgRSWEEAQL--EMEAMLED-------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 528078492 638 DSQCEQALqaW----RSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQL 680
Cdd:TIGR01257 1093 DPYSRRSI--WdlllKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRL 1138
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
483-682 |
1.25e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 68.28 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPL--QNLYQPTGGQLLLDGQPLVQYD-HHYLHRQVVLVGQEPVLFSG- 558
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVEIPGv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 SVKDNIAYGLKDCEDAQVMAAVRAACADDFIGE------MPDGIHTEIGEKGsqLAVGQKQRLAIARALVRNPRVLILDE 632
Cdd:PRK09580 94 SNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEkiallkMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 633 ATSALDSQC----EQALQAWRSkGDRTVLVIAH--RLHTVQNVDQVLVLKQGQLVE 682
Cdd:PRK09580 172 SDSGLDIDAlkivADGVNSLRD-GKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
177-362 |
1.57e-12 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 68.71 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 177 IDILGSDFDP*SFASAIFFM---CLFSVGSSLSAGCRGGSFLFTMSRINLRIRERLFSSLLRQDLGFFQENKTGELNSRL 253
Cdd:cd18605 26 VSHSNNSFFNFINDSFNFFLtvyGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 254 SSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPrltFLSLLDLPLTIAAEKVYNP-RHQAVltEIQ--DATAKaGQ 330
Cdd:cd18605 106 SSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLP---WLLLLLLPLAFIYYRIQRYyRATSR--ELKrlNSVNL-SP 179
|
170 180 190
....*....|....*....|....*....|....*
gi 528078492 331 V---VREAVGGLQTVRSFGAEEQEVSRYKEALERC 362
Cdd:cd18605 180 LythFSETLKGLVTIRAFRKQERFLKEYLEKLENN 214
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
472-666 |
2.86e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 472 DVTFSYpsRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLhrqVVLVGQ 551
Cdd:PRK15056 11 DVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 552 E-------PVLfsgsVKDNIAYG---------LKDCEDAQVMAAVRAACaddfigEMPDGIHTEIGEkgsqLAVGQKQRL 615
Cdd:PRK15056 86 SeevdwsfPVL----VEDVVMMGryghmgwlrRAKKRDRQIVTAALARV------DMVEFRHRQIGE----LSGGQKKRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 616 AIARALVRNPRVLILDEATSALDSQCE----QALQAWRSKGdRTVLVIAHRLHTV 666
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEariiSLLRELRDEG-KTMLVSTHNLGSV 205
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
484-640 |
2.90e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 66.69 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 484 PVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLL--DGQP--LVQYDHH---YLHRQVV-LVGQ---- 551
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWvdLAQASPReilALRRRTIgYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 552 -----------EPVLFSGsvkdniayglkdcEDAQVmAAVRAAcaddfigEMPDgiHTEIGEKGSQLAV-----GQKQRL 615
Cdd:COG4778 105 iprvsaldvvaEPLLERG-------------VDREE-ARARAR-------ELLA--RLNLPERLWDLPPatfsgGEQQRV 161
|
170 180
....*....|....*....|....*
gi 528078492 616 AIARALVRNPRVLILDEATSALDSQ 640
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAA 186
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
154-415 |
3.19e-12 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 67.81 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 154 VAFFFLAWAVLGETLIPHYSGRVID--ILGSDFDP*SFASAIFFMC-LFSVGSSLSAGcrggsflFTMSRINLR----IR 226
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIIDegIANGDLSYILRTGLLMLLLaLLGLIAGILAG-------YFAAKASQGfgrdLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 227 ERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLpynaNILLRSLVK----VIGLYCFMLQVSPRLTFLSLLDLPL 302
Cdd:cd18548 76 KDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFV----MMLLRMLVRapimLIGAIIMAFRINPKLALILLVAIPI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 303 TIAAekVY------NPRHQAVlteiQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALErcrqlwwrrDLeRALY 376
Cdd:cd18548 152 LALV--VFlimkkaIPLFKKV----QKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKAND---------DL-TDTS 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 528078492 377 LAIRRVMALGMQV--LILNCGV--------QQILAGEVTRGGLLSFLLY 415
Cdd:cd18548 216 LKAGRLMALLNPLmmLIMNLAIvailwfggHLINAGSLQVGDLVAFINY 264
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
489-682 |
3.29e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 489 LTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQ---PLVQYDHHYLHRQVVLVGQEPVLF---SGSVKD 562
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYASldpRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 563 NI-----AYGLKDCEDAqvmaAVRAACADDFIGEMPDgihtEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSAL 637
Cdd:PRK10261 423 SImeplrVHGLLPGKAA----AARVAWLLERVGLLPE----HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 528078492 638 D----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNVD-QVLVLKQGQLVE 682
Cdd:PRK10261 495 DvsirGQIINLLLDLQRDFGIAYLFISHDMAVVERIShRVAVMYLGQIVE 544
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
472-688 |
3.98e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.83 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 472 DVTFSYPSRP*KPVlKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQP---TGGQLLLDGQPLVQYDHHYLHR---- 544
Cdd:PRK09473 19 RVTFSTPDGDVTAV-NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKlrae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVGQEPV------------------LFSGSVKDNiAYGlkdcEDAQVMAAVRaacaddfigeMPDGiHTEIGEKGSQ 606
Cdd:PRK09473 98 QISMIFQDPMtslnpymrvgeqlmevlmLHKGMSKAE-AFE----ESVRMLDAVK----------MPEA-RKRMKMYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 607 LAVGQKQRLAIARALVRNPRVLILDEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHDLGVVAGIcDKVLVMYAGRTM 241
|
....*..
gi 528078492 682 EHSQLRE 688
Cdd:PRK09473 242 EYGNARD 248
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
479-681 |
6.14e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.60 E-value: 6.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 479 SRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPlVQY--DHHYLHRQVVLVGQE-PVL 555
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKE-IDFksSKEALENGISMVHQElNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 556 FSGSVKDNI---AYGLKDC-EDAQVMAAVRAACADDFigempdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILD 631
Cdd:PRK10982 86 LQRSVMDNMwlgRYPTKGMfVDQDKMYRDTKAIFDEL------DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 528078492 632 EATSAL-DSQCEQALQAWRSKGDR--TVLVIAHRLHTV-QNVDQVLVLKQGQLV 681
Cdd:PRK10982 160 EPTSSLtEKEVNHLFTIIRKLKERgcGIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
495-667 |
7.82e-12 |
|
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: 63.55 E-value: 7.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 495 PGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLlldgqplvqydhhylhrqvvlvgqepvlfsgsvkdniayglkdceda 574
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 575 qvmaaVRAACADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQA------- 647
Cdd:smart00382 34 -----IYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrll 108
|
170 180
....*....|....*....|..
gi 528078492 648 --WRSKGDRTVLVIAHRLHTVQ 667
Cdd:smart00382 109 llLKSEKNLTVILTTNDEKDLG 130
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
483-638 |
9.14e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.88 E-value: 9.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTvaapLQNL----YQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQEPVL--- 555
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAiagsLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 556 FSGSVKDN--IAY------GLKDCEDAQVMAAVRAACADDFIGeMPDGIHTEIGekgsQLAVGQKQRLAIARALVRNPRV 627
Cdd:COG1101 95 PSMTIEENlaLAYrrgkrrGLRRGLTKKRRELFRELLATLGLG-LENRLDTKVG----LLSGGQRQALSLLMATLTKPKL 169
|
170
....*....|.
gi 528078492 628 LILDEATSALD 638
Cdd:COG1101 170 LLLDEHTAALD 180
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
151-443 |
9.21e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 66.35 E-value: 9.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 151 FLMVAFFFLAWAVLgETLIPHYSGRVID--ILGSDFDp*SFASAIFFMCLFSVGSSLSagcrggSFLFTM------SRIN 222
Cdd:cd18540 4 LILLIILMLLVALL-DAVFPLLTKYAIDhfITPGTLD--GLTGFILLYLGLILIQALS------VFLFIRlagkieMGVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 223 LRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPL 302
Cdd:cd18540 75 YDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 303 tiaaekvynprhQAVLTEI-QDATAKAGQVVR-----------EAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRD 370
Cdd:cd18540 155 ------------LAVVSIYfQKKILKAYRKVRkinsritgafnEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAA 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 371 LERALYLAIrrVMALG--MQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMYGDMLSNVGAAEKV 443
Cdd:cd18540 223 RLSALFLPI--VLFLGsiATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
193-443 |
1.08e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 66.04 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 193 IFFMCLFSVGSSLSAGCRGGSFLFTMSRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSsDTSKMSRWLPYNA-NIL 271
Cdd:cd18568 45 LIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQ-ENQKIRRFLTRSAlTTI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 272 LRSLVKVIGLyCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQE 351
Cdd:cd18568 124 LDLLMVFIYL-GLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 352 VSRYKEALERCRQLWWR-RDLERALYLAIRRVMALGmQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGDYVRNLVYMY 430
Cdd:cd18568 203 RWRWENKFAKALNTRFRgQKLSIVLQLISSLINHLG-TIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLW 281
|
250
....*....|...
gi 528078492 431 GDMLSNVGAAEKV 443
Cdd:cd18568 282 DELQETRISVERL 294
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
483-680 |
1.26e-11 |
|
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: 63.99 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQ-VVLV----GQEPVLFS 557
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVpedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 558 GSVKDNIAYGlkdcedaqvmaavraacaddfigempdgihteigekgSQLAVGQKQRLAIARALVRNPRVLILDEATSAL 637
Cdd:cd03215 93 LSVAENIALS-------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 528078492 638 D----SQCEQALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQL 680
Cdd:cd03215 136 DvgakAEIYRLIRELADAG-KAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
485-683 |
2.02e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.53 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQ-----PLvqydHHYLHRQVVLVGQEPVLFSG- 558
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPL----HARARRGIGYLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 SVKDNIAYGLKDCEDaqVMAAVRAACADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALD 638
Cdd:PRK10895 94 SVYDNLMAVLQIRDD--LSAEQREDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 528078492 639 S----QCEQALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH 683
Cdd:PRK10895 170 PisviDIKRIIEHLRDSG-LGVLITDHNVRETLAVcERAYIVSQGHLIAH 218
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
151-447 |
2.05e-11 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 65.22 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 151 FLMVAFFFLAWAVLgeTLIPHYsgrVIDILGSDFDP*SFASAIFFM----CLFSVGSSLSAGCRGGSFLFTMSRINLRIR 226
Cdd:cd18580 1 VLLLLLLLLLLAFL--SQFSNI---WLDWWSSDWSSSPNSSSGYYLgvyaALLVLASVLLVLLRWLLFVLAGLRASRRLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 227 ERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAA 306
Cdd:cd18580 76 DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 307 EKVYnprhQAVLTEIQ--DATAKAG--QVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWrrdleraLYLAIRRV 382
Cdd:cd18580 156 QRYY----LRTSRQLRrlESESRSPlySHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFY-------LLLAVQRW 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 383 MALGMQVL--ILNCGV--------QQILAGEVtrgGL-LSFLLyqeEVGDYVRNLVYMYGDMLSNVGAAEKVFCYI 447
Cdd:cd18580 225 LGLRLDLLgaLLALVVallavllrSSISAGLV---GLaLTYAL---SLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
485-683 |
2.10e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 64.65 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQplvQYDHHY---------LHRQVVLVGQE--- 552
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDFSKtpsdkaireLRRNVGMVFQQynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 553 -PVLfsgSVKDNI------AYGL-KDCEDAQVMAAVRAACADDFIGEMPdgihteigekgSQLAVGQKQRLAIARALVRN 624
Cdd:PRK11124 94 wPHL---TVQQNLieapcrVLGLsKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 625 PRVLILDEATSALD----SQCEQALQAWRSKGDRTVLViAHRLHTVQNV-DQVLVLKQGQLVEH 683
Cdd:PRK11124 160 PQVLLFDEPTAALDpeitAQIVSIIRELAETGITQVIV-THEVEVARKTaSRVVYMENGHIVEQ 222
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
168-412 |
2.23e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 65.22 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 168 LIPHYSGRVID--ILGSDFDP*S-FASAIFFMCLFSVGSSLSagcRGGSFLFTMSRINLRIRERLFSSLLRQDLGFFQEN 244
Cdd:cd18555 20 LIPILTQYVIDnvIVPGNLNLLNvLGIGILILFLLYGLFSFL---RGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 245 KTGELNSRLSSdtskmsrwLPYNANILLRSLVK-------VIGLYCFMLQVSPRLTFLSLLdLPLTIAAEKVYNPR--HQ 315
Cdd:cd18555 97 SSGDLLFRANS--------NVYIRQILSNQVISliidlllLVIYLIYMLYYSPLLTLIVLL-LGLLIVLLLLLTRKkiKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 316 AVLTEIQdATAKAGQVVREAVGGLQTVRSFGAEEQevsRYKEALER-CRQLWWRRDLER--ALYLAIRRVMALGMQVLIL 392
Cdd:cd18555 168 LNQEEIV-AQTKVQSYLTETLYGIETIKSLGSEKN---IYKKWENLfKKQLKAFKKKERlsNILNSISSSIQFIAPLLIL 243
|
250 260
....*....|....*....|
gi 528078492 393 NCGVQQILAGEVTRGGLLSF 412
Cdd:cd18555 244 WIGAYLVINGELTLGELIAF 263
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
488-682 |
2.48e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.75 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 488 GLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLL--------------DGQPLVQYDHHYLHRQVVLVGQEP 553
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpDGRGRAKRYIGILHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 554 VLfsgsvkDNI--AYGLKDCEDAQVMAAVRAACADDFIGEMPDgihtEIGEK-GSQLAVGQKQRLAIARALVRNPRVLIL 630
Cdd:TIGR03269 382 VL------DNLteAIGLELPDELARMKAVITLKMVGFDEEKAE----EILDKyPDELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 631 DEATSALDS----QCEQALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVE 682
Cdd:TIGR03269 452 DEPTGTMDPitkvDVTHSILKAREEMEQTFIIVSHDMDFVLDVcDRAALMRDGKIVK 508
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
486-702 |
2.87e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPlVQYDH---------HYLHRQVVLVGQEpvlf 556
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE-VTFNGpkssqeagiGIIHQELNLIPQL---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 557 sgSVKDNIAYGLK-----DCEDAQVMAAVraacADDFIGEM--PDGIHTEIGEkgsqLAVGQKQRLAIARALVRNPRVLI 629
Cdd:PRK10762 95 --TIAENIFLGREfvnrfGRIDWKKMYAE----ADKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 630 LDEATSAL-DSQCEQ---ALQAWRSKGdRTVLVIAHRLHTV-QNVDQVLVLKQGQLV---EHSQLREDQdVYAHLVQQRL 701
Cdd:PRK10762 165 MDEPTDALtDTETESlfrVIRELKSQG-RGIVYISHRLKEIfEICDDVTVFRDGQFIaerEVADLTEDS-LIEMMVGRKL 242
|
.
gi 528078492 702 E 702
Cdd:PRK10762 243 E 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
483-662 |
4.09e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLY--QPTGGQLLLDGQPLvqydhhylHRQVVLVgqEPVLFSGSV 560
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF--------GREASLI--DAIGRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 561 KDNIAYgLKDC--EDAQVMAAvraacaddfigempdgihteigeKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALD 638
Cdd:COG2401 113 KDAVEL-LNAVglSDAVLWLR-----------------------RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180
....*....|....*....|....*....
gi 528078492 639 SQCEQAL-----QAWRSKGdRTVLVIAHR 662
Cdd:COG2401 169 RQTAKRVarnlqKLARRAG-ITLVVATHH 196
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
487-639 |
2.14e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.12 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 487 KGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLvqYDHHYLHRQVVLVGQEPVLFSG-SVKDNIA 565
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM--NDVPPAERGVGMVFQSYALYPHlSVAENMS 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 566 YGLKdcedaqvMAAVRAACADDFIGEMPDGIHTE--IGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDS 639
Cdd:PRK11000 98 FGLK-------LAGAKKEEINQRVNQVAEVLQLAhlLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
485-684 |
3.39e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.56 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHH----YLHRQVVLVGQEPVLFSgsv 560
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEarakLRAKHVGFVFQSFMLIP--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 561 kdniayGLKDCEDAQVMAAVRAAC-------ADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEA 633
Cdd:PRK10584 102 ------TLNALENVELPALLRGESsrqsrngAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 634 TSALDsqceqalqawRSKGDR--------------TVLVIAHRLHTVQNVDQVLVLKQGQLVEHS 684
Cdd:PRK10584 174 TGNLD----------RQTGDKiadllfslnrehgtTLILVTHDLQLAARCDRRLRLVNGQLQEEA 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
498-681 |
4.24e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.81 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 498 VTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVqyDHH---YL---HRQVVLVGQEPVLFSG-SVKDNIAYGlkd 570
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF--DAEkgiCLppeKRRIGYVFQDARLFPHyKVRGNLRYG--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 571 cedaqvMAAVRAACADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQAWRS 650
Cdd:PRK11144 101 ------MAKSMVAQFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 528078492 651 KGDRTV----LVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:PRK11144 173 RLAREInipiLYVSHSLDEILRLaDRVVVLEQGKVK 208
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
192-412 |
6.44e-10 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 60.98 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 192 AIFFMCLFSVGSSlsaGCRGGSFLFTMSRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSsDTSKMSRWLPYNANIL 271
Cdd:cd18588 47 GLLVVALFEAVLS---GLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARVR-ELESIRQFLTGSALTL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 272 LRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQE 351
Cdd:cd18588 123 VLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQF 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528078492 352 VSRYKEALerCRQLWWRRDLERALYLAIRRVMALG--MQVLILNCGVQQILAGEVTRGGLLSF 412
Cdd:cd18588 203 QRRWEELL--ARYVKASFKTANLSNLASQIVQLIQklTTLAILWFGAYLVMDGELTIGQLIAF 263
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
445-688 |
6.91e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.20 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 445 CYIDRKPNLPQPGTLAPSRLEGRVEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQP-- 522
Cdd:PLN03211 46 CYRVKFENMKNKGSNIKRILGHKPKISDETRQIQERT---ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnn 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 523 -TGGQLLLDGQPLVQydhhyLHRQVVLVGQEPVLFSG-SVKDNIAYGLKDCEDAQVMAAVRAACADDFIGEMpdGI---- 596
Cdd:PLN03211 123 fTGTILANNRKPTKQ-----ILKRTGFVTQDDILYPHlTVRETLVFCSLLRLPKSLTKQEKILVAESVISEL--GLtkce 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 597 HTEIGEKGSQ-LAVGQKQRLAIARALVRNPRVLILDEATSALDSQCE----QALQAWRSKGdRTVLVIAHRLHT--VQNV 669
Cdd:PLN03211 196 NTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyrlvLTLGSLAQKG-KTIVTSMHQPSSrvYQMF 274
|
250
....*....|....*....
gi 528078492 670 DQVLVLKQGQLVEHSQLRE 688
Cdd:PLN03211 275 DSVLVLSEGRCLFFGKGSD 293
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
466-634 |
6.98e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.96 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 466 GRvefqDVTFSYPSRP*K---PVL--KGLT---------FTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDG 531
Cdd:COG1129 238 GR----ELEDLFPKRAAApgeVVLevEGLSvggvvrdvsFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 532 QPLVQYD-HHYLHRQVVLV----GQEPVLFSGSVKDNIAYG-LKDCEDAQVM--AAVRAAcADDFIGEM---PDGIHTEI 600
Cdd:COG1129 314 KPVRIRSpRDAIRAGIAYVpedrKGEGLVLDLSIRENITLAsLDRLSRGGLLdrRRERAL-AEEYIKRLrikTPSPEQPV 392
|
170 180 190
....*....|....*....|....*....|....
gi 528078492 601 GekgsQLAVGQKQRLAIARALVRNPRVLILDEAT 634
Cdd:COG1129 393 G----NLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
485-681 |
7.56e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.89 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVVLVGQE--PVLFSGSVKD 562
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEgrRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 563 NIAYGLKDCEDAQVMAAVRAacaddfIGEMPDGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDS--- 639
Cdd:PRK11614 100 NLAMGGFFAERDQFQERIKW------VYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPiii 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 528078492 640 -QCEQALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQLV 681
Cdd:PRK11614 174 qQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
168-427 |
1.03e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 60.17 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 168 LIPHYSGRVID--ILGSDFDP*SFASAIFFM-CLFSVGSSLsagCRGGSFLFTMSRINLRIRERLFSSLLRQDLGFFQEN 244
Cdd:cd18567 20 ASPLYLQLVIDevIVSGDRDLLTVLAIGFGLlLLLQALLSA---LRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 245 KTGELNSRLSSdtskmsrwLPYNANILLRSLVK-------VIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKV-YNPRHQA 316
Cdd:cd18567 97 HLGDIVSRFGS--------LDEIQQTLTTGFVEalldglmAILTLVMMFLYSPKLALIVLAAVALYALLRLAlYPPLRRA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 317 VLTEIQdATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQVLILNCGV 396
Cdd:cd18567 169 TEEQIV-ASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGA 247
|
250 260 270
....*....|....*....|....*....|.
gi 528078492 397 QQILAGEVTRGGLLSFLLYQEEVGDYVRNLV 427
Cdd:cd18567 248 LLVLDGEFTVGMLFAFLAYKDQFSSRASSLI 278
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
469-678 |
1.06e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPSRP*KPV-LKGLTFTLHPGKVTALVGPNGSGKSTVaapLQNLYQP------TGGQLLLDGQPL---VQYD 538
Cdd:TIGR00956 761 HWRNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTTL---LNVLAERvttgviTGGDRLVNGRPLdssFQRS 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 539 HHYLHRQVVLVGQ----EPVLFSGSVKDNIAYGLKDcEDAQVMAAVRaacaddfIGEMPDGIHTEIGEKGSQLAVGQKQR 614
Cdd:TIGR00956 838 IGYVQQQDLHLPTstvrESLRFSAYLRQPKSVSKSE-KMEYVEEVIK-------LLEMESYADAVVGVPGEGLNVEQRKR 909
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 615 LAIARALVRNPRVLI-LDEATSALDSQceqalQAW------RSKGD--RTVLVIAHRLHTV--QNVDQVLVLKQG 678
Cdd:TIGR00956 910 LTIGVELVAKPKLLLfLDEPTSGLDSQ-----TAWsicklmRKLADhgQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
468-632 |
1.17e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.78 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSypsRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLH---R 544
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYtvrK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLVGQEPVLFSG-SVKDNIAYGLKdcEDAQ---------VMAAVRAACADDFIGEMPdgihteigekgSQLAVGQKQR 614
Cdd:PRK11831 85 RMSMLFQSGALFTDmNVFDNVAYPLR--EHTQlpapllhstVMMKLEAVGLRGAAKLMP-----------SELSGGMARR 151
|
170
....*....|....*...
gi 528078492 615 LAIARALVRNPRVLILDE 632
Cdd:PRK11831 152 AALARAIALEPDLIMFDE 169
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
479-683 |
1.32e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.46 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 479 SRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTV----AAPLQNLYQPTG----GQLLLDGQPLVQYDHHYLHR-QVVLV 549
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLlkalAGDLTGGGAPRGarvtGDVTLNGEPLAAIDAPRLARlRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 550 GQEPVLFSGSVKDNIAYGlkdcedaQVMAAVRAACADDFIGEMPD------GIHTEIGEKGSQLAVGQKQRLAIARAL-- 621
Cdd:PRK13547 90 QAAQPAFAFSAREIVLLG-------RYPHARRAGALTHRDGEIAWqalalaGATALVGRDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 622 -------VRNPRVLILDEATSALDSQCEQALQAWRSKGDRT----VLVIAHRLH-TVQNVDQVLVLKQGQLVEH 683
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnlgVLAIVHDPNlAARHADRIAMLADGAIVAH 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
471-681 |
1.43e-09 |
|
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: 61.10 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 471 QDVTFSYPsrP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLdgQPlvQYDHHYLHrqvvlvg 550
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--QP--GIKVGYLP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 551 QEPVL-FSGSVKDNIAYGLKDCEDAQV-MAAVRAACAD---DF------IGEMPDGIHTEIG-EKGSQLAV--------- 609
Cdd:TIGR03719 75 QEPQLdPTKTVRENVEEGVAEIKDALDrFNEISAKYAEpdaDFdklaaeQAELQEIIDAADAwDLDSQLEIamdalrcpp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 610 ----------GQKQRLAIARALVRNPRVLILDEATSALDSQC----EQALQawRSKGdrTVLVIAHRLHTVQNVDQ-VLV 674
Cdd:TIGR03719 155 wdadvtklsgGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQ--EYPG--TVVAVTHDRYFLDNVAGwILE 230
|
....*..
gi 528078492 675 LKQGQLV 681
Cdd:TIGR03719 231 LDRGRGI 237
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
466-682 |
1.48e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.64 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 466 GRVEFQDVTFSYPSR-P*K-PVLKGLTFTLHPGKVTALVGPNGSGKSTvaaplqnLYQPTGGQLLLD-GQPLV-QY---- 537
Cdd:PRK13645 5 KDIILDNVSYTYAKKtPFEfKALNNTSLTFKKNKVTCVIGTTGSGKST-------MIQLTNGLIISEtGQTIVgDYaipa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 538 ------DHHYLHRQVVLVGQEP--VLFSGSVKDNIAYGL----KDCEDA-----QVMAAVraACADDFIGEMPdgihtei 600
Cdd:PRK13645 78 nlkkikEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPvnlgENKQEAykkvpELLKLV--QLPEDYVKRSP------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 601 gekgSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQA-----LQAWRSKGDRTVLVIAHRLHTVQNVDQVLVL 675
Cdd:PRK13645 149 ----FELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDfinlfERLNKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
....*..
gi 528078492 676 KQGQLVE 682
Cdd:PRK13645 225 HEGKVIS 231
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
483-682 |
5.42e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQN--LYQPTGGQLLLDGQPLVQYD-HHYLHRQVVLVGQEPVLFSG- 558
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEpEERAHLGIFLAFQYPIEIPGv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 SVKD---------NIAYGLKDCEDAQVMAAVRAACadDFIGEMPDGIHTEIGEKGSQlavGQKQRLAIARALVRNPRVLI 629
Cdd:CHL00131 100 SNADflrlaynskRKFQGLPELDPLEFLEIINEKL--KLVGMDPSFLSRNVNEGFSG---GEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 630 LDEATSALDSqceQALQAWrSKG-------DRTVLVIAH--RLHTVQNVDQVLVLKQGQLVE 682
Cdd:CHL00131 175 LDETDSGLDI---DALKII-AEGinklmtsENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
485-681 |
9.82e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.40 E-value: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQ---LLLDGQPLVQYDHHY-------------------- 541
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEKEkvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 542 -LHRQVVLVGQ--EPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAAcadDFIgEMPdGIHTEIGEKGS-QLAVGQKQRLAI 617
Cdd:PRK13651 102 eIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAA---KYI-ELV-GLDESYLQRSPfELSGGQKRRVAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 618 ARALVRNPRVLILDEATSALDSQ-CEQALQAWRS--KGDRTVLVIAHRL-HTVQNVDQVLVLKQGQLV 681
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNlnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKII 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
468-697 |
1.63e-08 |
|
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: 57.50 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNL--YQPTGGQLL----------------L 529
Cdd:TIGR03269 1 IEVKNLTKKFDG---KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 530 DGQP--------------LVQYDHHY-----------LHRQVVLVGQEPVLfsgsvkDNIAYGLKDCEDAQVMAAVRAAc 584
Cdd:TIGR03269 78 VGEPcpvcggtlepeevdFWNLSDKLrrrirkriaimLQRTFALYGDDTVL------DNVLEALEEIGYEGKEAVGRAV- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 585 adDFIgEMPDGIHtEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQC----EQALQAWRSKGDRTVLVIA 660
Cdd:TIGR03269 151 --DLI-EMVQLSH-RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTaklvHNALEEAVKASGISMVLTS 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 528078492 661 HRLHTVQNV-DQVLVLKQGQLVEHSQLREDQDVYAHLV 697
Cdd:TIGR03269 227 HWPEVIEDLsDKAIWLENGEIKEEGTPDEVVAVFMEGV 264
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
490-663 |
3.35e-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: 55.07 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 490 TFTLH------PGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLllDGQPlvQYD-----------HHYLHR-------- 544
Cdd:cd03236 14 SFKLHrlpvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--DDPP--DWDeildefrgselQNYFTKllegdvkv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 --QVVLVGQEPVLFSGSVKDNIAYglKDCEDAQvmaavraacaDDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALV 622
Cdd:cd03236 90 ivKPQYVDLIPKAVKGKVGELLKK--KDERGKL----------DELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 528078492 623 RNPRVLILDEATSALDsqCEQALQAWR-----SKGDRTVLVIAHRL 663
Cdd:cd03236 156 RDADFYFFDEPSSYLD--IKQRLNAARlirelAEDDNYVLVVEHDL 199
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
479-638 |
4.72e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 479 SRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHhylHRQVVLVGQEPVLFSG 558
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR---SRFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 -SVKDNIAY--GLKDCEDAQvmaavraacaddfigeMPDGIHTEIGEKG------SQLAVGQKQRLAIARALVRNPRVLI 629
Cdd:PRK13543 97 lSTLENLHFlcGLHGRRAKQ----------------MPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWL 160
|
....*....
gi 528078492 630 LDEATSALD 638
Cdd:PRK13543 161 LDEPYANLD 169
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
483-662 |
5.66e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.80 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPlVQYDHHYLHRQVVLVGQE----PVLfsg 558
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS-IKKDLCTYQKQLCFVGHRsginPYL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 SVKDNIAYGLKDCEDA-QVMAAVRAACADDFIgEMPDGIhteigekgsqLAVGQKQRLAIARALVRNPRVLILDEATSAL 637
Cdd:PRK13540 90 TLRENCLYDIHFSPGAvGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180
....*....|....*....|....*....
gi 528078492 638 DSQCEQA----LQAWRSKGDrTVLVIAHR 662
Cdd:PRK13540 159 DELSLLTiitkIQEHRAKGG-AVLLTSHQ 186
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
485-684 |
6.66e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.39 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 485 VLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNlyQPTGG----QLLLDGQPLVQ--------Y-DHHYLHRQVVLVgQ 551
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyiegDIRISGFPKKQetfarisgYcEQNDIHSPQVTV-R 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 552 EPVLFSGSVKDNIAYGLKDCED--AQVMAAVRAACADDFIGEMP--DGIHTEigekgsqlavgQKQRLAIARALVRNPRV 627
Cdd:PLN03140 972 ESLIYSAFLRLPKEVSKEEKMMfvDEVMELVELDNLKDAIVGLPgvTGLSTE-----------QRKRLTIAVELVANPSI 1040
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 628 LILDEATSALDSQCEQ-ALQAWRSKGD--RTVLVIAHR--LHTVQNVDQVLVLKQGQLVEHS 684
Cdd:PLN03140 1041 IFMDEPTSGLDARAAAiVMRTVRNTVDtgRTVVCTIHQpsIDIFEAFDELLLMKRGGQVIYS 1102
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
486-681 |
6.73e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 54.71 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGqpLVQYDH--HYLHRQVVLVGQE-------PVLF 556
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVPFKRrkEFARRIGVVFGQRsqlwwdlPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 557 SGSVKDNIaYGLKDCEDAQVMaavraacaDDFIGEMpdgihtEIGEKGS----QLAVGQKQRLAIARALVRNPRVLILDE 632
Cdd:COG4586 116 SFRLLKAI-YRIPDAEYKKRL--------DELVELL------DLGELLDtpvrQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 528078492 633 ATSALD--SQCE--QALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:COG4586 181 PTIGLDvvSKEAirEFLKEYNRERGTTILLTSHDMDDIEALcDRVIVIDHGRII 234
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
489-662 |
7.22e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.91 E-value: 7.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 489 LTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYdhhylhrqvvlVGQEPVLFSGSVKDNIAYgl 568
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFY-----------VPQRPYMTLGTLRDQIIY-- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 569 KDCEDAQVMAAVRaacaDDFIGEMPDGIH-TEIGEKG----------SQLAVGQKQRLAIARALVRNPRVLILDEATSAL 637
Cdd:TIGR00954 538 PDSSEDMKRRGLS----DKDLEQILDNVQlTHILEREggwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180
....*....|....*....|....*.
gi 528078492 638 DSQCEQAL-QAWRSKGdRTVLVIAHR 662
Cdd:TIGR00954 614 SVDVEGYMyRLCREFG-ITLFSVSHR 638
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
467-696 |
7.56e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.25 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 467 RVEFQDVTFSYpsrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLY---QPTGGQLLLDGQPlVQYDHH--- 540
Cdd:PRK09984 6 RVEKLAKTFNQ-----HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRT-VQREGRlar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 541 ----------YLHRQVVLVGQEPVLfsgsvkDNIAYGLKDC-----------EDAQVMAAVRAACAddfIGeMPDGIHTE 599
Cdd:PRK09984 80 dirksrantgYIFQQFNLVNRLSVL------ENVLIGALGStpfwrtcfswfTREQKQRALQALTR---VG-MVHFAHQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 600 IgekgSQLAVGQKQRLAIARALVRNPRVLILDEATSALDSQCEQ----ALQAWRSKGDRTVLVIAHRL-HTVQNVDQVLV 674
Cdd:PRK09984 150 V----STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARivmdTLRDINQNDGITVVVTLHQVdYALRYCERIVA 225
|
250 260
....*....|....*....|...
gi 528078492 675 LKQGQLV-EHSQLREDQDVYAHL 696
Cdd:PRK09984 226 LRQGHVFyDGSSQQFDNERFDHL 248
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
491-683 |
7.75e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 7.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 491 FTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYL--HRQVVLVGQEpvlfSGSVKDNIAYGL 568
Cdd:PRK11701 27 FDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseAERRRLLRTE----WGFVHQHPRDGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 569 KDCEDA------QVMAA-------VRAAcADDFIGEMpdgihtEIG-----EKGSQLAVGQKQRLAIARALVRNPRVLIL 630
Cdd:PRK11701 103 RMQVSAggnigeRLMAVgarhygdIRAT-AGDWLERV------EIDaaridDLPTTFSGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 631 DEATSALDSQCeQA-----LQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQLVEH 683
Cdd:PRK11701 176 DEPTGGLDVSV-QArlldlLRGLVRELGLAVVIVTHDLAVARLLaHRLLVMKQGRVVES 233
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
445-638 |
9.11e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 9.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 445 CYIDRKPNLPQPGTLAPSRL------EGRVEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTvaaplqn 518
Cdd:PRK10938 232 AHSEQLEGVQLPEPDEPSARhalpanEPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKST------- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 519 lyqptggqlLLDgqpLVQYDH-HYLHRQVVLVGQEpvlfSGS------VKDNIAYGLKDCE-DAQVMAAVRAACADDF-- 588
Cdd:PRK10938 302 ---------LLS---LITGDHpQGYSNDLTLFGRR----RGSgetiwdIKKHIGYVSSSLHlDYRVSTSVRNVILSGFfd 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 589 -IG---EMPD-------------GIHTEIGEKGSQ-LAVGQkQRLA-IARALVRNPRVLILDEATSALD 638
Cdd:PRK10938 366 sIGiyqAVSDrqqklaqqwldilGIDKRTADAPFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
155-409 |
1.57e-07 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 53.66 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 155 AFFFLAWAVLGETLIPHYSGRVIDILgSDFDP*SFASAIFFM---CLFSVGSSLSAGCRggSFLFtmSRINLRIRERL-- 229
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDAL-SAPASALLAVPLLLLlayGLARILSSLFNELR--DALF--ARVSQRAVRRLal 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 230 --FSSLLRQDLGFFQENKTGELnsrlSSDTSKMSRWLPYNANILLRSLVKVI---GLYCFML--QVSPRLTFLSLLdlpl 302
Cdd:cd18582 76 rvFRHLHSLSLRFHLSRKTGAL----SRAIERGTRGIEFLLRFLLFNILPTIlelLLVCGILwyLYGWSYALITLV---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 303 TIAA---------EKVYNPRHQAVLTEiQDATAKAgqvvreaVGGLQ---TVRSFGAEEQEVSRYKEALERcrqlwwrrd 370
Cdd:cd18582 148 TVALyvaftikvtEWRTKFRREMNEAD-NEANAKA-------VDSLLnyeTVKYFNNEEYEAERYDKALAK--------- 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 528078492 371 LERALYLAIRRVMALGM-QVLILNCG--------VQQILAGEVTRGGL 409
Cdd:cd18582 211 YEKAAVKSQTSLALLNIgQALIISLGltaimllaAQGVVAGTLTVGDF 258
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
215-414 |
2.32e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 52.90 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 215 LFTMSRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSdTSKMSRWLpynANILLRSLVKVIGLYCF---MLQVSPR 291
Cdd:cd18783 67 LVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQ-IERIRQFL---TGQLFGTLLDATSLLVFlpvLFFYSPT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 292 LTFL----SLLDLPLTIAAEKVYNPRHQAVlteiQDATAKAGQVVREAVGGLQTVRSFgaeeqevsrykeALERCRqlww 367
Cdd:cd18783 143 LALVvlafSALIALIILAFLPPFRRRLQAL----YRAEGERQAFLVETVHGIRTVKSL------------ALEPRQ---- 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528078492 368 RRDLERALYLAIRRVMALG----------------MQVLILNCGVQQILAGEVTRGGLLSFLL 414
Cdd:cd18783 203 RREWDERVARAIRARFAVGrlsnwpqtltgpleklMTVGVIWVGAYLVFAGSLTVGALIAFNM 265
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
468-680 |
3.20e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQ-YDHHylHRQV 546
Cdd:PLN03073 509 ISFSDASFGYPGGPL--LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAvFSQH--HVDG 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 547 VLVGQEPVLFsgsvkdniaygLKDCEDAQVMAAVRAacaddFIGEMpdGIHTEIG-EKGSQLAVGQKQRLAIARALVRNP 625
Cdd:PLN03073 585 LDLSSNPLLY-----------MMRCFPGVPEQKLRA-----HLGSF--GVTGNLAlQPMYTLSGGQKSRVAFAKITFKKP 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 528078492 626 RVLILDEATSALDSQCEQALQAWRSKGDRTVLVIAHRLHTVQ-NVDQVLVLKQGQL 680
Cdd:PLN03073 647 HILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
484-638 |
3.27e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 484 PVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLqnlyqpTGGQLLLDGQplVQYDhhylhrQVVLVG---QEPVL-FSGS 559
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL------NGEVLLDDGR--IIYE------QDLIVArlqQDPPRnVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 560 VKDNIAYGLK------------------DCED------AQVMAAVRAACA---DDFIGEMPDGIHTEIGEKGSQLAVGQK 612
Cdd:PRK11147 83 VYDFVAEGIEeqaeylkryhdishlvetDPSEknlnelAKLQEQLDHHNLwqlENRINEVLAQLGLDPDAALSSLSGGWL 162
|
170 180
....*....|....*....|....*.
gi 528078492 613 QRLAIARALVRNPRVLILDEATSALD 638
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
463-646 |
3.86e-07 |
|
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: 53.40 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 463 RLEGRV-EFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLdGQPLvqydhhy 541
Cdd:TIGR03719 317 RLGDKViEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 542 lhrQVVLVGQ--EPVLFSGSVKDNIAYGLKDCEDAQVMAAVRAACAD-DFIGempdgihTEIGEKGSQLAVGQKQRLAIA 618
Cdd:TIGR03719 386 ---KLAYVDQsrDALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRfNFKG-------SDQQKKVGQLSGGERNRVHLA 455
|
170 180
....*....|....*....|....*...
gi 528078492 619 RALVRNPRVLILDEATSALDSQCEQALQ 646
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVETLRALE 483
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
495-663 |
3.96e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.25 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 495 PGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLllDGQPlvQYD-----------HHYLHR------QVVL----VGQEP 553
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEP--SWDevlkrfrgtelQDYFKKlangeiKVAHkpqyVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 554 VLFSGSVKDNiaygLKDCEDAQVmaavraacADDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEA 633
Cdd:COG1245 174 KVFKGTVREL----LEKVDERGK--------LDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....*
gi 528078492 634 TSALDsqCEQALQAWR-----SKGDRTVLVIAHRL 663
Cdd:COG1245 240 SSYLD--IYQRLNVARlirelAEEGKYVLVVEHDL 272
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
479-692 |
5.04e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 479 SRP*KPVL----------KGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYD-HHYLHRQVV 547
Cdd:PRK15439 262 QAAGAPVLtvedltgegfRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 LVG---QEPVLF---------SGSVKDNIAYGLKDCEDAQVMAAVRAACADDFigempdgihTEIGEKGSQLAVGQKQRL 615
Cdd:PRK15439 342 YLPedrQSSGLYldaplawnvCALTHNRRGFWIKPARENAVLERYRRALNIKF---------NHAEQAARTLSGGNQQKV 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 616 AIARALVRNPRVLILDEATSALDSQCEQAL-QAWRS--KGDRTVLVIAHRLHTV-QNVDQVLVLKQGQLvEHSQLREDQD 691
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIyQLIRSiaAQNVAVLFISSDLEEIeQMADRVLVMHQGEI-SGALTGAAIN 491
|
.
gi 528078492 692 V 692
Cdd:PRK15439 492 V 492
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
492-663 |
7.34e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 492 TLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLllDGQPlvQYD-----------HHYLHR------QVVL----VG 550
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--EEEP--SWDevlkrfrgtelQNYFKKlyngeiKVVHkpqyVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 551 QEPVLFSGSVKDNiaygLKDCEDAQVMaavraacaDDFIGEMpdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLIL 630
Cdd:PRK13409 171 LIPKVFKGKVREL----LKKVDERGKL--------DEVVERL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*
gi 528078492 631 DEATSALD-SQCEQALQAWRS-KGDRTVLVIAHRL 663
Cdd:PRK13409 237 DEPTSYLDiRQRLNVARLIRElAEGKYVLVVEHDL 271
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
192-413 |
8.06e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 51.39 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 192 AIFFMCLFSVGSSLsagCRGGSFLFTMSRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSdtskmsrwlpynaNIL 271
Cdd:cd18779 47 GLAALVLTQLLAGL---LRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSS-------------NAT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 272 LRSLVK------------VIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGL 339
Cdd:cd18779 111 IRELLTsqtlsalldgtlVLGYLALLFAQSPLLGLVVLGLAALQVALLLATRRRVRELMARELAAQAEAQSYLVEALSGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 340 QTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERALYLAIRRVMALGMQVLILNCGVQQILAGEVTRGGLLSFL 413
Cdd:cd18779 191 ETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALN 264
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
486-688 |
9.67e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.97 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQvvLVGQEPVLFSgsvkdNIA 565
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQ--LTGIENIEFK-----MLC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 566 YGLKDCEDAQVMAAVRAacaddfIGEMPDGIHTEIGEKGSqlavGQKQRLAIARALVRNPRVLILDEATSALDS----QC 641
Cdd:PRK13546 113 MGFKRKEIKAMTPKIIE------FSELGEFIYQPVKKYSS----GMRAKLGFSINITVNPDILVIDEALSVGDQtfaqKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 528078492 642 EQALQAWRSKgDRTVLVIAHRLHTVQN-VDQVLVLKQGQLVEHSQLRE 688
Cdd:PRK13546 183 LDKIYEFKEQ-NKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDD 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
476-681 |
1.04e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 476 SYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRQVV-------- 547
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVayipedrl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 ---LVGqepvlfSGSVKDNIAygLKDCEDAQV-------MAAVRAAcADDFIGEM---PDGIHTEIGekgsQLAVGQKQR 614
Cdd:COG3845 344 grgLVP------DMSVAENLI--LGRYRRPPFsrggfldRKAIRAF-AEELIEEFdvrTPGPDTPAR----SLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 615 LAIARALVRNPRVLILDEATSALD----SQCEQALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQLV 681
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLELRDAG-AAVLLISEDLDEILALsDRIAVMYEGRIV 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
460-661 |
1.25e-06 |
|
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: 51.71 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 460 APSRLEGR---VEFQDVTFSYPSrp*kpvlkgltFTL-------HPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLll 529
Cdd:COG1245 331 APRREKEEetlVEYPDLTKSYGG-----------FSLeveggeiREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 530 dgqplvqydhhylhrqvvlvgqepvlfSGSVKdnIAYG---LKDCEDAQVMAAVRAACADDFIGEM-------PDGIHtE 599
Cdd:COG1245 398 ---------------------------DEDLK--ISYKpqyISPDYDGTVEEFLRSANTDDFGSSYykteiikPLGLE-K 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 600 IGEKG-SQLAVGQKQRLAIARALVRNPRVLILDEATSALDSqcEQALQAWRS------KGDRTVLVIAH 661
Cdd:COG1245 448 LLDKNvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRLAVAKAirrfaeNRGKTAMVVDH 514
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
471-661 |
1.87e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 471 QDVTFSYPsrP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGqlllDGQPLVQYDHHYLHrqvvlvg 550
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG----EARPAPGIKVGYLP------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 551 QEPVL-FSGSVKDNIAYGLKDCEDAQ-----VMAAVrAACADDF------IGEMPDGI-HTEIGEKGSQLAV-------- 609
Cdd:PRK11819 77 QEPQLdPEKTVRENVEEGVAEVKAALdrfneIYAAY-AEPDADFdalaaeQGELQEIIdAADAWDLDSQLEIamdalrcp 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 610 -----------GQKQRLAIARALVRNPRVLILDEATSALDSQC----EQALQawRSKGdrTVLVIAH 661
Cdd:PRK11819 156 pwdakvtklsgGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlEQFLH--DYPG--TVVAVTH 218
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
168-389 |
2.36e-06 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 49.92 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 168 LIPHYSGRVIDIL--GSDFDP*SFASAIFFMCLFSVGSSLSAGCRGGSFLFTMSRINLRIRERLFSSLLRQDLGFFQENK 245
Cdd:cd18560 14 LAPLFLGRAVNALtlAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWHLSKK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 246 TGELNSRLSSDTSKMSRWL--------PYNANILLRSLVkviglycFMLQVSPRLTFLSLLDLPL-TIAAEKVYNPRhqa 316
Cdd:cd18560 94 TGEVVRIMDRGTESANTLLsylvfylvPTLLELIVVSVV-------FAFHFGAWLALIVFLSVLLyGVFTIKVTEWR--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 317 vlTEIQDATAKA-GQVVREAVGGL---QTVRSFGAEEQEVSRYKEALERCRQLWWRRD-----------------LERAL 375
Cdd:cd18560 164 --TKFRRAANKKdNEAHDIAVDSLlnfETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQaslsllnvgqqliiqlgLTLGL 241
|
250
....*....|....
gi 528078492 376 YLAIRRVMALGMQV 389
Cdd:cd18560 242 LLAGYRVVDGGLSV 255
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
606-688 |
2.54e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.19 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 606 QLAVGQKQRLAIARALVRNPRVLILDEATSALDS----QCEQALQAWRSKGDRTVLVIAHRLHTV-QNVDQVLVLKQGQL 680
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPttqaQIFRLLTRLNQNNNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
....*...
gi 528078492 681 VEHSQLRE 688
Cdd:PRK15093 238 VETAPSKE 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
469-680 |
6.22e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.44 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPT-GGQLLLDGQPL-VQYDHHYLHRQV 546
Cdd:TIGR02633 259 EARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVdIRNPAQAIRAGI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 547 VLVGQE-------PVLfsgSVKDNIAYGLKD--CEDAQVMAAVRAACADDFIGEM------PDgihTEIGekgsQLAVGQ 611
Cdd:TIGR02633 339 AMVPEDrkrhgivPIL---GVGKNITLSVLKsfCFKMRIDAAAELQIIGSAIQRLkvktasPF---LPIG----RLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528078492 612 KQRLAIARALVRNPRVLILDEATSALD----SQCEQALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQL 680
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDvgakYEIYKLINQLAQEG-VAIIVVSSELAEVLGLsDRVLVIGEGKL 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
484-680 |
6.71e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 484 PVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLV-QYDHHYLHRQVVLVGQEP----VLFSG 558
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLANGIVYISEDRkrdgLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 559 SVKDNI-----------AYGLKdcEDAQVMAAvraacaDDFIGEMpdGIHT-----EIGEkgsqLAVGQKQRLAIARALV 622
Cdd:PRK10762 346 SVKENMsltalryfsraGGSLK--HADEQQAV------SDFIRLF--NIKTpsmeqAIGL----LSGGNQQKVAIARGLM 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528078492 623 RNPRVLILDEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNVDQVLVLKQGQL 680
Cdd:PRK10762 412 TRPKVLILDEPTRGVDvgakKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
606-682 |
8.16e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.58 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 606 QLAVGQKQRLAIARALVRNPRVLILDEATSALD----SQCEQALQAWRSKGDRTVLVIAHRLHTVQNV-DQVLVLKQGQL 680
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqAQIIELLLELQQKENMALVLITHDLALVAEAaHKIIVMYAGQV 232
|
..
gi 528078492 681 VE 682
Cdd:PRK11022 233 VE 234
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
491-699 |
8.36e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 491 FTLHPGKVTALVGPNGSGKSTVAAPLQnlyqptgGQL-LLDGQplvqYDHHYlhRQVVLVGQEPV--LFSGSVKDNIAYG 567
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALA-------GELpLLSGE----RQSQF--SHITRLSFEQLqkLVSDEWQRNNTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 568 LKDCED------AQVM---AAVRAAC---ADDFigempdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATS 635
Cdd:PRK10938 91 LSPGEDdtgrttAEIIqdeVKDPARCeqlAQQF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 636 ALDSQCEQALQ---AWRSKGDRTVLVIAHRLHTVQN-VDQVLVLKQGQLVEHSqlrEDQDVYAH-LVQQ 699
Cdd:PRK10938 165 GLDVASRQQLAellASLHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETG---EREEILQQaLVAQ 230
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
483-676 |
8.88e-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: 46.58 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 483 KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAaplqnlyqptggqllldgqplvqydhhylhRQVVLVgqepVLFSGSVKD 562
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTIL------------------------------DAIGLA----LGGAQSATR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 563 NIAYGLKDCEDAQVMAavraacadDFIGEMPdgihteigekgsQLAVGQKQRLAIARALV---RNPRVL-ILDEATSALD 638
Cdd:cd03227 54 RRSGVKAGCIVAAVSA--------ELIFTRL------------QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLD 113
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 528078492 639 SQCEQALqAW----RSKGDRTVLVIAHRLHTVQNVDQVLVLK 676
Cdd:cd03227 114 PRDGQAL-AEaileHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
168-429 |
1.18e-05 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 47.63 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 168 LIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSLSAGCRGGSFLFTMSR----------INLRIRERLFSSLLRQD 237
Cdd:cd18581 14 LVPILYKKIVDSLTPDSADSPLAFPWALILLYVFLKFLQGGGSGSVGLLSNLRsflwipvqqfTTREISVKLFAHLHSLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 238 LGFFQENKTGELNSRLSSDTSKMSRWLPYNA-NILLRSLVKVIGLYCFMLQVSPRL---TFLSL-LDLPLTIaaekvynp 312
Cdd:cd18581 94 LRWHLSRKTGEVLRVMDRGTSSINSLLSYVLfNIGPTIADIIIAIIYFAIAFNPWFgliVFVTMaLYLILTI-------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 313 rhqaVLTE----------IQDATAKAgqvvrEAVGGL---QTVRSFGAEEQEVSRYKEALERCRQLWWRRDLERA-LYLA 378
Cdd:cd18581 166 ----IITEwrtkfrremnKLDNEKRA-----KAVDSLlnfETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNlLNTA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 528078492 379 IRRVMALGMQVLILNCgVQQILAGEVTrggllsfllyqeeVGDYVRNLVYM 429
Cdd:cd18581 237 QNLIITIGLLAGSLLC-AYFVVEGKLT-------------VGDFVLFLTYI 273
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
469-680 |
2.11e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPSRP*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQptG---GQLLLDGQPL-VQYDHHYLHR 544
Cdd:PRK13549 261 EVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGKPVkIRNPQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 QVVLV-------GQEPVLfsgSVKDNIAYGLKD--CEDAQVMAAVRAACADDFIGEMPdgIHT-----EIGekgsQLAVG 610
Cdd:PRK13549 339 GIAMVpedrkrdGIVPVM---GVGKNITLAALDrfTGGSRIDDAAELKTILESIQRLK--VKTaspelAIA----RLSGG 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528078492 611 QKQRLAIARALVRNPRVLILDEATSALD--SQCE--QALQAWRSKGdRTVLVIAHRLHTVQNV-DQVLVLKQGQL 680
Cdd:PRK13549 410 NQQKAVLAKCLLLNPKILILDEPTRGIDvgAKYEiyKLINQLVQQG-VAIIVISSELPEVLGLsDRVLVMHEGKL 483
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
496-679 |
2.39e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 496 GKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVqYDHHYLhrqvvlvgqepvlfsgsvkdniayglkdcedaq 575
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-YKPQYI--------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 576 vmaavraacaddfigempdgihteigekgsQLAVGQKQRLAIARALVRNPRVLILDEATSALDSqcEQALQAWRS----- 650
Cdd:cd03222 71 ------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI--EQRLNAARAirrls 118
|
170 180 190
....*....|....*....|....*....|
gi 528078492 651 -KGDRTVLVIAHRLHTVQNVDQVLVLKQGQ 679
Cdd:cd03222 119 eEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
503-638 |
3.11e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 503 GPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQYDHHYLHRqvvlVG---QEpvlFS--G--SVKDNIA-----YGLkd 570
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRR----VGymsQA---FSlyGelTVRQNLElharlFHL-- 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528078492 571 cEDAQVMAAVRAAcADDFigempdGIHTEIGEKGSQLAVGQKQRLAIARALVRNPRVLILDEATSALD 638
Cdd:NF033858 370 -PAAEIAARVAEM-LERF------DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
501-664 |
3.82e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 501 LVGPNGSGKSTVAAPLQNLYQPTGGQLLLD-GQPLvqydhHYLhRQ------------VVLVGQEPVLFSGSVKDNIaYG 567
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERL-----GKL-RQdqfafeeftvldTVIMGHTELWEVKQERDRI-YA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 568 LKDCEDAQVMaavRAACADDFIGEMpDGIHTE-----------IGEK---G--SQLAVGQKQRLAIARALVRNPRVLILD 631
Cdd:PRK15064 105 LPEMSEEDGM---KVADLEVKFAEM-DGYTAEaragelllgvgIPEEqhyGlmSEVAPGWKLRVLLAQALFSNPDILLLD 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 528078492 632 EATSALD----SQCEQALQAWRSkgdrTVLVIAHRLH 664
Cdd:PRK15064 181 EPTNNLDintiRWLEDVLNERNS----TMIIISHDRH 213
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
469-661 |
1.01e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 469 EFQDVTFSYPSrp*KPVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQY-DHhylHRQVV 547
Cdd:PRK11147 321 EMENVNYQIDG---KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYfDQ---HRAEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 548 lvgqEPvlfSGSVKDNIAYGLKDCE----DAQV--------------MAAVRAacaddfigempdgihteigekgsqLAV 609
Cdd:PRK11147 395 ----DP---EKTVMDNLAEGKQEVMvngrPRHVlgylqdflfhpkraMTPVKA------------------------LSG 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 528078492 610 GQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQAWRSKGDRTVLVIAH 661
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSH 495
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
208-447 |
2.58e-04 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 43.74 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 208 GCRGGSFLFTMSRI----NLRIRERLFSSLLRQDL----GFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLVKVI 279
Cdd:cd18559 48 AILQGITVFQYSMAvsigGIFASRAVHLDLYHKALrspiSFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 280 GLYCFMLQVSPRLTFLSLLDLpLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEqevsRYKEAL 359
Cdd:cd18559 128 GLYLLILLAGPMAAVGIPLGL-LYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEE----AFIRQV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 360 ERCrqlwwrRDLERALYLAIRRVMALGMQV-LILNCGVQ-QILAGEVTRGGLLSF----LLYQEEVGDYVRNLVYMYGDM 433
Cdd:cd18559 203 DAK------RDNELAYLPSIVYLRALAVRLwCVGPCIVLfASFFAYVSRHSLAGLvalkVFYSLALTTYLNWPLNMSPEV 276
|
250
....*....|....
gi 528078492 434 LSNVGAAEKVFCYI 447
Cdd:cd18559 277 ITNIVAAEVSLERS 290
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
597-675 |
2.60e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 597 HTEIGEKGSQLAVGQKQRLAIARAL---VRNPRVLILDEATSALDS----QCEQALQAWRSKGdRTVLVIAHRLHTVQNV 669
Cdd:PRK00635 800 YLPLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHThdikALIYVLQSLTHQG-HTVVIIEHNMHVVKVA 878
|
....*.
gi 528078492 670 DQVLVL 675
Cdd:PRK00635 879 DYVLEL 884
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
208-412 |
2.70e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 43.34 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 208 GCRGGSFLFTMSRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSsDTSKMSRWLPYNANILLRSLVKVIGLYCFMLQ 287
Cdd:cd18566 60 LLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREFLTGQALLALLDLPFVLIFLGLIWY 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 288 VSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRqlww 367
Cdd:cd18566 139 LGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAA---- 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 528078492 368 RRDLERALYLAIrrVMALG------MQVLILNCGVQQILAGEVTRGGLLSF 412
Cdd:cd18566 215 YAGFKVAKINAV--AQTLGqlfsqvSMVAVVAFGALLVINGDLTVGALIAC 263
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
498-661 |
3.98e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 498 VTALVGPNGSGKSTVaapLQNLYQPTGGQLLLDGQPLVQYDHhylhrqvvlvgqepVLFSGSVKDNIAYGLKDCEDAQVM 577
Cdd:cd03240 24 LTLIVGQNGAGKTTI---IEALKYALTGELPPNSKGGAHDPK--------------LIREGEVRAQVKLAFENANGKKYT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 578 AAVRAACADDFI----GEMPDGIHTEIGekgsQLAVGQKQ------RLAIARALVRNPRVLILDEATSALDS-QCEQAL- 645
Cdd:cd03240 87 ITRSLAILENVIfchqGESNWPLLDMRG----RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLa 162
|
170
....*....|....*....
gi 528078492 646 ---QAWRSKGDRTVLVIAH 661
Cdd:cd03240 163 eiiEERKSQKNFQLIVITH 181
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
610-702 |
4.27e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 610 GQKQRLAIARALVRNPRVLILDEATSALDSQCEQALQAWRSKGDRTVLVIAHR---LHTVqnVDQVLVLKQGQLVEHsql 686
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHArefLNTV--VTDILHLHGQKLVTY--- 422
|
90
....*....|....*.
gi 528078492 687 REDQDVYAHLVQQRLE 702
Cdd:PLN03073 423 KGDYDTFERTREEQLK 438
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
168-429 |
4.62e-04 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 42.90 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 168 LIPHYSGRVIDILGSDFDP*SFASAIFFMCLFSVGSSlsagcrGG-SFLFTM--------SRINLRIRerLFSSLLRQDL 238
Cdd:cd18583 14 LVPRQLGIIVDSLSGGSGKSPWKEIGLYVLLRFLQSG------GGlGLLRSWlwipveqySYRALSTA--AFNHVMNLSM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 239 GFFQENKTGELnsrlssdTSKMSRwlpynanilLRSLVKVIGLYCFmlQVSPrltflSLLDLPLTIA------------- 305
Cdd:cd18583 86 DFHDSKKSGEV-------LKAIEQ---------GSSINDLLEQILF--QIVP-----MIIDLVIAIVylyylfdpymgli 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 306 ----------AEKVYNPRHQAVLTEIQDATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLwwRRDLERAL 375
Cdd:cd18583 143 vavvmvlyvwSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKA--ERKYLFSL 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 376 YLAIrrvmalGMQVLILNCGvqqILAG------EVTRGgllsfllyQEEVGDYVRNLVYM 429
Cdd:cd18583 221 NLLN------AVQSLILTLG---LLAGcflaayQVSQG--------QATVGDFVTLLTYW 263
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
468-661 |
6.96e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 468 VEFQDVTFSYPSRP*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDGQPLVQY---DHHYlhr 544
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYyaqDHAY--- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 545 qvvlvgqepvLFSG--SVKDNIAYGLKDCEDAQvmaAVRAAcaddfIGEMPDGiHTEIGEKGSQLAVGQKQRLAIARALV 622
Cdd:PRK15064 394 ----------DFENdlTLFDWMSQWRQEGDDEQ---AVRGT-----LGRLLFS-QDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190
....*....|....*....|....*....|....*....
gi 528078492 623 RNPRVLILDEATSALDSQCEQALQAWRSKGDRTVLVIAH 661
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSH 493
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
488-524 |
8.80e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.96 E-value: 8.80e-04
10 20 30
....*....|....*....|....*....|....*..
gi 528078492 488 GLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTG 524
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
463-527 |
1.04e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 1.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528078492 463 RLEGRV-EFQDVTFSYPSRp*kpVL-KGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQL 527
Cdd:PRK11819 319 RLGDKViEAENLSKSFGDR----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
467-661 |
1.49e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 40.44 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 467 RVEFQDVTFSY---PSRP*KPVLKGLtftLHPGKVTALVGPNGSGKSTVAAplqnlyqptggQLLLD---GQPLVQYDHH 540
Cdd:pfam13481 4 PLELLDVLADGlaaPPPPRRWLIKGL---LPAGGLGLLAGAPGTGKTTLAL-----------DLAAAvatGKPWLGGPRV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 541 YLHRQVVLVgqepvlfsgsvkdniayglkDCEDAQVMAAVR--AACAD-------DFIGEMPDGIHTEIGEKGSQLAVGQ 611
Cdd:pfam13481 70 PEQGKVLYV--------------------SAEGPADELRRRlrAAGADldlparlLFLSLVESLPLFFLDRGGPLLDADV 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 528078492 612 KQRLAIARAlVRNPRVLILDEATSAL------DSQCEQALQAWRSKGDR---TVLVIAH 661
Cdd:pfam13481 130 DALEAALEE-VEDPDLVVIDPLARALggdensNSDVGRLVKALDRLARRtgaTVLLVHH 187
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
470-640 |
2.75e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 470 FQDVTFSYPSRp*kpVLKGLTFTLHPGKVTALVGPNGSGKSTVAAPLQNLYQPTGGQLLLDG-------QPLVQYDHHYL 542
Cdd:PRK13541 4 LHQLQFNIEQK----NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcninniaKPYCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 543 HRQVVLVGQEPVLFSGSVKDNIayglkdcedAQVMAAVRAACADDFigempdgihteIGEKGSQLAVGQKQRLAIARALV 622
Cdd:PRK13541 80 GLKLEMTVFENLKFWSEIYNSA---------ETLYAAIHYFKLHDL-----------LDEKCYSLSSGMQKIVAIARLIA 139
|
170
....*....|....*...
gi 528078492 623 RNPRVLILDEATSALDSQ 640
Cdd:PRK13541 140 CQSDLWLLDEVETNLSKE 157
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
219-414 |
2.86e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 40.34 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 219 SRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKM----SRWLPYNANILLRSLVKVIGLYcFMLQVSPRLTF 294
Cdd:cd18561 65 QRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALeayyGRYLPQLLVALLGPLLILIYLF-FLDPLVALILL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 295 LSLLDLPLTIA----AEKVYNPRHQAvlteiqdATAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRD 370
Cdd:cd18561 144 VFALLIPLSPAlwdrLAKDTGRRHWA-------AYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVL 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 528078492 371 LERALYLAIRRVMALGMQVLILNCGVQQILAGEVTRGGLLSFLL 414
Cdd:cd18561 217 AVSLLSSGIMGLATALGTALALGVGALRVLGGQLTLSSLLLILF 260
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
189-357 |
3.40e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 40.24 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 189 FASAIFFMCLFSVgsslsagCRGGSFLFTMSRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNA 268
Cdd:cd18599 64 YGGSILVILLLSL-------IRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 269 NILLRSLVKVIGLYCFMLQVSPRLTFLSLLDLPLTIAAEKVYNP------RHQ-----AVLTEIQdatakagqvvrEAVG 337
Cdd:cd18599 137 ENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIFRRairelkRLEnisrsPLFSHLT-----------ATIQ 205
|
170 180
....*....|....*....|
gi 528078492 338 GLQTVRSFGAEEQEVSRYKE 357
Cdd:cd18599 206 GLSTIHAFNKEKEFLSKFKK 225
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
197-361 |
6.69e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 39.12 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 197 CLFSVGSSLSAGCRGGSFLFTMSRINLRIRERLFSSLLRQDLGFFQENKTGELNSRLSSDTSKMSRWLPYNANILLRSLV 276
Cdd:cd18602 57 AGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 277 KVIGlyCFMLQVSPRLTFLSLLdLPLTIAA---EKVYnprhQAVLTEIQ--DATAKaGQVV---REAVGGLQTVRSFGAE 348
Cdd:cd18602 137 LCLS--AIIVNAIVTPYFLIAL-IPIIIVYyflQKFY----RASSRELQrlDNITK-SPVFshfSETLGGLTTIRAFRQQ 208
|
170
....*....|...
gi 528078492 349 EQEVSRYKEALER 361
Cdd:cd18602 209 ARFTQQMLELIDR 221
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
484-511 |
8.34e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 38.59 E-value: 8.34e-03
10 20
....*....|....*....|....*....
gi 528078492 484 PVLKGL-TFTLHPGkVTALVGPNGSGKST 511
Cdd:COG3910 25 PAVRNLeGLEFHPP-VTFFVGENGSGKST 52
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
486-664 |
8.57e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 38.83 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 486 LKGLTFTLHPGkVTALVGPNGSGKSTVaapLQNLyqptggQLLLDGQPLVQYDHHYLHRQVVLVGQEPVL---FSGSVKD 562
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSI---LEAL------RLLLGPSSSRKFDEEDFYLGDDPDLPEIEIeltFGSLLSR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 563 NIAYGLKDCEDAQVMAAVRAacADDFIGEMPDGIHTEIGEKGSQLAVGQKQRLAIA----RALVRNPRVLILDEATSALD 638
Cdd:COG3593 84 LLRLLLKEEDKEELEEALEE--LNEELKEALKALNELLSEYLKELLDGLDLELELSldelEDLLKSLSLRIEDGKELPLD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 528078492 639 SQ-----------CEQALQAWRSKGDRTVLVI----AHrLH 664
Cdd:COG3593 162 RLgsgfqrlillaLLSALAELKRAPANPILLIeepeAH-LH 201
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
600-681 |
8.75e-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: 39.61 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528078492 600 IGEKGSQLAVGQKQRLAIARALVR---NPRVLILDEATSALD----SQCEQALQAWRSKGDrTVLVIAHRLHTVQNVDQV 672
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHfddiKKLLEVLQRLVDKGN-TVVVIEHNLDVIKTADYI 901
|
90
....*....|....*
gi 528078492 673 LVL------KQGQLV 681
Cdd:TIGR00630 902 IDLgpeggdGGGTVV 916
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
491-512 |
9.27e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.76 E-value: 9.27e-03
|
| |
