|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-696 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 1078.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 1 MALSYLRPWVSLLLADMALLGLLQGS---LGNLLPQGLPGLWIEGTLRLGVLWG------LLKVGELLGLVGTLLPLLCL 71
Cdd:TIGR00958 1 AALAYLLPWFSLLLVDWALLRDLLQGifgLLLPFEKGLYVLWLEGTLRLGVLWLgalgilLNKAGGLLAAVKPLVAALCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 72 ATPLFFSLRALVGGTASTSVVRVASASWGWLLAGYGAVALSWAVWAVLSPAGVQEKEPGQE---NRTLMKRLLKLSRPDL 148
Cdd:TIGR00958 81 ATPSLSSLRALAFWEALDPAVRVALGLWSWFVWSYGAALPAAALWAVLSSAGASEKEAEQGqseTADLLFRLLGLSGRDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 149 PFLIAAFFFLVVAVWGETLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIREQL 228
Cdd:TIGR00958 161 PWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 229 FSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKV 308
Cdd:TIGR00958 241 FRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 309 YNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQV 388
Cdd:TIGR00958 321 FGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 389 LILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKVFSYLDRKPNLPQPGILAPPWLEGRVE 468
Cdd:TIGR00958 401 LVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 469 FQDVSFSYPRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLV 548
Cdd:TIGR00958 481 FQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 549 GQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLI 628
Cdd:TIGR00958 561 GQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLI 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 629 LDEATSALDAQCEQALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE---HDQLRDGQDVYAHLV 696
Cdd:TIGR00958 641 LDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEmgtHKQLMEDQGCYKHLV 711
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
154-442 |
6.46e-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: 454.87 E-value: 6.46e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 154 AFFFLVVAVWGETLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIREQLFSSLL 233
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 234 RQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRH 313
Cdd:cd18590 81 QQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 314 QAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQVLILNC 393
Cdd:cd18590 161 QKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYC 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 37572301 394 GVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18590 241 GRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
132-702 |
8.94e-156 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 463.10 E-value: 8.94e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 132 ENRTLMKRLLKLSRPDLPFLIAAFFFLVVAVWGETLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRGG 211
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 212 SFLFTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRL 291
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 292 TFLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLE 371
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 372 KDVYLVIRRVMALGMQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKVFSYLDRKPN 451
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 452 LPQP-GILAPPWLEGRVEFQDVSFSYPrrPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG 530
Cdd:COG1132 324 IPDPpGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 531 EPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRD--------------CEDaqvmaaaqaacaddFIGEMTNGIN 596
Cdd:COG1132 402 VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDatdeeveeaakaaqAHE--------------FIEALPDGYD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 597 TEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQN--WRSQGDRTMLVIAHRLHTVQNADQVLVL 674
Cdd:COG1132 468 TVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEalERLMKGRTTIVIAHRLSTIRNADRILVL 547
|
570 580 590
....*....|....*....|....*....|.
gi 37572301 675 KQGRLVE---HDQLRDGQDVYAHLVQQRLEA 702
Cdd:COG1132 548 DDGRIVEqgtHEELLARGGLYARLYRLQFGE 578
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
139-700 |
5.88e-114 |
|
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: 359.15 E-value: 5.88e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 139 RLLKLSRPDLPFLIAAFFFL-VVAVwgetLIPRYSGRVID--ILGGDFDP-DAFASAIFFMCLFSVGSSFSagcRGGSFL 214
Cdd:COG2274 149 RLLRRYRRLLLQVLLASLLInLLAL----ATPLFTQVVIDrvLPNQDLSTlWVLAIGLLLALLFEGLLRLL---RSYLLL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 215 FTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSrwlpFNANILLRSLVKVVGLYFF---MLQVSPRL 291
Cdd:COG2274 222 RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDVESIRE----FLTGSLLTALLDLLFVLIFlivLFFYSPPL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 292 TFLSLLDLPLTIAAEKVYNPR-HQAVLKEIQDAVAKAGQVVrEAVGGLQTVRSFGAEEQEVSRYKEALERcrQLWWRRDL 370
Cdd:COG2274 298 ALVVLLLIPLYVLLGLLFQPRlRRLSREESEASAKRQSLLV-ETLRGIETIKALGAESRFRRRWENLLAK--YLNARFKL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 371 EK--DVYLVIRRVMALGMQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKVFSYLDR 448
Cdd:COG2274 375 RRlsNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 449 KP-NLPQPGILAPPWLEGRVEFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLL 527
Cdd:COG2274 455 PPeREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 528 LDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLA 607
Cdd:COG2274 534 IDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLS 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 608 VGQKQRLAIARALVRNPRVLILDEATSALDAQCE----QALQNWRsqGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE-- 681
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEaiilENLRRLL--KGRTVIIIAHRLSTIRLADRIIVLDKGRIVEdg 691
|
570 580
....*....|....*....|
gi 37572301 682 -HDQLRDGQDVYAHLVQQRL 700
Cdd:COG2274 692 tHEELLARKGLYAELVQQQL 711
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
456-679 |
8.40e-114 |
|
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: 341.76 E-value: 8.40e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 456 GILAPPWLEGRVEFQDVSFSYPRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTE 535
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 536 YDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLA 615
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 616 IARALVRNPRVLILDEATSALDA----QCEQALQNWRSqgDRTMLVIAHRLHTVQNADQVLVLKQGRL 679
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAeseqQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
138-695 |
4.97e-107 |
|
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: 336.69 E-value: 4.97e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 138 KRLLKLSRPDLPFLIAAFFFLVVAVWGETLIPrysGRVIDILGGDFDpDAFASAIFFMCLFSVGSSFSAG-CRGGSFLFt 216
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLA---ALLKPLLDDGFG-GRDRSVLWWVPLVVIGLAVLRGiCSFVSTYL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 217 MSRINLR----IREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLT 292
Cdd:TIGR02203 78 LSWVSNKvvrdIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 293 FLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEK 372
Cdd:TIGR02203 158 LIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 373 DVYL-VIRRVMALGMQVLILNCGVQQiLAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKVFSYLDRKPN 451
Cdd:TIGR02203 238 SISSpITQLIASLALAVVLFIALFQA-QAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 452 lPQPGILAPPWLEGRVEFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGE 531
Cdd:TIGR02203 317 -KDTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 532 PLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYG-LRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQ 610
Cdd:TIGR02203 395 DLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 611 KQRLAIARALVRNPRVLILDEATSALDAQCEQALQNW--RSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE---HDQL 685
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESERLVQAAleRLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVErgtHNEL 554
|
570
....*....|
gi 37572301 686 RDGQDVYAHL 695
Cdd:TIGR02203 555 LARNGLYAQL 564
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
154-442 |
4.61e-98 |
|
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: 303.70 E-value: 4.61e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 154 AFFFLVVAVWGETLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIREQLFSSLL 233
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 234 RQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRH 313
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 314 QAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQVLILNC 393
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 37572301 394 GVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18572 241 GGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
467-698 |
2.98e-95 |
|
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: 294.45 E-value: 2.98e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRV 626
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 627 LILDEATSALDAQCEQALQNW--RSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE---HDQLRDGQDVYAHLVQQ 698
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEAldRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEqgtHDELMAQKGVYAKLVKA 237
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
154-442 |
1.76e-86 |
|
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: 273.42 E-value: 1.76e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 154 AFFFLVVAVWGETLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIREQLFSSLL 233
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 234 RQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRH 313
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 314 QAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQVLILNC 393
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 37572301 394 GVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18784 241 GGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
154-442 |
4.36e-82 |
|
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: 262.11 E-value: 4.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 154 AFFFLVVAVWGETLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIREQLFSSLL 233
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 234 RQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRH 313
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 314 QAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQVLILNC 393
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 37572301 394 GVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18557 241 GGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
134-685 |
6.12e-79 |
|
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: 262.39 E-value: 6.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 134 RTLMKRLLKLSRPDLPFLIAAFFF-------LVVAVWgetLIprysGRVID-ILGGDFDPDAFASAIFFMCLFSVGSSFS 205
Cdd:COG4988 2 KPLDKRLKRLARGARRWLALAVLLgllsgllIIAQAW---LL----ASLLAgLIIGGAPLSALLPLLGLLLAVLLLRALL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 206 AGCRGgSFLFTMS-RINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLM----SRWLPfnanILLRSLVKVVGL 280
Cdd:COG4988 75 AWLRE-RAAFRAAaRVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALdgyfARYLP----QLFLAALVPLLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 281 YFFMLQVSPRLTFLSLLDLPLT--------IAAEKVyNPRHQAVLKEIqdavakAGQVVrEAVGGLQTVRSFGAEEQEVS 352
Cdd:COG4988 150 LVAVFPLDWLSGLILLVTAPLIplfmilvgKGAAKA-SRRQWRALARL------SGHFL-DRLRGLTTLKLFGRAKAEAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 353 RYKEALERCRqlwwRRDLEkdvylVIRR----------VMALGMQVLILNCGVQqILAGEVTRGGLLSFLLYQEEVGQYV 422
Cdd:COG4988 222 RIAEASEDFR----KRTMK-----VLRVaflssavlefFASLSIALVAVYIGFR-LLGGSLTLFAALFVLLLAPEFFLPL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 423 RNLVYMYGDMLSNVGAAEKVFSYLDRKPNLPQPGILAPPWLEG-RVEFQDVSFSYPrrPEKPVLQGLTFTLHPGTVTALV 501
Cdd:COG4988 292 RDLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 502 GPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQA 581
Cdd:COG4988 370 GPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 582 ACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQN---WRSQGdRTMLVI 658
Cdd:COG4988 450 AGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQalrRLAKG-RTVILI 528
|
570 580 590
....*....|....*....|....*....|
gi 37572301 659 AHRLHTVQNADQVLVLKQGRLVE---HDQL 685
Cdd:COG4988 529 THRLALLAQADRILVLDDGRIVEqgtHEEL 558
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
465-687 |
1.07e-78 |
|
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: 250.99 E-value: 1.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 465 GRVEFQDVSFSYprRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQ 544
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 545 VVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNP 624
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 625 RVLILDEATSALDAQCEQALQN--WRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE---HDQLRD 687
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEalEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEegtHDELLA 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
134-702 |
1.13e-77 |
|
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: 260.52 E-value: 1.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 134 RTLMKRLLKLSRPDLPFL-IAAFFFLVVAVWGETLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSfsagcRGGS 212
Cdd:COG5265 17 DLLLRLLLLLLLPPYLRRrRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLLLAYGLL-----RLLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 213 FLFT------MSRINLRIREQL----FSSLLRQDLGFFQETKTGELN---SRLSSDTSLMSRWLPFNA--NILLRSLVKV 277
Cdd:COG5265 92 VLFGelrdalFARVTQRAVRRLalevFRHLHALSLRFHLERQTGGLSrdiERGTKGIEFLLRFLLFNIlpTLLEIALVAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 278 VGLYFFmlqvSPRLTFLSLLDLPLTIAAE-KVYNPRHQAVlKEIQDAVAKAGQVvreAVGGL---QTVRSFGAEEQEVSR 353
Cdd:COG5265 172 ILLVKY----DWWFALITLVTVVLYIAFTvVVTEWRTKFR-REMNEADSEANTR---AVDSLlnyETVKYFGNEAREARR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 354 YKEALERCRQLWWRrdlekdvylvIRRVMAL--GMQVLILNCGV--------QQILAGEVTRGGL-------------LS 410
Cdd:COG5265 244 YDEALARYERAAVK----------SQTSLALlnFGQALIIALGLtammlmaaQGVVAGTMTVGDFvlvnayliqlyipLN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 411 FL--LYQEevgqyVRN-LVymygDMlsnvgaaEKVFSYLDRKPNLP-QPGilAPPwL---EGRVEFQDVSFSYprRPEKP 483
Cdd:COG5265 314 FLgfVYRE-----IRQaLA----DM-------ERMFDLLDQPPEVAdAPD--APP-LvvgGGEVRFENVSFGY--DPERP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNI 563
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 564 AYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQA 643
Cdd:COG5265 453 AYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERA 532
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 644 LQ---NWRSQGdRTMLVIAHRLHTVQNADQVLVLKQGRLVE---HDQLRDGQDVYAHL--VQQRLEA 702
Cdd:COG5265 533 IQaalREVARG-RTTLVIAHRLSTIVDADEILVLEAGRIVErgtHAELLAQGGLYAQMwaRQQEEEE 598
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
467-695 |
9.29e-76 |
|
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: 243.29 E-value: 9.29e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:cd03251 1 VEFKNVTFRYPGD-GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRV 626
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37572301 627 LILDEATSALDAQCEQALQNW--RSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE---HDQLRDGQDVYAHL 695
Cdd:cd03251 160 LILDEATSALDTESERLVQAAleRLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVErgtHEELLAQGGVYAKL 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
467-678 |
2.63e-75 |
|
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: 239.59 E-value: 2.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPeKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSGSVKDNIayglrdcedaqvmaaaqaacaddfigemtnginteigekggqLAVGQKQRLAIARALVRNPRV 626
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 627 LILDEATSALDAQCE----QALQNWRsqGDRTMLVIAHRLHTVQNADQVLVLKQGR 678
Cdd:cd03228 118 LILDEATSALDPETEalilEALRALA--KGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
193-701 |
1.40e-74 |
|
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: 254.28 E-value: 1.40e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 193 FFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSrWLPFNANILLR 272
Cdd:TIGR01846 183 LAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRELEQIRN-FLTGSALTVVL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 273 SLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVS 352
Cdd:TIGR01846 262 DLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 353 RYKEALERCRQLWWRRDL-----EKDVYLVIRRVMALgmqvlILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVY 427
Cdd:TIGR01846 342 RWDRQLAAYVAASFRVTNlgniaGQAIELIQKLTFAI-----LLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 428 MYGDMLSNVGAAEKVFSYLDRKPNLPQPGILAPPWLEGRVEFQDVSFSYprRPEKP-VLQGLTFTLHPGTVTALVGPNGS 506
Cdd:TIGR01846 417 LWQDFQQTGIALERLGDILNSPTEPRSAGLAALPELRGAITFENIRFRY--APDSPeVLSNLNLDIKPGEFIGIVGPSGS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 507 GKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADD 586
Cdd:TIGR01846 495 GKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHD 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 587 FIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQ-NWR--SQGdRTMLVIAHRLH 663
Cdd:TIGR01846 575 FISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMrNMReiCRG-RTVIIIAHRLS 653
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 37572301 664 TVQNADQVLVLKQGRLVE---HDQLRDGQDVYAHLVQQRLE 701
Cdd:TIGR01846 654 TVRACDRIIVLEKGQIAEsgrHEELLALQGLYARLWQQQSG 694
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
222-695 |
7.35e-74 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 249.55 E-value: 7.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 222 LRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMsrwlpfnANILLRSLVKVV-------GLYFFMLQVSPRLTFL 294
Cdd:PRK11176 98 MTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQV-------ASSSSGALITVVregasiiGLFIMMFYYSWQLSLI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 295 SLLDLPLTIAAEKVYNPRHQAVLKEIQDAVakaGQVVREA---VGGLQTVRSFGAEEQEVSRYKEALERCRQLwwrrdle 371
Cdd:PRK11176 171 LIVIAPIVSIAIRVVSKRFRNISKNMQNTM---GQVTTSAeqmLKGHKEVLIFGGQEVETKRFDKVSNRMRQQ------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 372 kdvylvirrvmalGMQVL----ILNCGVQQI--LAgevtrgglLSFLLYQEEVGQYVRNL-------VY--MYGDM---- 432
Cdd:PRK11176 241 -------------GMKMVsassISDPIIQLIasLA--------LAFVLYAASFPSVMDTLtagtitvVFssMIALMrplk 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 433 -LSNV--------GAAEKVFSYLDRKPNLPQpGILAPPWLEGRVEFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGP 503
Cdd:PRK11176 300 sLTNVnaqfqrgmAACQTLFAILDLEQEKDE-GKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGR 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 504 NGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRD-CEDAQVMAAAQAA 582
Cdd:PRK11176 378 SGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEqYSREQIEEAARMA 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 583 CADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNWRS--QGDRTMLVIAH 660
Cdd:PRK11176 458 YAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDelQKNRTSLVIAH 537
|
490 500 510
....*....|....*....|....*....|....*...
gi 37572301 661 RLHTVQNADQVLVLKQGRLVE---HDQLRDGQDVYAHL 695
Cdd:PRK11176 538 RLSTIEKADEILVVEDGEIVErgtHAELLAQNGVYAQL 575
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
467-698 |
4.44e-72 |
|
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: 233.66 E-value: 4.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRV 626
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 627 LILDEATSALDAQCEQALQNW--RSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE---HDQLRDGQDVYAHLVQQ 698
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAAlrDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVErgtHEELLAKGGLYAEMWKA 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
467-697 |
6.24e-64 |
|
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: 212.35 E-value: 6.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYprRPEKP-VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQV 545
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 546 VLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPR 625
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 626 VLILDEATSALDAQCEQAL-QNWRSQGD-RTMLVIAHRLHTVQNADQVLVLKQGRLVE---HDQLRDGQDVYAHLVQ 697
Cdd:cd03252 159 ILIFDEATSALDYESEHAImRNMHDICAgRTVIIIAHRLSTVKNADRIIVMEKGRIVEqgsHDELLAENGLYAYLYQ 235
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
151-415 |
1.15e-63 |
|
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: 212.89 E-value: 1.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVWGETLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRGGSFLF--TMSRINLRIREQL 228
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLnhTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 229 FSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKV 308
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 309 YNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQV 388
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260
....*....|....*....|....*..
gi 37572301 389 LILNCGVQQILAGEVTRGGLLSFLLYQ 415
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLF 267
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
223-698 |
1.38e-61 |
|
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: 215.79 E-value: 1.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 223 RIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMsrwlpfnANILLR-------SLVKVVGLYFFMLQVSPRL---- 291
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDAL-------DNLYLRvllpllvALLVILAAVAFLAFFSPALalvl 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 292 ---TFLSLLDLPLTIAAekvynpRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERcrqlwWRR 368
Cdd:COG4987 162 algLLLAGLLLPLLAAR------LGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEAR-----LAA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 369 DLEKDVYLVIRR--VMALGMQ-----VLILncGVQQILAGEVTrGGLL---------SFllyqeEVGQYVRNLVYMYGDM 432
Cdd:COG4987 231 AQRRLARLSALAqaLLQLAAGlavvaVLWL--AAPLVAAGALS-GPLLallvlaalaLF-----EALAPLPAAAQHLGRV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 433 LSnvgAAEKVFSYLDRKPNLPQPGILAPPWLEGRVEFQDVSFSYPRRPEkPVLQGLTFTLHPGTVTALVGPNGSGKSTVA 512
Cdd:COG4987 303 RA---AARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 513 ALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMT 592
Cdd:COG4987 379 ALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALP 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 593 NGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQN--WRSQGDRTMLVIAHRLHTVQNADQ 670
Cdd:COG4987 459 DGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAdlLEALAGRTVLLITHRLAGLERMDR 538
|
490 500 510
....*....|....*....|....*....|.
gi 37572301 671 VLVLKQGRLVE---HDQLRDGQDVYAHLVQQ 698
Cdd:COG4987 539 ILVLEDGRIVEqgtHEELLAQNGRYRQLYQR 569
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
465-680 |
1.39e-59 |
|
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: 199.74 E-value: 1.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 465 GRVEFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQ 544
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 545 VVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNP 624
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 625 RVLILDEATSALDAQCE----QALQNWRsqGDRTMLVIAHRLHTVQNADQVLVLKQGRLV 680
Cdd:cd03245 160 PILLLDEPTSAMDMNSEerlkERLRQLL--GDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
223-700 |
3.33e-59 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 209.96 E-value: 3.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 223 RIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLT 302
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 303 IAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGL-------QTVRsFGAEEQEVSR--YKEALERCRQlwwrrdlekD 373
Cdd:PRK10790 179 LVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMsviqqfrQQAR-FGERMGEASRshYMARMQTLRL---------D 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 374 VYLvIRRVMALgMQVLILnCGVQQIL----AGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKVFSYLDRK 449
Cdd:PRK10790 249 GFL-LRPLLSL-FSALIL-CGLLMLFgfsaSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 450 PNlpQPGILAPPWLEGRVEFQDVSFSYprRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLD 529
Cdd:PRK10790 326 RQ--QYGNDDRPLQSGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLD 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 530 GEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGlRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVG 609
Cdd:PRK10790 402 GRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG-RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVG 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 610 QKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNW----RSQgdRTMLVIAHRLHTVQNADQVLVLKQGRLVE---H 682
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAlaavREH--TTLVVIAHRLSTIVEADTILVLHRGQAVEqgtH 558
|
490
....*....|....*...
gi 37572301 683 DQLRDGQDVYAHLVQQRL 700
Cdd:PRK10790 559 QQLLAAQGRYWQMYQLQL 576
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
443-681 |
1.34e-58 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 208.28 E-value: 1.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 443 FSYLDRKPNLPQ-PGILAPPWLEGRVEFQDVSFSYPRRpeKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQP 521
Cdd:PRK13657 310 FEVEDAVPDVRDpPGAIDLGRVKGAVEFDDVSFSYDNS--RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDP 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 522 TGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGE 601
Cdd:PRK13657 388 QSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 602 KGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCE----QALQNWRSqgDRTMLVIAHRLHTVQNADQVLVLKQG 677
Cdd:PRK13657 468 RGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEakvkAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNG 545
|
....
gi 37572301 678 RLVE 681
Cdd:PRK13657 546 RVVE 549
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
156-442 |
1.93e-58 |
|
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: 199.23 E-value: 1.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 156 FFLVVAVWGETLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIREQLFSSLLRQ 235
Cdd:cd18589 3 GLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 236 DLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQA 315
Cdd:cd18589 83 EIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 316 VLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQVLILNCGV 395
Cdd:cd18589 163 LAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 37572301 396 QQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18589 243 QLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
465-683 |
4.17e-58 |
|
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: 195.79 E-value: 4.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 465 GRVEFQDVSFSYpRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQ 544
Cdd:cd03244 1 GDIEFKNVSLRY-RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 545 VVLVGQEPVLFSGSVKDNIA-YG----------LRDCedaqvmaaaqaaCADDFIGEMTNGINTEIGEKGGQLAVGQKQR 613
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLDpFGeysdeelwqaLERV------------GLKEFVESLPGGLDTVVEEGGENLSVGQRQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37572301 614 LAIARALVRNPRVLILDEATSALDAQCEQALQN-WRSQ-GDRTMLVIAHRLHTVQNADQVLVLKQGRLVEHD 683
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKtIREAfKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
224-674 |
3.03e-57 |
|
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: 203.29 E-value: 3.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 224 IREQLFSSLLRQDLGFFQETKTGELNS----RLSSDTSLMSRWLPfnaNILLRSLVKVVgLYFFMLQVSPRLTFLSLLDL 299
Cdd:TIGR02857 79 LRERLLEAVAALGPRWLQGRPSGELATlaleGVEALDGYFARYLP---QLVLAVIVPLA-ILAAVFPQDWISGLILLLTA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 300 PLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQlwwrRDLE--KDVYL- 376
Cdd:TIGR02857 155 PLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRE----RTMRvlRIAFLs 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 377 --VIRRVMALGMQVLILNCGVQqILAGEVT-RGGLLSFLLyQEEVGQYVRNLVYMYGDMLSNVGAAEKVFSYLDRKPnLP 453
Cdd:TIGR02857 231 saVLELFATLSVALVAVYIGFR-LLAGDLDlATGLFVLLL-APEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAP-RP 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 454 QPGILAPPWLEGR-VEFQDVSFSYPRRPekPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEP 532
Cdd:TIGR02857 308 LAGKAPVTAAPASsLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 533 LTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQ 612
Cdd:TIGR02857 386 LADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQ 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 613 RLAIARALVRNPRVLILDEATSALDAQCEQALQ---NWRSQGdRTMLVIAHRLHTVQNADQVLVL 674
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLealRALAQG-RTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
134-700 |
1.87e-54 |
|
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: 198.64 E-value: 1.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 134 RTLMKRLLKLSRPDLpfLIAAFFFLVVAVWGeTLIPRYSGrvidILGGDFDPDAFASAIFFMCLFSVGSSFSAG----CR 209
Cdd:TIGR03797 124 RDLLRFALRGARRDL--LAILAMGLLGTLLG-MLVPIATG----ILIGTAIPDADRSLLVQIALALLAAAVGAAafqlAQ 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 210 GGSFLFTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSdTSLMSRWLpfnANILLRSLVKVV-GL--YFFMLQ 286
Cdd:TIGR03797 197 SLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRIL---SGSTLTTLLSGIfALlnLGLMFY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 287 VSPRLTFLSLLDLPLTIA---AEKVYNPRHQAVLKEIQDAVAkaGQVVrEAVGGLQTVRSFGAEEQEVSRYKEALERCRQ 363
Cdd:TIGR03797 273 YSWKLALVAVALALVAIAvtlVLGLLQVRKERRLLELSGKIS--GLTV-QLINGISKLRVAGAENRAFARWAKLFSRQRK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 364 LWWRRDLEKDVYLVIRRVM-ALGMQVLILNCGvQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:TIGR03797 350 LELSAQRIENLLTVFNAVLpVLTSAALFAAAI-SLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERA 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 443 FSYLDRKP----NLPQPGILAppwleGRVEFQDVSFSYprRPEKP-VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQN 517
Cdd:TIGR03797 429 KPILEALPevdeAKTDPGKLS-----GAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLG 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 518 LYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGlrdcEDAQVMAAAQAACADDF---IGEMTNG 594
Cdd:TIGR03797 502 FETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGG----APLTLDEAWEAARMAGLaedIRAMPMG 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 595 INTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNWRSQGDRTMLVIAHRLHTVQNADQVLVL 674
Cdd:TIGR03797 578 MHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVL 657
|
570 580
....*....|....*....|....*....
gi 37572301 675 KQGRLVE---HDQLRDGQDVYAHLVQQRL 700
Cdd:TIGR03797 658 DAGRVVQqgtYDELMAREGLFAQLARRQL 686
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
213-702 |
1.70e-53 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 193.78 E-value: 1.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 213 FLFTMS-RINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSrwlpFNAN----ILLRSLVKVVGLYFFM-LQ 286
Cdd:PRK10789 59 LLFGASyQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVV----FAAGegvlTLVDSLVMGCAVLIVMsTQ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 287 VSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKE-ALERCRQLW 365
Cdd:PRK10789 135 ISWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAAdAEDTGKKNM 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 366 W--RRDLEKDVYLVIrrvmALGM-QVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:PRK10789 215 RvaRIDARFDPTIYI----AIGMaNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 443 FSYLDRKPNLpQPGILAPPWLEGRVEFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPT 522
Cdd:PRK10789 291 RAMLAEAPVV-KDGSEPVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 523 GGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEK 602
Cdd:PRK10789 369 EGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGER 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 603 GGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCE-QALQNWRSQGD-RTMLVIAHRLHTVQNADQVLVLKQGRLV 680
Cdd:PRK10789 449 GVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEhQILHNLRQWGEgRTVIISAHRLSALTEASEILVMQHGHIA 528
|
490 500
....*....|....*....|....*....
gi 37572301 681 E---HDQL--RDG--QDVYAHlvqQRLEA 702
Cdd:PRK10789 529 QrgnHDQLaqQSGwyRDMYRY---QQLEA 554
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
237-696 |
4.10e-51 |
|
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: 189.57 E-value: 4.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 237 LGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLrSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAV 316
Cdd:TIGR01193 244 MSFFSTRRTGEIVSRFTDASSIIDALASTILSLFL-DMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 317 LKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQVLILNCGVQ 396
Cdd:TIGR01193 323 NHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAY 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 397 QILAGEVTRGGLLSF-------------------LLYQEEVGQYVRNLVYMYGDMLSNvgaaEKVFSYLDRkpnlpqpgi 457
Cdd:TIGR01193 403 LVMRGKLTLGQLITFnallsyfltpleniinlqpKLQAARVANNRLNEVYLVDSEFIN----KKKRTELNN--------- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 458 lappwLEGRVEFQDVSFSYPRrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYD 537
Cdd:TIGR01193 470 -----LNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 538 HHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRD-CEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAI 616
Cdd:TIGR01193 543 RHTLRQFINYLPQEPYIFSGSILENLLLGAKEnVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIAL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 617 ARALVRNPRVLILDEATSALDAQCEQA-LQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE---HDQLRDGQDVY 692
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKiVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEqgsHDELLDRNGFY 702
|
....
gi 37572301 693 AHLV 696
Cdd:TIGR01193 703 ASLI 706
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
154-442 |
1.24e-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: 170.12 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 154 AFFFLVVAVWGETLIPRYSGRVIDIL------GGDFDPDAFASAIFFMCLFSVGSSFSAGCRggSFLFTMS--RINLRIR 225
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVtnhsgsGGEEALRALNQAVLILLGVVLIGSIATFLR--SWLFTLAgeRVVARLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 226 EQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAA 305
Cdd:cd18780 79 KRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 306 EKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALG 385
Cdd:cd18780 159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 386 MQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18780 239 AIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
151-442 |
5.59e-47 |
|
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: 168.11 E-value: 5.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVWGETLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIREQLFS 230
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 231 SLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYN 310
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 311 PRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQVLI 390
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 37572301 391 LNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
154-442 |
1.08e-46 |
|
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: 167.31 E-value: 1.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 154 AFFFLVVAVWGETLIPRYSGRVIDILGGDFDPDAFAS------AIFFMCLFSVGSSFSAGcrgGSFLFTMS--RINLRIR 225
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGlslktfALALLGVFVVGAAANFG---RVYLLRIAgeRIVARLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 226 EQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAA 305
Cdd:cd18573 78 KRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 306 EKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALG 385
Cdd:cd18573 158 AVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 386 MQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18573 238 SLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
446-699 |
3.85e-46 |
|
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: 172.63 E-value: 3.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 446 LDRKPNLPQPGILAPPwlEGRVEFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQ 525
Cdd:COG4618 312 LAAVPAEPERMPLPRP--KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 526 LLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAY----------------GLRDcedaqvmaaaqaacaddFIG 589
Cdd:COG4618 389 VRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARfgdadpekvvaaaklaGVHE-----------------MIL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 590 EMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQAL----QNWRSQGdRTMLVIAHRLHTV 665
Cdd:COG4618 452 RLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALaaaiRALKARG-ATVVVITHRPSLL 530
|
250 260 270
....*....|....*....|....*....|....
gi 37572301 666 QNADQVLVLKQGRLVEHDqlrDGQDVYAHLVQQR 699
Cdd:COG4618 531 AAVDKLLVLRDGRVQAFG---PRDEVLARLARPA 561
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
169-681 |
1.03e-45 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 172.00 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 169 PRYSGRVIDILGGDfdPDAFASAIFFMClFSVGS--SFSAGCRGGSFLFTMSRINLRirEQLFSSLLRQDLGFFQETKTG 246
Cdd:TIGR01192 39 PILFGRIIDAISSK--SDVLPTLALWAG-FGVFNtiAYVLVAREADRLAHGRRATLL--TEAFGRIISMPLSWHQQRGTS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 247 E-LNSRLSSDTSLMSRWLPFnANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRH---QAVLKEIQD 322
Cdd:TIGR01192 114 NaLHTLLRATETLFGLWLEF-MRQHLATFVALFLLIPTAFAMDWRLSIVLMVLGILYILIAKLVMQRTkngQAAVEHHYH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 323 AVAKAgqvVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQL------WWRrdlekdVYLVIRRVMALGMQVLILNCGVQ 396
Cdd:TIGR01192 193 NVFKH---VSDSISNVSVVHSYNRIEAETSALKQFTNNLLSAqypvldWWA------LASGLNRMASTISMMCILVIGTV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 397 QILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKVFSYLDRKPNLPQPGILAP-PWLEGRVEFQDVSFS 475
Cdd:TIGR01192 264 LVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPElPNVKGAVEFRHITFE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 476 YPRRPEKpvLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLF 555
Cdd:TIGR01192 344 FANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLF 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 556 SGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSA 635
Cdd:TIGR01192 422 NRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSA 501
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 37572301 636 LDAQCEQALQNWRS--QGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE 681
Cdd:TIGR01192 502 LDVETEARVKNAIDalRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIE 549
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
436-702 |
5.61e-45 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 170.03 E-value: 5.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 436 VGAAEKVFSYLDRKPNLPQPGILAPPWLEG-RVEFQDVS-FSyprrPE-KPVLQGLTFTLHPGTVTALVGPNGSGKST-V 511
Cdd:PRK11174 318 VGAAESLVTFLETPLAHPQQGEKELASNDPvTIEAEDLEiLS----PDgKTLAGPLNFTLPAGQRIALVGPSGAGKTSlL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 512 AALLQNL-YQptgGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGE 590
Cdd:PRK11174 394 NALLGFLpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 591 MTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQAL-----QNWRSQgdrTMLVIAHRLHTV 665
Cdd:PRK11174 471 LPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVmqalnAASRRQ---TTLMVTHQLEDL 547
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 37572301 666 QNADQVLVLKQGRLVE---HDQLRDGQDVYAHLVQQRLEA 702
Cdd:PRK11174 548 AQWDQIWVMQDGQIVQqgdYAELSQAGGLFATLLAHRQEE 587
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
468-679 |
3.49e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 157.67 E-value: 3.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFsypRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVL 547
Cdd:COG4619 2 ELEGLSF---RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 548 VGQEPVLFSGSVKDNIAYGLRdcedaQVMAAAQAACADDFIGEMtnGINTEIGEKG-GQLAVGQKQRLAIARALVRNPRV 626
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQ-----LRERKFDRERALELLERL--GLPPDILDKPvERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 627 LILDEATSALDAQ----CEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRL 679
Cdd:COG4619 152 LLLDEPTSALDPEntrrVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
344-700 |
4.49e-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: 165.85 E-value: 4.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 344 FGAEEQEVSRyKEALERCRQLWWRRDLEK--DVY-----------LVIRRVMALGMQVLILN--------CGVQQILA-- 400
Cdd:COG1123 107 EALENLGLSR-AEARARVLELLEAVGLERrlDRYphqlsggqrqrVAIAMALALDPDLLIADepttaldvTTQAEILDll 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 401 GEVTRGGLLSFLL---YQEEVGQYVRNLVYMYGDMLSNVGAAEKVFSY---LDRKPNLPQPGILAPPWLEGR---VEFQD 471
Cdd:COG1123 186 RELQRERGTTVLLithDLGVVAEIADRVVVMDDGRIVEDGPPEEILAApqaLAAVPRLGAARGRAAPAAAAAeplLEVRN 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 472 VSFSYP--RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDH---HYLHRQVV 546
Cdd:COG1123 266 LSKRYPvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQ 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPV--LFSG-SVKDNIAYGLRDCEDAQVMAAAQAacaddfIGEMTN--GINTEIGEK-GGQLAVGQKQRLAIARAL 620
Cdd:COG1123 346 MVFQDPYssLNPRmTVGDIIAEPLRLHGLLSRAERRER------VAELLErvGLPPDLADRyPHELSGGQRQRVAIARAL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 621 VRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEHDqlrDGQDVYA-- 693
Cdd:COG1123 420 ALEPKLLILDEPTSALDvsvqAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG---PTEEVFAnp 496
|
....*...
gi 37572301 694 -HLVQQRL 700
Cdd:COG1123 497 qHPYTRAL 504
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
468-679 |
4.92e-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: 155.84 E-value: 4.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVL 547
Cdd:cd03246 2 EVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 548 VGQEPVLFSGSVKDNIayglrdcedaqvmaaaqaacaddfigemtnginteigekggqLAVGQKQRLAIARALVRNPRVL 627
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 628 ILDEATSALDAQCE----QALQNWRSQGdRTMLVIAHRLHTVQNADQVLVLKQGRL 679
Cdd:cd03246 119 VLDEPNSHLDVEGEralnQAIAALKAAG-ATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
467-680 |
7.22e-44 |
|
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: 157.49 E-value: 7.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPV--LFSGSVKDNIAYGLRDcedaqvmaaaqaacaddfIG----EMTNGINtEIGEKGG----------QLAVGQ 610
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPEN------------------LGlpreEIRERVE-EALELVGlehladrpphELSGGQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 611 KQRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGdRTMLVIAHRLHTV-QNADQVLVLKQGRLV 680
Cdd:COG1122 140 KQRVAIAGVLAMEPEVLVLDEPTAGLDprgrRELLELLKRLNKEG-KTVIIVTHDLDLVaELADRVIVLDDGRIV 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
224-697 |
9.71e-43 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 167.13 E-value: 9.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 224 IREQLFSSLLRQDLGFFQETKT--GELNSRLSSDTSLMSRWLPFN----ANILLRSLVKVVGLYFFMLQVSPRLTFLSLL 297
Cdd:PTZ00265 901 MKRRLFENILYQEISFFDQDKHapGLLSAHINRDVHLLKTGLVNNivifTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFI 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 298 DLPL-----TIAA-----EKVYNPRHQAVLKEIQDAVAKAGQ-VVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWW 366
Cdd:PTZ00265 981 FMRVfairaRLTAnkdveKKEINQPGTVFAYNSDDEIFKDPSfLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQK 1060
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 367 RRDLEKDVYLVIRRVMALGMQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKVFSYL 446
Cdd:PTZ00265 1061 RKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLI 1140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 447 DRKPNLPQPG-----ILAPPWLEGRVEFQDVSFSYPRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLY-- 519
Cdd:PTZ00265 1141 IRKSNIDVRDnggirIKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdl 1220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 520 ----------QPTG------------------------------------------GQLLLDGEPLTEYDHHYLHRQVVL 547
Cdd:PTZ00265 1221 kndhhivfknEHTNdmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSI 1300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 548 VGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVL 627
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 628 ILDEATSALDAQCEQALQ----NWRSQGDRTMLVIAHRLHTVQNADQVLVL----KQGRLVE----HDQLRDGQD-VYAH 694
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEktivDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQahgtHEELLSVQDgVYKK 1460
|
...
gi 37572301 695 LVQ 697
Cdd:PTZ00265 1461 YVK 1463
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
223-699 |
1.22e-41 |
|
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: 163.96 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 223 RIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPrltFLSLLDLPLT 302
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATP---IAAVIIPPLG 1115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 303 IA---AEKVYnprhqavlkeiqdaVAKAGQVVR-EAVGGLQTVRSFGAEEQEVSRYKeALERCRQLWWRRDLEKDV---- 374
Cdd:TIGR00957 1116 LLyffVQRFY--------------VASSRQLKRlESVSRSPVYSHFNETLLGVSVIR-AFEEQERFIHQSDLKVDEnqka 1180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 375 ---YLVIRRVMALGMQvLILNCGVQ-QILAGEVTRGGLLSFLL-----YQEEVGQYVRNLVYMYGDMLSNVGAAEKVFSY 445
Cdd:TIGR00957 1181 yypSIVANRWLAVRLE-CVGNCIVLfAALFAVISRHSLSAGLVglsvsYSLQVTFYLNWLVRMSSEMETNIVAVERLKEY 1259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 446 LDRKPNLP-QPGILAPP--WLE-GRVEFQDVSFSYpRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQP 521
Cdd:TIGR00957 1260 SETEKEAPwQIQETAPPsgWPPrGRVEFRNYCLRY-REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINES 1338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 522 TGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNI----AYGLRDcedaqVMAAAQAACADDFIGEMTNGINT 597
Cdd:TIGR00957 1339 AEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYSDEE-----VWWALELAHLKTFVSALPDKLDH 1413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 598 EIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNW-RSQ-GDRTMLVIAHRLHTVQNADQVLVLK 675
Cdd:TIGR00957 1414 ECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTiRTQfEDCTVLTIAHRLNTIMDYTRVIVLD 1493
|
490 500
....*....|....*....|....
gi 37572301 676 QGRLVEHDQLrdgqdvyAHLVQQR 699
Cdd:TIGR00957 1494 KGEVAEFGAP-------SNLLQQR 1510
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
485-634 |
2.36e-41 |
|
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: 147.79 E-value: 2.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSG-SVKDNI 563
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 564 AYGLRDCEDAQVMAAAQAACADDFIGeMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATS 634
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
223-683 |
2.47e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 162.84 E-value: 2.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 223 RIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPrLTFLSLLDLPLT 302
Cdd:PLN03232 984 RLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVST-ISLWAIMPLLIL 1062
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 303 IAAEKVYnprHQAVLKEIQ--DAVAKAGQVVR--EAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRrDLEKDVYLVI 378
Cdd:PLN03232 1063 FYAAYLY---YQSTSREVRrlDSVTRSPIYAQfgEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLA-NTSSNRWLTI 1138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 379 RRVMALGMQVL------ILNCGVQQILAGEVTRGGLLsfLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKVFSYLDrkpnL 452
Cdd:PLN03232 1139 RLETLGGVMIWltatfaVLRNGNAENQAGFASTMGLL--LSYTLNITTLLSGVLRQASKAENSLNSVERVGNYID----L 1212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 453 PQ--PGILA---PP--W-LEGRVEFQDVSFSYprRPE-KPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTG 523
Cdd:PLN03232 1213 PSeaTAIIEnnrPVsgWpSRGSIKFEDVHLRY--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEK 1290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 524 GQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAyGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKG 603
Cdd:PLN03232 1291 GRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID-PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGG 1369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 604 GQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNWRSQGDR--TMLVIAHRLHTVQNADQVLVLKQGRLVE 681
Cdd:PLN03232 1370 ENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKscTMLVIAHRLNTIIDCDKILVLSSGQVLE 1449
|
..
gi 37572301 682 HD 683
Cdd:PLN03232 1450 YD 1451
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
438-698 |
2.26e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 156.52 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 438 AAEKVFSYLDRKPNLPQPGILAPPWLEGRVEFQDVSFSYPRRPEkPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQN 517
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 518 LYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIgEMTNGINT 597
Cdd:PRK11160 389 AWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLL-EDDKGLNA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 598 EIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCE-QALQNWRSQG-DRTMLVIAHRLHTVQNADQVLVLK 675
Cdd:PRK11160 468 WLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETErQILELLAEHAqNKTVLMITHRLTGLEQFDRICVMD 547
|
250 260
....*....|....*....|....*.
gi 37572301 676 QGRLVE---HDQLRDGQDVYAHLVQQ 698
Cdd:PRK11160 548 NGQIIEqgtHQELLAQQGRYYQLKQR 573
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
468-678 |
4.36e-40 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 146.46 E-value: 4.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVL 547
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 548 VGQEP--VLFSGSVKDNIAYGLRDCEDAQVmaaaqaacaddfigEMTNGINtEIGEKGG----------QLAVGQKQRLA 615
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLGLPEE--------------EIEERVE-EALELVGleglrdrspfTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 616 IARALVRNPRVLILDEATSALDAQ-CEQ---ALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGR 678
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAgRRElleLLKKLKAEG-KTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
468-702 |
6.69e-40 |
|
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: 146.93 E-value: 6.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLhRQVVL 547
Cdd:COG4555 3 EVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 548 VGQEPVLFSG-SVKDNI-----AYGLRDCEDAQVMAAAQAACaddfigEMTNGINTEIGEkggqLAVGQKQRLAIARALV 621
Cdd:COG4555 79 LPDERGLYDRlTVRENIryfaeLYGLFDEELKKRIEELIELL------GLEEFLDRRVGE----LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 622 RNPRVLILDEATSALD--AQCE--QALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEHDQLrdgQDVYAHLV 696
Cdd:COG4555 149 HDPKVLLLDEPTNGLDvmARRLlrEILRALKKEG-KTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSL---DELREEIG 224
|
....*.
gi 37572301 697 QQRLEA 702
Cdd:COG4555 225 EENLED 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
467-682 |
8.65e-40 |
|
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: 146.11 E-value: 8.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRP-EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHH---YLH 542
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 543 RQVVLVGQE------PVLfsgSVKDNIAYGLRdcedaQVMAAAQAACADDFIGEMTNGINTE---IGEKGGQLAVGQKQR 613
Cdd:cd03257 82 KEIQMVFQDpmsslnPRM---TIGEQIAEPLR-----IHGKLSKKEARKEAVLLLLVGVGLPeevLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37572301 614 LAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEH 682
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
462-683 |
2.09e-39 |
|
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: 144.09 E-value: 2.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 462 WLE-GRVEFQDVSFSY-PRRPekPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHH 539
Cdd:cd03369 1 WPEhGEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 540 YLHRQVVLVGQEPVLFSGSVKDNI-AYGLRDCEDAQVMAaaqaacaddfigemtngintEIGEKGGQLAVGQKQRLAIAR 618
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSGTIRSNLdPFDEYSDEEIYGAL--------------------RVSEGGLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 619 ALVRNPRVLILDEATSALDAQCEQALQN-WRSQ-GDRTMLVIAHRLHTVQNADQVLVLKQGRLVEHD 683
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKtIREEfTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
151-442 |
3.07e-39 |
|
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: 146.47 E-value: 3.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVavwgetliPRYSGRVIDILGGDFDPDAFAS-AIFFMCLFSVGSSFSAGcrgGSFLFTMS--RINLRIREQ 227
Cdd:cd18576 6 LLSSAIGLVF--------PLLAGQLIDAALGGGDTASLNQiALLLLGLFLLQAVFSFF---RIYLFARVgeRVVADLRKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 228 LFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEK 307
Cdd:cd18576 75 LYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 308 VYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQ 387
Cdd:cd18576 155 LFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 388 VLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18576 235 VAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
154-442 |
4.27e-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: 143.39 E-value: 4.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 154 AFFFLVVAVwGETL-IPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRggsFLFTMS---RINLRIREQLF 229
Cdd:cd18575 1 ALIALLIAA-AATLaLGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALR---FYLVSWlgeRVVADLRKAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 230 SSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVY 309
Cdd:cd18575 77 AHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 310 NPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERC-----RQLWWRRDLekdVYLVIrrVMAL 384
Cdd:cd18575 157 GRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAfaaalRRIRARALL---TALVI--FLVF 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 385 GMQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18575 232 GAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
467-701 |
5.86e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 140.97 E-value: 5.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRrpeKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEyDHHYLHRQVV 546
Cdd:COG1131 1 IEVRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNI-----AYGLRDCEDAQVmaaaqaacaddfIGEMTN--GINTEIGEKGGQLAVGQKQRLAIAR 618
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARER------------IDELLElfGLTDAADRKVGTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 619 ALVRNPRVLILDEATSALDAQCEQA----LQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEH---DQLRDGQ- 689
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRElwelLRELAAEG-KTVLLSTHYLEEAERlCDRVAIIDKGRIVADgtpDELKARLl 223
|
250
....*....|...
gi 37572301 690 -DVYAHLVQQRLE 701
Cdd:COG1131 224 eDVFLELTGEEAR 236
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
219-662 |
9.27e-38 |
|
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: 147.89 E-value: 9.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 219 RINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDT----SLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLT-- 292
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVdalqDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAag 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 293 -FLSLLDLPL-TIAAEKVYNPRHQAVLKEIQDAVakagqvvREAVGGLQTVRSFGAEEQEVSRYKEALERC-----RQLW 365
Cdd:TIGR02868 163 lLLAGFVAPLvSLRAARAAEQALARLRGELAAQL-------TDALDGAAELVASGALPAALAQVEEADRELtraerRAAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 366 WRRdLEKDVYLVIRRVMALGMQVLilncGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKVFSY 445
Cdd:TIGR02868 236 ATA-LGAALTLLAAGLAVLGALWA----GGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 446 LDRKPNLP---QPGILAPPWLEGRVEFQDVSFSYPRRPekPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPT 522
Cdd:TIGR02868 311 LDAAGPVAegsAPAAGAVGLGKPTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 523 GGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEK 602
Cdd:TIGR02868 389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEG 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37572301 603 GGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNWRSQGD--RTMLVIAHRL 662
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALsgRTVVLITHHL 530
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
467-684 |
7.00e-37 |
|
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: 137.70 E-value: 7.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLY-----QPTGGQLLLDGEPLTEYDHH-- 539
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 540 YLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIgeKGGQLAVGQKQRLAIARA 619
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRL--HALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 620 LVRNPRVLILDEATSALD----AQCEQALQNWRsqGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEHDQ 684
Cdd:cd03260 156 LANEPEVLLLDEPTSALDpistAKIEELIAELK--KEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGP 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
467-678 |
7.03e-37 |
|
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: 137.22 E-value: 7.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPE--KPVLQGLTFTLHPGTVTALVGPNGSGKSTV-AALLQNLyQPTGGQLlldgeplteydhhYLHR 543
Cdd:cd03250 1 ISVEDASFTWDSGEQetSFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGEL-EKLSGSV-------------SVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVVLVGQEPVLFSGSVKDNIAYG-----------LRDCEDAQVmaaaqaacaddfIGEMTNGINTEIGEKGGQLAVGQKQ 612
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGkpfdeeryekvIKACALEPD------------LEILPDGDLTEIGEKGINLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 613 RLAIARALVRNPRVLILDEATSALDAQ-----CEQALQNwRSQGDRTMLVIAHRLHTVQNADQVLVLKQGR 678
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHvgrhiFENCILG-LLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
468-678 |
1.19e-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: 134.68 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVL 547
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 548 VGQepvlFSGsvkdniayglrdcedaqvmaaaqaacaddfigemtnginteigekggqlavGQKQRLAIARALVRNPRVL 627
Cdd:cd00267 78 VPQ----LSG---------------------------------------------------GQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 628 ILDEATSALD----AQCEQALQNWRSQGdRTMLVIAHRLHTVQNA-DQVLVLKQGR 678
Cdd:cd00267 103 LLDEPTSGLDpasrERLLELLRELAEEG-RTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
467-687 |
1.80e-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: 137.24 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPE-KPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQV 545
Cdd:COG1124 2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 546 VLVGQEPvlfSGS------VKDNIAYGLRDCEDAQVMAAaqaacaddfIGEMTN--GINTEIGEK-GGQLAVGQKQRLAI 616
Cdd:COG1124 82 QMVFQDP---YASlhprhtVDRILAEPLRIHGLPDREER---------IAELLEqvGLPPSFLDRyPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 617 ARALVRNPRVLILDEATSALDA--QCE--QALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEHDQLRD 687
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVsvQAEilNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
467-681 |
6.56e-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: 134.91 E-value: 6.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYP-RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEydhhyLHRQV 545
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 546 VLVGQEPVLFS-GSVKDNIAYGLrdcedaqvmaaaqaacaddfigEMTNGINTEIGEKG-----------------GQLA 607
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGL----------------------ELQGVPKAEARERAeellelvglsgfenaypHQLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 608 VGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQN-----WRSQGdRTMLVIAHRLH-TVQNADQVLVLKQ--GRL 679
Cdd:cd03293 134 GGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEelldiWRETG-KTVLLVTHDIDeAVFLADRVVVLSArpGRI 212
|
..
gi 37572301 680 VE 681
Cdd:cd03293 213 VA 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
467-681 |
2.71e-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: 131.67 E-value: 2.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHyLHRQVV 546
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSGSVKDNIayglrdcedaqvmaaaqaacaddfigemtnginteigekGGQLAVGQKQRLAIARALVRNPRV 626
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 627 LILDEATSALDAQCEQALQN--WRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE 681
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSliFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
467-682 |
2.96e-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: 140.42 E-value: 2.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTG---GQLLLDGEPLTEYDHHYLHR 543
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVVLVGQEP--VLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIgemtnGINTEIGEKGGQLAVGQKQRLAIARALV 621
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAV-----GLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 622 RNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTV-QNADQVLVLKQGRLVEH 682
Cdd:COG1123 159 LDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVED 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
466-680 |
5.27e-35 |
|
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: 133.25 E-value: 5.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 466 RVEFQDVSFSYPRRPekpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQV 545
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 546 VLVGQEPVL-FSGSVKDNIAYGLRdcedaqvmaaaqaaCADDFIGEMTN-------------GInTEIGEKG-GQLAVGQ 610
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGRY--------------PHLGLFGRPSAedreaveealertGL-EHLADRPvDELSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 611 KQRLAIARALVRNPRVLILDEATSALD--AQCE--QALQNWRSQGDRTMLVIAHRL-HTVQNADQVLVLKQGRLV 680
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDlaHQLEvlELLRRLARERGRTVVMVLHDLnLAARYADRLVLLKDGRIV 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
467-679 |
8.25e-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: 130.21 E-value: 8.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRrpeKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEyDHHYLHRQVV 546
Cdd:cd03230 1 IEVRNLSKRYGK---KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNIAYGLrdcedaqvmaaaqaacaddfigemtnginteigekggqlavGQKQRLAIARALVRNPR 625
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKLSG-----------------------------------------GMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 626 VLILDEATSALD----AQCEQALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRL 679
Cdd:cd03230 116 LLILDEPTSGLDpesrREFWELLRELKKEG-KTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
467-680 |
2.26e-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: 132.17 E-value: 2.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG-EPLTEYDHHYLHRQV 545
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 546 VLVGQEP--VLFSGSVKDNIAYGL------RDcedaqvmaaaqaacaddfigEMTNGINTEIGEKG---------GQLAV 608
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLenlgvpRE--------------------EMRKRVDEALKLVGmedfrdrepHLLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 609 GQKQRLAIARALVRNPRVLILDEATSALDAQCE----QALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLV 680
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRkevlETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIV 215
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
210-697 |
2.72e-34 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 141.03 E-value: 2.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 210 GGSFLFTMSRINL--RIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQV 287
Cdd:PLN03130 972 LNSYWLIMSSLYAakRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIV 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 288 SPrLTFLSLLDLPLTIAAEKVYnprHQAVLKEIQ--DAVAKAGQVVR--EAVGGLQTVRSFGAEEQEVSRYKEALERCRQ 363
Cdd:PLN03130 1052 ST-ISLWAIMPLLVLFYGAYLY---YQSTAREVKrlDSITRSPVYAQfgEALNGLSTIRAYKAYDRMAEINGRSMDNNIR 1127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 364 lWWRRDLEKDVYLVIRRVMALGMQV-LILNCGV--------QQILAGevTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLS 434
Cdd:PLN03130 1128 -FTLVNMSSNRWLAIRLETLGGLMIwLTASFAVmqngraenQAAFAS--TMGLLLSYALNITSLLTAVLRLASLAENSLN 1204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 435 NVgaaEKVFSYLDRKP--------NLPQPGilappW-LEGRVEFQDVSFSYprRPE-KPVLQGLTFTLHPGTVTALVGPN 504
Cdd:PLN03130 1205 AV---ERVGTYIDLPSeaplvienNRPPPG-----WpSSGSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRT 1274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 505 GSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNI-----------------AYgL 567
Cdd:PLN03130 1275 GAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLdpfnehndadlweslerAH-L 1353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 568 RDCedaqvmaaaqaacaddfIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQN- 646
Cdd:PLN03130 1354 KDV-----------------IRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKt 1416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 647 ----WRSQgdrTMLVIAHRLHTVQNADQVLVLKQGRLVEHDQ----LRDGQDVYAHLVQ 697
Cdd:PLN03130 1417 ireeFKSC---TMLIIAHRLNTIIDCDRILVLDAGRVVEFDTpenlLSNEGSAFSKMVQ 1472
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
179-674 |
3.49e-34 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 140.55 E-value: 3.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 179 LGGDFDPDAFASAI--FFMCLFSVGSSFSAGcrggsflFTMSRINLRIREQLFSSLLRQDlGFFQETKTGelnSRLSSDT 256
Cdd:PTZ00265 92 LGENVNDIIFSLVLigIFQFILSFISSFCMD-------VVTTKILKTLKLEFLKSVFYQD-GQFHDNNPG---SKLTSDL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 257 SLMSRWLpfNANILLRSLV------KVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQV 330
Cdd:PTZ00265 161 DFYLEQV--NAGIGTKFITiftyasAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 331 VREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYL-----VIRRVMALGMQV---LILNCGVQQILAGE 402
Cdd:PTZ00265 239 IEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIgmingFILASYAFGFWYgtrIIISDLSNQQPNND 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 403 VTRGGLLSFLLyqeevGQYVRnlVYMYGDMLSNVG-------AAEKVFSYLDRKPNLP--QPGILAPPWleGRVEFQDVS 473
Cdd:PTZ00265 319 FHGGSVISILL-----GVLIS--MFMLTIILPNITeymksleATNSLYEIINRKPLVEnnDDGKKLKDI--KKIQFKNVR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 474 FSYPRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLL-DGEPLTEYDHHYLHRQVVLVGQEP 552
Cdd:PTZ00265 390 FHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDP 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 553 VLFSGSVKDNIAYGL---RDCEDAQVMAAAQAACADD------------------------------------------- 586
Cdd:PTZ00265 470 LLFSNSIKNNIKYSLyslKDLEALSNYYNEDGNDSQEnknkrnscrakcagdlndmsnttdsneliemrknyqtikdsev 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 587 -----------FIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQ----NWRSQG 651
Cdd:PTZ00265 550 vdvskkvlihdFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQktinNLKGNE 629
|
570 580
....*....|....*....|...
gi 37572301 652 DRTMLVIAHRLHTVQNADQVLVL 674
Cdd:PTZ00265 630 NRITIIIAHRLSTIRYANTIFVL 652
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
467-680 |
4.80e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 131.27 E-value: 4.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEP-VLFSGS-VKDNIAYGLRD-CEDAqvmaaaqaacaddfiGEMtNGINTEIGEKGG----------QLAVGQKQR 613
Cdd:PRK13632 87 IIFQNPdNQFIGAtVEDDIAFGLENkKVPP---------------KKM-KDIIDDLAKKVGmedyldkepqNLSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 614 LAIARALVRNPRVLILDEATSALDAQCE----QALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLV 680
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKreikKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
464-681 |
8.98e-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: 8.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 464 EGRVEFQDVSFSYPRRP-EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEydhhyLH 542
Cdd:COG1116 5 APALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 543 RQVVLVGQEPVLFs-gSVKDNIAYGLrdcEDAQVMAAAQAACADDFIGEMtnginteiGEKG------GQLAVGQKQRLA 615
Cdd:COG1116 80 PDRGVVFQEPALLpwlTVLDNVALGL---ELRGVPKAERRERARELLELV--------GLAGfedaypHQLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 616 IARALVRNPRVLILDEATSALDAQCEQALQN-----WRSQGdRTMLVIAH------RLhtvqnADQVLVLKQ--GRLVE 681
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDellrlWQETG-KTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
467-678 |
1.86e-33 |
|
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: 126.53 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYL-HRQV 545
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPpLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 546 V-LVGQEPVLFSG-SVKDNIAYGLrdcedaqvmaaaqaacaddfigemtNGinteigekggqlavGQKQRLAIARALVRN 623
Cdd:cd03229 78 IgMVFQDFALFPHlTVLENIALGL-------------------------SG--------------GQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 624 PRVLILDEATSALDAQC----EQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGR 678
Cdd:cd03229 119 PDVLLLDEPTSALDPITrrevRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
467-680 |
1.93e-33 |
|
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: 126.00 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPlteydhhylhrqvv 546
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 lvgqepVLFSgSVKDNIAyglrdcedaqvmaaaqaacaddfigemtNGINTEIgekggQLAVGQKQRLAIARALVRNPRV 626
Cdd:cd03216 64 ------VSFA-SPRDARR----------------------------AGIAMVY-----QLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 627 LILDEATSALDAQCEQAL----QNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:cd03216 104 LILDEPTAALTPAEVERLfkviRRLRAQG-VAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
467-683 |
3.74e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.90 E-value: 3.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPekpVLQGLTFTLHPGTVTALVGPNGSGKST-VAALLqNLYQPTGGQLLLDGEPLTEYDHH--YLHR 543
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTlLKAIL-GLLPPTSGTVRLFGKPPRRARRRigYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVVLVGQEPVlfsgSVKDNIAYGLRdcedaqvmaaaQAACADDFIG--------------EMTNGINTEIGEkggqLAVG 609
Cdd:COG1121 83 RAEVDWDFPI----TVRDVVLMGRY-----------GRRGLFRRPSradreavdealervGLEDLADRPIGE----LSGG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 610 QKQRLAIARALVRNPRVLILDEATSALDAQCEQA----LQNWRSQGdRTMLVIAHRLHTV-QNADQVLVLKQGRLVEHD 683
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEAlyelLRELRREG-KTILVVTHDLGAVrEYFDRVLLLNRGLVAHGP 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
467-683 |
4.39e-33 |
|
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: 126.48 E-value: 4.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHylHRQVV 546
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNIAYGLRDCEDAQVMAAAQAACADdfigEMTnGINTEIGEKGGQLAVGQKQRLAIARALVRNPR 625
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVPKAEIRARVRELL----ELV-GLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37572301 626 VLILDEATSALDAQCEQALQN-----WRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVEHD 683
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREelkelQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
463-683 |
2.45e-32 |
|
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: 125.79 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 463 LEGRVEFQDVSFSYPRRPeKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLH 542
Cdd:cd03288 16 LGGEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 543 RQVVLVGQEPVLFSGSVKDNIAyGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVR 622
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37572301 623 NPRVLILDEATSALDAQCEQALQN--WRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVEHD 683
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKvvMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECD 236
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
468-680 |
2.80e-32 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 123.31 E-value: 2.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFSYPRRPekpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVL 547
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 548 VGQ--EPVlfsgsvkdNIAYgLRDCEdaqvmaaaqaacaddfigemtngINTeigekggqLAVGQKQRLAIARALVRNPR 625
Cdd:cd03214 78 VPQalELL--------GLAH-LADRP-----------------------FNE--------LSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 626 VLILDEATSALDAQCEQA----LQNWRSQGDRTMLVIAHRL-HTVQNADQVLVLKQGRLV 680
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIEllelLRRLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
467-700 |
3.33e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 126.28 E-value: 3.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:PRK13635 6 IRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEP-VLFSGS-VKDNIAYGLRDCEDAQVmaaaqaacaddfigEMTNGINTEIGEKGGQ---------LAVGQKQRLA 615
Cdd:PRK13635 85 MVFQNPdNQFVGAtVQDDVAFGLENIGVPRE--------------EMVERVDQALRQVGMEdflnrephrLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 616 IARALVRNPRVLILDEATSALDAQCEQ----ALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE---------- 681
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRRevleTVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEegtpeeifks 230
|
250 260
....*....|....*....|.
gi 37572301 682 -HDQLRDGQDV-YAHLVQQRL 700
Cdd:PRK13635 231 gHMLQEIGLDVpFSVKLKELL 251
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
150-442 |
8.62e-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: 125.23 E-value: 8.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 150 FLIAAFFFLVVAVwGETLIPRYSGRVIDILGGDFDPDAfasaIFFMCLFSVGSSFsagCRG-GSFL--FTMSRINLRI-- 224
Cdd:cd18552 1 LALAILGMILVAA-TTAALAWLLKPLLDDIFVEKDLEA----LLLVPLAIIGLFL---LRGlASYLqtYLMAYVGQRVvr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 225 --REQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLT 302
Cdd:cd18552 73 dlRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 303 IAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRrdlekdvylvIRRVM 382
Cdd:cd18552 153 ALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMK----------IARAR 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 383 ALG---MQVL-------ILNCGVQQILAGEVTRGGLLSF-----LLYQEevgqyVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18552 223 ALSsplMELLgaiaialVLWYGGYQVISGELTPGEFISFitallLLYQP-----IKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
467-687 |
9.75e-32 |
|
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: 123.46 E-value: 9.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYP-RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYL---H 542
Cdd:cd03258 2 IELKNVSKVFGdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 543 RQVVLVGQEPVLFSG-SVKDNIAYGLRDCEDAQVMAAAQAACADDFIGemtnginteIGEKG----GQLAVGQKQRLAIA 617
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELVG---------LEDKAdaypAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 618 RALVRNPRVLILDEATSALDAQCEQA----LQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEHDQLRD 687
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSilalLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
468-677 |
1.72e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 121.87 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFSYPRRPekpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEydhhyLHRQVVL 547
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 548 VGQEPVL---FSGSVKDNIAYGLRdcedaqvmaaaqaaCADDFIG-----------------EMTNGINTEIGEkggqLA 607
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLY--------------GHKGLFRrlskadkakvdealervGLSELADRQIGE----LS 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 608 VGQKQRLAIARALVRNPRVLILDEATSALDAQCEQA----LQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQG 677
Cdd:cd03235 135 GGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDiyelLRELRREG-MTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
471-680 |
5.51e-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: 120.44 E-value: 5.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 471 DVSFSYPRRPEkpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDhhyLHRQVVLVGQ 550
Cdd:cd03226 4 NISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 551 EP--VLFSGSVKDNIAYGLRDCEDAqvmaaaqaacaddfiGEMTNGINTEIG-----EKGGQ-LAVGQKQRLAIARALVR 622
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAG---------------NEQAETVLKDLDlyalkERHPLsLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37572301 623 NPRVLILDEATSALDAQCEQALQNW----RSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELirelAAQG-KAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
467-690 |
1.14e-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: 120.30 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEP---LTEYDHHYLHR 543
Cdd:cd03261 1 IELRGLTKSFG---GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVVLVGQEPVLFSG-SVKDNIAYGLRdcedaqvmaaaqaacaddfigEMTNGINTEIGEK--------G---------GQ 605
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLR---------------------EHTRLSEEEIREIvlekleavGlrgaedlypAE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 606 LAVGQKQRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTV-QNADQVLVLKQGRLV 680
Cdd:cd03261 137 LSGGMKKRVALARALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIV 216
|
250
....*....|...
gi 37572301 681 EH---DQLRDGQD 690
Cdd:cd03261 217 AEgtpEELRASDD 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
467-679 |
1.18e-30 |
|
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: 119.90 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPEK-PVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDH----HYL 541
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 542 HRQVVLVGQEPVLFSG-SVKDNIAYGLRdceDAQVMAAAQAACADDFIGEMtnGINTEIGEKGGQLAVGQKQRLAIARAL 620
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLL---LAGVPKKERRERAEELLERV--GLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37572301 621 VRNPRVLILDEATSALDAQCEQA----LQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRL 679
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEvmelLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
173-410 |
6.69e-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: 120.27 E-value: 6.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 173 GRVIDILG----GDFDPDAFASAI----FFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIREQLFSSLLRQDLGFFQETK 244
Cdd:cd18577 23 GDLFDAFTdfgsGESSPDEFLDDVnkyaLYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 245 TGELNSRLSSDTSL----MSRWLPfnanILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEI 320
Cdd:cd18577 103 AGELTSRLTSDTNLiqdgIGEKLG----LLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 321 QDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQlwwrrdlekdvyLVIRRVMALGMQVLILNC------- 393
Cdd:cd18577 179 QEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARK------------AGIKKGLVSGLGLGLLFFiifamya 246
|
250 260
....*....|....*....|..
gi 37572301 394 -----GVQQILAGEVTRGGLLS 410
Cdd:cd18577 247 lafwyGSRLVRDGEISPGDVLT 268
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
151-442 |
8.03e-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: 119.46 E-value: 8.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVWGETLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIREQLFS 230
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 231 SLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYN 310
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 311 PRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQVLI 390
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 37572301 391 LNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
467-679 |
8.07e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.45 E-value: 8.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEP-VLFSG-SVKDNIAYGLRDCEDAQVMAAAQAACADDFIGeMTNGINTEigekGGQLAVGQKQRLAIARALVRNP 624
Cdd:PRK13650 85 MVFQNPdNQFVGaTVEDDVAFGLENKGIPHEEMKERVNEALELVG-MQDFKERE----PARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 625 RVLILDEATSALDAQCEQAL----QNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRL 679
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELiktiKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
467-681 |
8.73e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 117.45 E-value: 8.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPEK-PVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYL---- 541
Cdd:COG1136 5 LELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 542 HRQVVLVGQEPVLFSG-SVKDNIAYGLRdceDAQVMAAAQAACADDFIGEMtnGINTEIGEKGGQLAVGQKQRLAIARAL 620
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALPLL---LAGVSRKERRERARELLERV--GLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 621 VRNPRVLILDEATSALDAQ-CEQ---ALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE 681
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKtGEEvleLLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
466-678 |
1.39e-29 |
|
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: 116.42 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 466 RVEFQDVSFsypRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYlHRQV 545
Cdd:COG4133 2 MLEAENLSC---RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 546 VLVGQEPVLFSG-SVKDNIAYGLRdcedaQVMAAAQAACADDFIGEMtnGINTEIGEKGGQLAVGQKQRLAIARALVRNP 624
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRFWAA-----LYGLRADREAIDEALEAV--GLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 625 RVLILDEATSALDAQ----CEQALQNWRSQGdrTMLVIA-HRLHTVqNADQVLVLKQGR 678
Cdd:COG4133 151 PLWLLDEPFTALDAAgvalLAELIAAHLARG--GAVLLTtHQPLEL-AAARVLDLGDFK 206
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
467-687 |
3.50e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.59 E-value: 3.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGEPLTEYDHHYLHR 543
Cdd:PRK13640 6 VEFKHVSFTYPDS-KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVVLVGQEP-VLFSG-SVKDNIAYGLRDCEDAQVMAAAQAACADDFIGeMTNGINTEigekGGQLAVGQKQRLAIARALV 621
Cdd:PRK13640 85 KVGIVFQNPdNQFVGaTVGDDVAFGLENRAVPRPEMIKIVRDVLADVG-MLDYIDSE----PANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 622 RNPRVLILDEATSALD-AQCEQALQNWR---SQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVEHDQLRD 687
Cdd:PRK13640 160 VEPKIIILDESTSMLDpAGKEQILKLIRklkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
467-687 |
5.78e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.28 E-value: 5.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPekpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYD-HHYLHRQV 545
Cdd:COG1129 5 LEMRGISKSFGGVK---ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 546 VLVGQEPVLFSG-SVKDNIayglrdcedaqvmaaaqaacaddFIG-EMTN--------------------GINTEIGEKG 603
Cdd:COG1129 82 AIIHQELNLVPNlSVAENI-----------------------FLGrEPRRgglidwramrrrarellarlGLDIDPDTPV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 604 GQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQcE-----QALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQG 677
Cdd:COG1129 139 GDLSVAQQQLVEIARALSRDARVLILDEPTASLTER-EverlfRIIRRLKAQG-VAIIYISHRLDEVFEiADRVTVLRDG 216
|
250
....*....|
gi 37572301 678 RLVEHDQLRD 687
Cdd:COG1129 217 RLVGTGPVAE 226
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
152-413 |
1.38e-28 |
|
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: 116.11 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 152 IAAFFFLVVAVWgetlIPRYSGRVIDIL-------GGDFDPDAFASAIFFMCLFSVGSSFSAGCRggSFLFTMS-RINLR 223
Cdd:cd18574 3 LSALAAALVNIQ----IPLLLGDLVNVIsrslketNGDFIEDLKKPALKLLGLYLLQSLLTFAYI--SLLSVVGeRVAAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 224 IREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTI 303
Cdd:cd18574 77 LRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 304 AAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLwwrrdlekdvylviRRVMA 383
Cdd:cd18574 157 LVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKL--------------NEKLG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 37572301 384 LGMQV------LILNC--------GVQQILAGEVTRGGLLSFLL 413
Cdd:cd18574 223 LGIGIfqglsnLALNGivlgvlyyGGSLVSRGELTAGDLMSFLV 266
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
151-414 |
1.40e-28 |
|
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: 115.97 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVWGETLIPRYSGRVIDIL-GGDFDPDAFASAIFFMCLFSVGSsfsAGCRGGS--FLFTMSR-INLRIRE 226
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALtAGTLTASQLLRYALLILLLALLI---GIFRFLWryLIFGASRrIEYDLRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 227 QLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAE 306
Cdd:cd18541 78 DLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 307 KVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALercrqlwwRRDLEKDVYLVirRVMAL-- 384
Cdd:cd18541 158 YRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLN--------EEYVEKNLRLA--RVDALff 227
|
250 260 270
....*....|....*....|....*....|....*...
gi 37572301 385 -------GM-QVLILNCGVQQILAGEVTRGGLLSFLLY 414
Cdd:cd18541 228 pliglliGLsFLIVLWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
467-694 |
3.58e-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: 3.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEydhhyL---HR 543
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-----LppeKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVVLVGQEPVLFSG-SVKDNIAYGLRdcedaqvmaaaqaacaddfigeMTNGINTEIGEK----------GG-------Q 605
Cdd:COG3842 78 NVGMVFQDYALFPHlTVAENVAFGLR----------------------MRGVPKAEIRARvaellelvglEGladryphQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 606 LAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNW-----RSQGdRTMLVIAHRlhtvQN-----ADQVLVLK 675
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREElrrlqRELG-ITFIYVTHD----QEealalADRIAVMN 210
|
250
....*....|....*....
gi 37572301 676 QGRLVEHDqlrDGQDVYAH 694
Cdd:COG3842 211 DGRIEQVG---TPEEIYER 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
467-689 |
7.01e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 113.31 E-value: 7.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYpRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:PRK13648 8 IVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPV-LFSGS-VKDNIAYGLRDCEDAQVMAAAQAACADDFIgEMTNGINTEigekGGQLAVGQKQRLAIARALVRNP 624
Cdd:PRK13648 87 IVFQNPDnQFVGSiVKYDVAFGLENHAVPYDEMHRRVSEALKQV-DMLERADYE----PNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37572301 625 RVLILDEATSALDAQCEQAL----QNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE----HDQLRDGQ 689
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLldlvRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKegtpTEIFDHAE 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
466-683 |
8.01e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 112.82 E-value: 8.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 466 RVEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQNL--------YQPTGGQLLLDGEPLteYD 537
Cdd:COG1117 11 KIEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKST---LLRCLnrmndlipGARVEGEILLDGEDI--YD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 538 HHY----LHRQVVLVGQEPVLFSGSVKDNIAYGLRdcedaqvmaaaqaacaddfigemTNGINT-----EIGEK------ 602
Cdd:COG1117 83 PDVdvveLRRRVGMVFQKPNPFPKSIYDNVAYGLR-----------------------LHGIKSkseldEIVEEslrkaa 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 603 ------------GGQLAVGQKQRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSqgDRTMLVIAHRLHtvQ 666
Cdd:COG1117 140 lwdevkdrlkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELILELKK--DYTIVIVTHNMQ--Q 215
|
250 260
....*....|....*....|
gi 37572301 667 NA---DQVLVLKQGRLVEHD 683
Cdd:COG1117 216 AArvsDYTAFFYLGELVEFG 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
467-684 |
4.72e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 109.76 E-value: 4.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHH---YLHR 543
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVVLVGQE-PVLFSGSVKDNIAYGLRdcedaqvmaaaqaacaddFIGEMTNGINTEI---------GEKG----GQLAVG 609
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALPLR------------------VTGKSRKEIRRRVrevldlvglSDKAkalpHELSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 610 QKQRLAIARALVRNPRVLILDEATSALDAqcEQALQNWR------SQGdrTMLVIA-HRLHTVQNADQ-VLVLKQGRLVE 681
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDP--ETSWEIMElleeinRRG--TTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
...
gi 37572301 682 HDQ 684
Cdd:COG2884 218 DEA 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
467-694 |
4.98e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 112.52 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYP------RRPEKPV--LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDH 538
Cdd:COG4608 8 LEVRDLKKHFPvrgglfGRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 539 HYL---HRQVVLVGQEPvlfSGS------VKDNIAYGLRdcedaqvmaaaqaacaddfigemTNGINT--EIGEKGGQL- 606
Cdd:COG4608 88 RELrplRRRMQMVFQDP---YASlnprmtVGDIIAEPLR-----------------------IHGLASkaERRERVAELl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 607 -AV----------------GQKQRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTV 665
Cdd:COG4608 142 eLVglrpehadryphefsgGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQVLNLLEDLQDELGLTYLFISHDLSVV 221
|
250 260 270
....*....|....*....|....*....|
gi 37572301 666 QN-ADQVLVLKQGRLVEHDqlrDGQDVYAH 694
Cdd:COG4608 222 RHiSDRVAVMYLGKIVEIA---PRDELYAR 248
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
467-687 |
8.14e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 112.09 E-value: 8.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPEK-PVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLH--- 542
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 543 RQVVLVGQEPVLFSG-SVKDNIAYGLRdcedaqvmaaaqaacaddfigemTNGINTE--------------IGEKGG--- 604
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENVALPLE-----------------------IAGVPKAeirkrvaellelvgLSDKADayp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 605 -QLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQA----LQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGR 678
Cdd:COG1135 139 sQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSildlLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGR 218
|
....*....
gi 37572301 679 LVEHDQLRD 687
Cdd:COG1135 219 IVEQGPVLD 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
467-694 |
1.08e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.78 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPekpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTeYDHHYLHRQVV 546
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNIAYGLRDCEDAqvmaaaqaacaddfigemtngiNTEIGEK-----------G------GQLAV 608
Cdd:COG1118 79 FVFQHYALFPHmTVAENIAFGLRVRPPS----------------------KAEIRARveellelvqleGladrypSQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 609 GQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNW-----RSQGDRTMLVI-----AHRLhtvqnADQVLVLKQGR 678
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWlrrlhDELGGTTVFVThdqeeALEL-----ADRVVVMNQGR 211
|
250
....*....|....*.
gi 37572301 679 LVehdQLRDGQDVYAH 694
Cdd:COG1118 212 IE---QVGTPDEVYDR 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
484-687 |
1.47e-26 |
|
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: 108.58 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHylHRQVVLVGQEPVLFSG-SVKDN 562
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 563 IAYGLRdcedAQVMAAAQAACADDFIGEMTnGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQ 642
Cdd:cd03299 92 IAYGLK----KRKVDKKEIERKVLEIAEML-GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 37572301 643 ALQN----WRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEHDQLRD 687
Cdd:cd03299 167 KLREelkkIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
467-682 |
1.95e-26 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 108.16 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLT--EYDHHYLHRQ 544
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 545 VVLVGQEPVLFSG-SVKDNIAYGLRdcedaqvmaaaqaacaddfigeMTNGINTE--------------IGEKG----GQ 605
Cdd:COG1126 79 VGMVFQQFNLFPHlTVLENVTLAPI----------------------KVKKMSKAeaeeramellervgLADKAdaypAQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 606 LAVGQKQRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGdRTMLVIAHRLH---TVqnADQVLVLKQGR 678
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelvGEVLDVMRDLAKEG-MTMVVVTHEMGfarEV--ADRVVFMDGGR 213
|
....
gi 37572301 679 LVEH 682
Cdd:COG1126 214 IVEE 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
467-681 |
3.48e-26 |
|
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: 106.53 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEyDHHYLHRQVV 546
Cdd:cd03268 1 LKTNDLTKTYG---KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVgQEPVLFSG-SVKDNI-----AYGLRDCEdaqvmaaaqaacaddfIGEMTN--GINTEIGEKGGQLAVGQKQRLAIAR 618
Cdd:cd03268 77 LI-EAPGFYPNlTARENLrllarLLGIRKKR----------------IDEVLDvvGLKDSAKKKVKGFSLGMKQRLGIAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 619 ALVRNPRVLILDEATSALD----AQCEQALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRLVE 681
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDpdgiKELRELILSLRDQG-ITVLISSHLLSEIQKvADRIGIINKGKLIE 206
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
467-690 |
3.92e-26 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 107.37 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:COG1127 6 IEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVG---QEPVLFSG-SVKDNIAYGLRdcedaqvmaaaqaacaddfigEMTNGINTEIGEK--------G---------GQ 605
Cdd:COG1127 83 RIGmlfQGGALFDSlTVFENVAFPLR---------------------EHTDLSEAEIRELvleklelvGlpgaadkmpSE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 606 LAVGQKQRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDpitsAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKII 221
|
250
....*....|...
gi 37572301 681 EH---DQLRDGQD 690
Cdd:COG1127 222 AEgtpEELLASDD 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
467-692 |
4.38e-26 |
|
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: 107.32 E-value: 4.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHylHRQVV 546
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNIAYGLRDCEDAQVMAAAQAACADDFIGeMTNGINTEIGEKGGqlavGQKQRLAIARALVRNPR 625
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALDLVQ-LEGYANRKPSQLSG----GQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37572301 626 VLILDEATSALDAQCEQALQ-NWRSQGDRTMLVIAHRLHTVQNA----DQVLVLKQGRLvehDQLRDGQDVY 692
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQlELKRLQKELGITFVFVTHDQEEAltmsDRIAVMNKGKI---QQIGTPEEIY 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
485-682 |
6.42e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.04 E-value: 6.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYD-HHYLHRQVVLVGQEPVLFSG-SVKDN 562
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 563 IAYGLRDcedaqvmaaaqaaCADDFIGemTNGINTEIGEKG-------------GQLAVGQKQRLAIARALVRNPRVLIL 629
Cdd:COG3845 101 IVLGLEP-------------TKGGRLD--RKAARARIRELSerygldvdpdakvEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 630 DEATSALDAQcE-----QALQNWRSQGdRTMLVIAHRLHTV-QNADQVLVLKQGRLVEH 682
Cdd:COG3845 166 DEPTAVLTPQ-EadelfEILRRLAAEG-KSIIFITHKLREVmAIADRVTVLRRGKVVGT 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
484-680 |
7.73e-26 |
|
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: 107.05 E-value: 7.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHylhrQVVLVG-----QEPVLFSG- 557
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH----RIARLGiartfQNPRLFPEl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 SVKDNIAYGLRdCEDAQVMAAAQAACADDFIGEMTN-----------GINTEIGEKGGQLAVGQKQRLAIARALVRNPRV 626
Cdd:COG0411 95 TVLENVLVAAH-ARLGRGLLAALLRLPRARREEREAreraeellervGLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 627 LILDEATSALDAQcE-----QALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:COG0411 174 LLLDEPAAGLNPE-EteelaELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVI 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
467-694 |
8.24e-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: 8.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPekpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTeyDHHYLHRQVV 546
Cdd:cd03296 3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNIAYGLRdceDAQVMAAAQAACADDFIGEMTNGINTEIGEKG--GQLAVGQKQRLAIARALVRN 623
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLR---VKPRSERPPEAEIRAKVHELLKLVQLDWLADRypAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 624 PRVLILDEATSALDAQCEQALQNW-RSQGDR----TMLVIAHRLHTVQNADQVLVLKQGRLvehDQLRDGQDVYAH 694
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWlRRLHDElhvtTVFVTHDQEEALEVADRVVVMNKGRI---EQVGTPDEVYDH 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
470-681 |
1.58e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 106.69 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 470 QDVSFSYP------RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYD---HHY 540
Cdd:PRK10419 7 SGLSHHYAhgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 541 LHRQVVLVGQEP---VLFSGSVKDNIAYGLRDcedaqvMAAAQAACADDFIGEMTN--GINTEIGEK-GGQLAVGQKQRL 614
Cdd:PRK10419 87 FRRDIQMVFQDSisaVNPRKTVREIIREPLRH------LLSLDKAERLARASEMLRavDLDDSVLDKrPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37572301 615 AIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVE 681
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
484-691 |
1.75e-25 |
|
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: 105.60 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHylhrQVVLVG-----QEPVLFSG- 557
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH----EIARLGigrtfQIPRLFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 SVKDNIAYGLRdCEDAQVMAAAQAACADDFIGEMTNGINTEIG------EKGGQLAVGQKQRLAIARALVRNPRVLILDE 631
Cdd:cd03219 91 TVLENVMVAAQ-ARTGSGLLLARARREEREARERAEELLERVGladladRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 632 ATSALDAQCEQAL----QNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEH---DQLRDGQDV 691
Cdd:cd03219 170 PAAGLNPEETEELaeliRELRERG-ITVLLVEHDMDVVMSlADRVTVLDQGRVIAEgtpDEVRNNPRV 236
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
141-368 |
1.76e-25 |
|
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: 107.54 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 141 LKLSRPDLPFLIAAFFFLVVAvwGeTLIPRYS---GRVIDILGGDFDPDAFASAIFFMCLF---SVGSSFSAGCRGGSFL 214
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIA--G-AVFPVFAilfSKLISVFSLPDDDELRSEANFWALMFlvlAIVAGIAYFLQGYLFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 215 FTMSRINLRIREQLFSSLLRQDLGFFQETK--TGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVG-----LYFfmlqv 287
Cdd:cd18578 78 IAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAgliiaFVY----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 288 SPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWR 367
Cdd:cd18578 153 GWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLR 232
|
.
gi 37572301 368 R 368
Cdd:cd18578 233 R 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
483-683 |
3.75e-25 |
|
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: 104.05 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 483 PVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHY-LHRQVVLVGQEPVLFSG-SVK 560
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 561 DNI---AYGLRDCEdaqvMAAAQAACADDF--IGEMTNginteigEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSA 635
Cdd:cd03224 94 ENLllgAYARRRAK----RKARLERVYELFprLKERRK-------QLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 37572301 636 LD----AQCEQALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEHD 683
Cdd:cd03224 163 LApkivEEIFEAIRELRDEG-VTILLVEQNARFALEiADRAYVLERGRVVLEG 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
465-694 |
4.01e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 107.47 E-value: 4.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 465 GRVEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEydhhyL--- 541
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD-----Lppk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 542 HRQVVLVGQEPVLF-SGSVKDNIAYGLRdcedaqvmaaaqaacaddfigemTNG-----INTEIGE-------------K 602
Cdd:COG3839 74 DRNIAMVFQSYALYpHMTVYENIAFPLK-----------------------LRKvpkaeIDRRVREaaellgledlldrK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 603 GGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALqnwrsqgdRTMLViahRLH------TV-----QN---- 667
Cdd:COG3839 131 PKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEM--------RAEIK---RLHrrlgttTIyvthdQVeamt 199
|
250 260
....*....|....*....|....*...
gi 37572301 668 -ADQVLVLKQGRLVehdQLRDGQDVYAH 694
Cdd:COG3839 200 lADRIAVMNDGRIQ---QVGTPEELYDR 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
459-682 |
5.17e-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: 109.77 E-value: 5.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 459 APPWLEGRvefqDVSFSYP------RRPEKPV--LQGLTFTLHPGTVTALVGPNGSGKSTVA-ALLQnLyQPTGGQLLLD 529
Cdd:COG4172 272 APPLLEAR----DLKVWFPikrglfRRTVGHVkaVDGVSLTLRRGETLGLVGESGSGKSTLGlALLR-L-IPSEGEIRFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 530 GEPLTEYDHHYL-----HRQVVLvgQEPvlFSG-----SVKDNIAYGLRdcedaqvmaaaqaacaDDFIG-------EMT 592
Cdd:COG4172 346 GQDLDGLSRRALrplrrRMQVVF--QDP--FGSlsprmTVGQIIAEGLR----------------VHGPGlsaaerrARV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 593 NGINTEIG-----------EKGGqlavGQKQRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLV 657
Cdd:COG4172 406 AEALEEVGldpaarhryphEFSG----GQRQRIAIARALILEPKLLVLDEPTSALDvsvqAQILDLLRDLQREHGLAYLF 481
|
250 260
....*....|....*....|....*.
gi 37572301 658 IAHRLHTVQN-ADQVLVLKQGRLVEH 682
Cdd:COG4172 482 ISHDLAVVRAlAHRVMVMKDGKVVEQ 507
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
494-680 |
6.11e-25 |
|
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: 103.14 E-value: 6.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 494 PGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHyLH-----RQVVLVGQEPVLFSG-SVKDNIAYGL 567
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKK-INlppqqRKIGLVFQQYALFPHlNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 568 RDCEDAQVMAaaqaacaddFIGEMTN--GINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDA----QCE 641
Cdd:cd03297 101 KRKRNREDRI---------SVDELLDllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRalrlQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 37572301 642 QALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQ 211
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
468-700 |
1.08e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 104.15 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFSY------PRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYL 541
Cdd:COG4167 6 EVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 542 HRQVVLVGQEPvlfsgsvkdNIAY--GLRdcedaqvmaaaqaacaddfIGEMTNG---INTEIGEKGGQ----------- 605
Cdd:COG4167 86 CKHIRMIFQDP---------NTSLnpRLN-------------------IGQILEEplrLNTDLTAEEREerifatlrlvg 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 606 ------------LAVGQKQRLAIARALVRNPRVLILDEATSALDAQCeqalqnwRSQGDRTML-----------VIAHRL 662
Cdd:COG4167 138 llpehanfyphmLSSGQKQRVALARALILQPKIIIADEALAALDMSV-------RSQIINLMLelqeklgisyiYVSQHL 210
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 37572301 663 HTVQN-ADQVLVLKQGRLVEHDqlrDGQDVYA---HLVQQRL 700
Cdd:COG4167 211 GIVKHiSDKVLVMHQGEVVEYG---KTAEVFAnpqHEVTKRL 249
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
151-414 |
1.47e-24 |
|
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: 104.44 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVWGETLIPRYSGRVIDILGGDfdpDAFASAIFFMCLFSVGSSFSAGcrGGSFLFTMS--RINLRIREQL 228
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAG---GSSGGLLALLVALFLLQAVLSA--LSSYLLGRTgeRVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 229 FSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKV 308
Cdd:cd18551 76 WRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 309 YNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLekdVYLVIRRVMALGMQ- 387
Cdd:cd18551 156 LGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAK---IEALIGPLMGLAVQl 232
|
250 260
....*....|....*....|....*....
gi 37572301 388 --VLILNCGVQQILAGEVTRGGLLSFLLY 414
Cdd:cd18551 233 alLVVLGVGGARVASGALTVGTLVAFLLY 261
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
467-679 |
4.39e-24 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 100.68 E-value: 4.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLT--EYDHHYLHRQ 544
Cdd:cd03262 1 IEIKNLHKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 545 VVLVGQEPVLFSG-SVKDNIAYGLRdcEDAQVMAAAQAACADDFIGEMtnGINTEIGEKGGQLAVGQKQRLAIARALVRN 623
Cdd:cd03262 78 VGMVFQQFNLFPHlTVLENITLAPI--KVKGMSKAEAEERALELLEKV--GLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 624 PRVLILDEATSALD----AQCEQALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRL 679
Cdd:cd03262 154 PKVMLFDEPTSALDpelvGEVLDVMKDLAEEG-MTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
151-442 |
8.09e-24 |
|
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: 102.48 E-value: 8.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVWGETLIPRYSGRVIDIL------GGDFDPDAFASAIFFMCLFSVGSSFSagcrggSFL--FTMSRI-- 220
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIieglggGGGVDFSGLLRILLLLLGLYLLSALF------SYLqnRLMARVsq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 221 --NLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLD 298
Cdd:cd18547 75 rtVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 299 LPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWrrdleKDVYL-- 376
Cdd:cd18547 155 VPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASF-----KAQFYsg 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 377 ----VIRRVMALGmQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18547 230 llmpIMNFINNLG-YVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
151-414 |
8.82e-24 |
|
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: 102.08 E-value: 8.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVWGETLIPRYSGRVID--ILGGDFDPDA---FASAIFFMCLFSVGSSFsagcrGGSFLFTMS--RINLR 223
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDdyIVPGQGDLQGlllLALLYLGLLLLSFLLQY-----LQTYLLQKLgqRIIYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 224 IREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWlpFNANI--LLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPL 301
Cdd:cd18544 76 LRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNEL--FTSGLvtLIGDLLLLIGILIAMFLLNWRLALISLLVLPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 302 TIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALE-----RCRQLWWrrdlekdvYL 376
Cdd:cd18544 154 LLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQeyrkaNLKSIKL--------FA 225
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 37572301 377 VIRRVM----ALGMqVLILNCGVQQILAGEVTRGGLLSFLLY 414
Cdd:cd18544 226 LFRPLVellsSLAL-ALVLWYGGGQVLSGAVTLGVLYAFIQY 266
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
467-681 |
9.56e-24 |
|
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: 99.64 E-value: 9.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHylHRQVV 546
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNIAYGLRdcedAQVMAAAQAACADDFIGEMTnGINTEIGEKGGQLAVGQKQRLAIARALVRNPR 625
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGLK----LRKVPKDEIDERVREVAELL-QIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 626 VLILDEATSALDA----QCEQALQNWRSQGDRTMLVIAH-RLHTVQNADQVLVLKQGRLVE 681
Cdd:cd03301 151 VFLMDEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQ 211
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
151-442 |
1.13e-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: 101.79 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVWGETLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRggsfLFTMSRINLRI----RE 226
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLR----RYLAGRLSLGVehdlRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 227 QLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFnANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAE 306
Cdd:cd18543 77 DLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 307 KVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYL-VIRRVMALG 385
Cdd:cd18543 156 RRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWpLLEALPELG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 386 mQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18543 236 -LAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
467-665 |
1.16e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.88 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTG-----GQLLLDGEPLTE--YDHH 539
Cdd:PRK14258 8 IKVNNLSFYYD---TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 540 YLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARA 619
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 37572301 620 LVRNPRVLILDEATSALDA----QCEQALQNWRSQGDRTMLVIAHRLHTV 665
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPiasmKVESLIQSLRLRSELTMVIVSHNLHQV 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
473-680 |
1.66e-23 |
|
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: 99.36 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 473 SFSYPRRPEKpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGeplteYDHHYLHRQV-----VL 547
Cdd:cd03266 10 RFRDVKKTVQ-AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-----FDVVKEPAEArrrlgFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 548 VGQEPVLFSGSVKDNIAY-----GLRDCEDAQVMAAAQAACaddfigemtnGINTEIGEKGGQLAVGQKQRLAIARALVR 622
Cdd:cd03266 84 SDSTGLYDRLTARENLEYfaglyGLKGDELTARLEELADRL----------GMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37572301 623 NPRVLILDEATSALDAQCEQAL----QNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALrefiRQLRALG-KCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
467-694 |
2.42e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.80 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYP-RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYL---H 542
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 543 RQVVLVGQEPVLFSG-SVKDNIAYGLrdcedaqvmaaaqaacaddfigEMTNGINTEIGEK--------G---------G 604
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALPL----------------------ELAGTPKAEIKARvtellelvGlsdkadrypA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 605 QLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNWRSQGDR----TMLVIAHRLHTV-QNADQVLVLKQGRL 679
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelglTIVLITHEMDVVkRICDRVAVIDAGRL 219
|
250
....*....|....*
gi 37572301 680 VEHDQLrdgQDVYAH 694
Cdd:PRK11153 220 VEQGTV---SEVFSH 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
467-682 |
2.84e-23 |
|
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: 98.42 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRrpeKPVLQGLTFTLHPGtVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEyDHHYLHRQVV 546
Cdd:cd03264 1 LQLENLTKRYGK---KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNIAY-----GLRDCEDAQVmaaaqaacaddfIGEMTN--GINTEIGEKGGQLAVGQKQRLAIAR 618
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkGIPSKEVKAR------------VDEVLElvNLGDRAKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 619 ALVRNPRVLILDEATSALDAQCEQALQNWRSQ--GDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEH 682
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSElgEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFE 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
467-646 |
3.12e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 102.33 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHylHRQVV 546
Cdd:PRK09452 15 VELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNIAYGLRdcedaqvmaaaqaacaddfigeMTNGINTEIGE-----------------KGGQLAV 608
Cdd:PRK09452 90 TVFQSYALFPHmTVFENVAFGLR----------------------MQKTPAAEITPrvmealrmvqleefaqrKPHQLSG 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 37572301 609 GQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQN 646
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQN 185
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
481-681 |
3.98e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.99 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNL--YQPTGGQLLLDGEPLTEYD-HHYLHRQVVLVGQEPVLFSG 557
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSpDERARAGIFLAFQYPVEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 -SVKD--NIAYGLRDCEdaqvmaaaqAACADDFIGEMTN-----GINTEIGEKGgqLAV----GQKQRLAIARALVRNPR 625
Cdd:COG0396 92 vSVSNflRTALNARRGE---------ELSAREFLKLLKEkmkelGLDEDFLDRY--VNEgfsgGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37572301 626 VLILDEATSALDAqceQALQ------NWRSQGDRTMLVIAH--RLHTVQNADQVLVLKQGRLVE 681
Cdd:COG0396 161 LAILDETDSGLDI---DALRivaegvNKLRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVK 221
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
151-442 |
4.00e-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: 100.28 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVwGETLIPRY-SGRVID----ILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIR 225
Cdd:cd18563 1 LILGFLLMLLGT-ALGLVPPYlTKILIDdvliQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 226 EQLFSSLLRQDLGFFQETKTGELNSRLSSDTS----LMSRWLPFnaniLLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPL 301
Cdd:cd18563 80 RDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDrlqdFLSDGLPD----FLTNILMIIGIGVVLFSLNWKLALLVLIPVPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 302 TIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLwwRRDLEKdVYLVIRRV 381
Cdd:cd18563 156 VVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDA--NIRAEK-LWATFFPL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37572301 382 MALGMQ---VLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18563 233 LTFLTSlgtLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
459-680 |
4.98e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 103.21 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 459 APPWLEGRvefqDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDH 538
Cdd:PRK15439 8 APPLLCAR----SISKQYS---GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 539 HYLHR-QVVLVGQEPVLFSG-SVKDNIAYGLrdcedaqVMAAAQAACADDFIGEMTNGINTEIgeKGGQLAVGQKQRLAI 616
Cdd:PRK15439 81 AKAHQlGIYLVPQEPLLFPNlSVKENILFGL-------PKRQASMQKMKQLLAALGCQLDLDS--SAGSLEVADRQIVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 617 ARALVRNPRVLILDEATSALD-AQCE---QALQNWRSQGdRTMLVIAHRLHTV-QNADQVLVLKQGRLV 680
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLTpAETErlfSRIRELLAQG-VGIVFISHKLPEIrQLADRISVMRDGTIA 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
466-682 |
7.33e-23 |
|
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: 96.85 E-value: 7.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 466 RVEFQDVSFSYPRRP---EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALL--QNLYQPTGGQLLLDGEPLTEydhHY 540
Cdd:cd03213 3 TLSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 541 LHRQVVLVGQEPVLFSG-SVKDNIAY--GLRdcedaqvmaaaqaacaddfigemtnGINTeigekggqlavGQKQRLAIA 617
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLMFaaKLR-------------------------GLSG-----------GERKRVSIA 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 618 RALVRNPRVLILDEATSALDA----QCEQALQNWRSQGdRTMLVIAHRLHT--VQNADQVLVLKQGRLVEH 682
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSssalQVMSLLRRLADTG-RTIICSIHQPSSeiFELFDKLLLLSQGRVIYF 193
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
467-681 |
8.24e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.01 E-value: 8.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEP--VLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIgemtNGINTEIGEKgGQLAVGQKQRLAIARALVRNP 624
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAV----NMLDFKTREP-ARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 625 RVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE 681
Cdd:PRK13642 160 EIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIK 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
467-683 |
1.16e-22 |
|
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: 97.37 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRpeKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:cd03295 1 IEFENVTKRYGGG--KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNIAyglrdceDAQVMAAAQAACADDFIGEMTNGINTEIGEKGG----QLAVGQKQRLAIARALV 621
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIA-------LVPKLLKWPKEKIRERADELLALVGLDPAEFADryphELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 622 RNPRVLILDEATSALDAQCEQALQ----NWRSQGDRTMLVIAHRL-HTVQNADQVLVLKQGRLVEHD 683
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQeefkRLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVG 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
467-681 |
1.29e-22 |
|
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: 99.36 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPEK-PVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGEPLTEYDH---- 538
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 539 HYLHRQVVLVGQE------PVLfsgSVKDNIAYGLRDCEDAQVMAAAQAacaddfIGEMTN--GINTE---IGEKGGQLA 607
Cdd:COG0444 82 KIRGREIQMIFQDpmtslnPVM---TVGDQIAEPLRIHGGLSKAEARER------AIELLErvGLPDPerrLDRYPHELS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 608 VGQKQRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTV-QNADQVLVLKQGRLVE 681
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDvtiqAQILNLLKDLQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVE 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
467-680 |
2.06e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.50 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPEkpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:PRK13647 5 IEVEDLHFRYKDGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEP--VLFSGSVKDNIAYGLRDCEDAQVmaaaqaacaddfigEMTNGINTEIGEKGGQ---------LAVGQKQRLA 615
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNMGLDKD--------------EVERRVEEALKAVRMWdfrdkppyhLSYGQKKRVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 616 IARALVRNPRVLILDEATSALDAQCEQALQN--WR-SQGDRTMLVIAHRLH-TVQNADQVLVLKQGRLV 680
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEilDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVL 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
465-687 |
2.19e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 103.32 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 465 GRVEFQDVSFSYprRPEKP-VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHR 543
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVVLVGQEPVLFSGSVKDNI----------------AYGLRDcedaqvmaaaqaacaddFIGEMTNGINTEIGEKGGQLA 607
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVdpfleassaevwaaleLVGLRE-----------------RVASESEGIDSRVLEGGSNYS 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 608 VGQKQRLAIARALVRNPRVLIL-DEATS----ALDAQCEQALQNWRSQgdRTMLVIAHRLHTVQNADQVLVLKQGRLVEH 682
Cdd:PTZ00243 1448 VGQRQLMCMARALLKKGSGFILmDEATAnidpALDRQIQATVMSAFSA--YTVITIAHRLHTVAQYDKIIVMDHGAVAEM 1525
|
....*
gi 37572301 683 DQLRD 687
Cdd:PTZ00243 1526 GSPRE 1530
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
468-682 |
2.58e-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: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFSYPRRPekpvlqgLTFTLH--PGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHylHRQV 545
Cdd:COG3840 3 RLDDLTYRYGDFP-------LRFDLTiaAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 546 VLVGQEPVLFSG-SVKDNIAYGLR-DCEDAQVMAAAqaacaddfIGEMTN--GINTEIGEKGGQLAVGQKQRLAIARALV 621
Cdd:COG3840 74 SMLFQENNLFPHlTVAQNIGLGLRpGLKLTAEQRAQ--------VEQALErvGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 622 RNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEH 682
Cdd:COG3840 146 RKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAAD 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
468-688 |
3.73e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.55 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFsypRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVL 547
Cdd:PRK10247 9 QLQNVGY---LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 548 VGQEPVLFSGSVKDNIA--YGLRDcedaqvmaaaQAACADDFIGEMTN-GINTEIGEKG-GQLAVGQKQRLAIARALVRN 623
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIfpWQIRN----------QQPDPAIFLDDLERfALPDTILTKNiAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 624 PRVLILDEATSALDAQCEQ----ALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLkQGRLVEHDQLRDG 688
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHnvneIIHRYVREQNIAVLWVTHDKDEINHADKVITL-QPHAGEMQEARYE 223
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
479-682 |
3.99e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 98.11 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 479 RPEKPV--LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHY---LHRQVVLVGQEPV 553
Cdd:PRK11308 23 KPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 554 lfsGSVKDNIAYGlrdcedaqvmaaaqaacaddFIGEMTNGINTEIG-----EKGGQLAV------------------GQ 610
Cdd:PRK11308 103 ---GSLNPRKKVG--------------------QILEEPLLINTSLSaaerrEKALAMMAkvglrpehydryphmfsgGQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 611 KQRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEH 682
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDvsvqAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEK 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
484-681 |
6.56e-22 |
|
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: 94.90 E-value: 6.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYL-HRQVVLVGQEPVLFSG-SVKD 561
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPRlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 562 NIAYGLrdcedaqVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALD---- 637
Cdd:TIGR03410 95 NLLTGL-------AALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQpsii 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 37572301 638 AQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVE 681
Cdd:TIGR03410 168 KDIGRVIRRLRAEGGMAILLVEQYLDFARElADRYYVMERGRVVA 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
484-694 |
6.68e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.87 E-value: 6.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTeyDHHYLHRQVVLVGQEPVLFSG-SVKDN 562
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRDICMVFQSYALFPHmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 563 IAYGLRdcedaqvmaaaqaacaddfigeMTNGINTEIGEK----------GG-------QLAVGQKQRLAIARALVRNPR 625
Cdd:PRK11432 99 VGYGLK----------------------MLGVPKEERKQRvkealelvdlAGfedryvdQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37572301 626 VLILDEATSALDAQCEQALQN----WRSQGDRTMLVIAH-RLHTVQNADQVLVLKQGRLVehdQLRDGQDVYAH 694
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREkireLQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIM---QIGSPQELYRQ 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
478-680 |
7.56e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 95.61 E-value: 7.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 478 RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQV-VLVGQEPVLFS 556
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRaVLPQHSSLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 557 GSVKDNIAYGLRDCEDAQVMAAAQAACAddfigeMTngiNTEIGEKGG----QLAVGQKQRLAIARALVR------NPRV 626
Cdd:PRK13548 91 FTVEEVVAMGRAPHGLSRAEDDALVAAA------LA---QVDLAHLAGrdypQLSGGEQQRVQLARVLAQlwepdgPPRW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 627 LILDEATSALD-AQCEQALQNWRSQGDR---TMLVIAHRLH-TVQNADQVLVLKQGRLV 680
Cdd:PRK13548 162 LLLDEPTSALDlAHQHHVLRLARQLAHErglAVIVVLHDLNlAARYADRIVLLHQGRLV 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
490-687 |
8.71e-22 |
|
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: 97.48 E-value: 8.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 490 FTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLteYDHHYLH------RQVVLVGQEPVLFSG-SVKDN 562
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIflpphrRRIGYVFQEARLFPHlSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 563 IAYGLRDCEDAQVMAAAQAacaddfIGEMTnGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQ 642
Cdd:COG4148 98 LLYGRKRAPRAERRISFDE------VVELL-GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 37572301 643 A----LQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEHDQLRD 687
Cdd:COG4148 171 EilpyLERLRDELDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAE 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
468-691 |
1.41e-21 |
|
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: 94.28 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFSYPRRPekpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYD-HHYLHRQVV 546
Cdd:COG0410 5 EVENLHAGYGGIH---VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNI---AYGLRDCEDAQVMAAAQAACaddF--IGEMTNginteigEKGGQLAVGQKQRLAIARAL 620
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLllgAYARRDRAEVRADLERVYEL---FprLKERRR-------QRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 621 VRNPRVLILDEATSALD----AQCEQALQNWRSQGdRTMLVIAHRLHTV-QNADQVLVLKQGRLVEH---DQLRDGQDV 691
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAplivEEIFEIIRRLNREG-VTILLVEQNARFAlEIADRAYVLERGRIVLEgtaAELLADPEV 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
467-680 |
1.93e-21 |
|
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: 93.34 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPeKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTeYDHHYLHRQVV 546
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNIAY-----GLRDCEDAQVMAAAQAacaddfIGEMTNGINTEIgekgGQLAVGQKQRLAIARAL 620
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLR------VLGLTDKANKRA----RTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 621 VRNPRVLILDEATSALDAQCEQALqnW----RSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAI--WdlilEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
470-680 |
1.99e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 94.41 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 470 QDVSFSYPRRPekpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYL--HR---- 543
Cdd:COG4559 5 ENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarRRavlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 ------------QVVLVGQEPVLFSGSVKDNIAyglRDCEDAqvmaaaqaacaddfigemtnginTEIGEKGG----QLA 607
Cdd:COG4559 82 qhsslafpftveEVVALGRAPHGSSAAQDRQIV---REALAL-----------------------VGLAHLAGrsyqTLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 608 VGQKQRLAIARALV-------RNPRVLILDEATSALD----AQCEQALQNWRSQGdRTMLVIAHRLH-TVQNADQVLVLK 675
Cdd:COG4559 136 GGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDlahqHAVLRLARQLARRG-GGVVAVLHDLNlAAQYADRILLLH 214
|
....*
gi 37572301 676 QGRLV 680
Cdd:COG4559 215 QGRLV 219
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
478-681 |
2.65e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 94.09 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 478 RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPvlfSG 557
Cdd:PRK15112 22 RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---ST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 SVKDNIAYG------LR-DCEDAQVMAAAQAACADDFIGEMTNGINTeigeKGGQLAVGQKQRLAIARALVRNPRVLILD 630
Cdd:PRK15112 99 SLNPRQRISqildfpLRlNTDLEPEQREKQIIETLRQVGLLPDHASY----YPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 631 EATSALDAQCEQALQNW-----RSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE 681
Cdd:PRK15112 175 EALASLDMSMRSQLINLmlelqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
467-680 |
2.74e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 94.37 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPEkpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLtEYDHHYL--HRQ 544
Cdd:PRK13639 2 LETRDLKYSYPDGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLleVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 545 VV-LVGQEP--VLFSGSVKDNIAYGlrdcedaqvmaaaqaacaddfigEMTNGINTE------------IGEKGGQ---- 605
Cdd:PRK13639 79 TVgIVFQNPddQLFAPTVEEDVAFG-----------------------PLNLGLSKEevekrvkealkaVGMEGFEnkpp 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 606 --LAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNWRSQGDRTMLVIAHRLHTVQ----NADQVLVLKQGRL 679
Cdd:PRK13639 136 hhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDlvpvYADKVYVMSDGKI 215
|
.
gi 37572301 680 V 680
Cdd:PRK13639 216 I 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
467-680 |
3.57e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.04 E-value: 3.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPR-RP-EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEY----DHHY 540
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 541 LHRQVVLVGQ--EPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIgemtnGINTEIGEKGG-QLAVGQKQRLAIA 617
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALV-----GISESLFEKNPfELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 618 RALVRNPRVLILDEATSALDAQCEQALQNWRS---QGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKklhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLV 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
467-679 |
4.79e-21 |
|
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: 92.09 E-value: 4.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHH---YLHR 543
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVVLVGQEPVLFSG-SVKDNIAYGLRDCEDAQVMAAAQAACADDFIGemtngINTEIGEKGGQLAVGQKQRLAIARALVR 622
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEVTGVPPREIRKRVPAALELVG-----LSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 623 NPRVLILDEATSALDAQCEQALQNWRSQGDR---TMLVIAHRLHTVQN-ADQVLVLKQGRL 679
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKagtTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
487-691 |
5.28e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.13 E-value: 5.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 487 GLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQ-VVLVGQEPVLFSG-------- 557
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgVVRTFQHVRLFREmtvienll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 -----SVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMtnGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEA 632
Cdd:PRK11300 103 vaqhqQLKTGLFSGLLKTPAFRRAESEALDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 633 TSALDAQCEQALQ----NWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEH---DQLRDGQDV 691
Cdd:PRK11300 181 AAGLNPKETKELDeliaELRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANgtpEEIRNNPDV 247
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
459-698 |
5.93e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.08 E-value: 5.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 459 APPWLegRVEFQDVSFSYPRR------PEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVA-ALLQNLyqPTGGQLLLDGE 531
Cdd:PRK15134 272 ASPLL--DVEQLQVAFPIRKGilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGlALLRLI--NSQGEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 532 PLTEYDHHYL---HRQVVLVGQEPvlFSG-----SVKDNIAYGLRdcedAQVMAAAQAACADDFIGEMTN-GINTEIGEK 602
Cdd:PRK15134 348 PLHNLNRRQLlpvRHRIQVVFQDP--NSSlnprlNVLQIIEEGLR----VHQPTLSAAQREQQVIAVMEEvGLDPETRHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 603 -GGQLAVGQKQRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQ 676
Cdd:PRK15134 422 yPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHDLHVVRAlCHQVIVLRQ 501
|
250 260
....*....|....*....|..
gi 37572301 677 GRLVEHDqlrDGQDVYAHLVQQ 698
Cdd:PRK15134 502 GEVVEQG---DCERVFAAPQQE 520
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
184-681 |
6.01e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 98.51 E-value: 6.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 184 DPdAFASAIFFMCLFsVGSSFSAGCRGGSFLfTMSRINLRIREQLFSSLLRQDLGFFQETK----TGELNSRLSSDTSLM 259
Cdd:PLN03232 335 DP-AWVGYVYAFLIF-FGVTFGVLCESQYFQ-NVGRVGFRLRSTLVAAIFHKSLRLTHEARknfaSGKVTNMITTDANAL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 260 SR--------W-LPFnanillRSLVKVVGLYffmLQVSPRLTFLSLLdLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQV 330
Cdd:PLN03232 412 QQiaeqlhglWsAPF------RIIVSMVLLY---QQLGVASLFGSLI-LFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGI 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 331 VREAVGGLQTVRSFGAEEQEVSRYKEAleRCRQLWWRRDLEKDVYLVIRRVMALGMQVLILNCGVQQILAGEVTRGGLLS 410
Cdd:PLN03232 482 INEILASMDTVKCYAWEKSFESRIQGI--RNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPARAFT 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 411 FLlyqeEVGQYVRNLVYMYGDMLSNVGAA-------EKVFSYLDR--KPNLP-QPGILAppwlegrVEFQDVSFSYPRRP 480
Cdd:PLN03232 560 SL----SLFAVLRSPLNMLPNLLSQVVNAnvslqriEELLLSEERilAQNPPlQPGAPA-------ISIKNGYFSWDSKT 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGK-STVAALLQNLYQPTGGQLLLDGeplteydhhylhrQVVLVGQEPVLFSGSV 559
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAETSSVVIRG-------------SVAYVPQVSWIFNATV 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 560 KDNIAYGlRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQ 639
Cdd:PLN03232 696 RENILFG-SDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 37572301 640 -CEQALQNWRSQG--DRTMLVIAHRLHTVQNADQVLVLKQGRLVE 681
Cdd:PLN03232 775 vAHQVFDSCMKDElkGKTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
467-680 |
7.92e-21 |
|
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: 91.19 E-value: 7.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRrpeKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHH------- 539
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNrigylpe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 540 ----YLHRQVvlvgQEPVLFSGSVKD-NIAYGLRDCEDAQVMAAaqaacaddfIGEMTNginteigEKGGQLAVGQKQRL 614
Cdd:cd03269 78 erglYPKMKV----IDQLVYLAQLKGlKKEEARRRIDEWLERLE---------LSEYAN-------KRVEELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 615 AIARALVRNPRVLILDEATSALDA----QCEQALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPvnveLLKDVIRELARAG-KTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
485-692 |
1.26e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 95.75 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPlteydHHY------LHRQVVLVGQE----PVL 554
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-----MRFasttaaLAAGVAIIYQElhlvPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 555 fsgSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMtnGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATS 634
Cdd:PRK11288 95 ---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 635 ALDAQCEQAL----QNWRSQGdRTMLVIAHRLHTV-QNADQVLVLKQGRLVE---------HDQL------RDGQDVY 692
Cdd:PRK11288 170 SLSAREIEQLfrviRELRAEG-RVILYVSHRMEEIfALCDAITVFKDGRYVAtfddmaqvdRDQLvqamvgREIGDIY 246
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
481-680 |
1.29e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.00 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSG-SV 559
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 560 KDNIAYGlrdcedaqvmaaaqAACADDFIGEMTN-------------GINTEIGEKGGQLAVGQKQRLAIARALVRNPRV 626
Cdd:PRK11231 94 RELVAYG--------------RSPWLSLWGRLSAednarvnqameqtRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 627 LILDEATSALDA--QCE--QALQNWRSQGdRTMLVIAHRLHTV-QNADQVLVLKQGRLV 680
Cdd:PRK11231 160 VLLDEPTTYLDInhQVElmRLMRELNTQG-KTVVTVLHDLNQAsRYCDHLVVLANGHVM 217
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
151-414 |
1.65e-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: 92.60 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVWGETLIPRYSGRVIDILGGdfdPDAFASAIFFMCLFSVGS-SFSAGCRGGSFLFtMSRINLR----IR 225
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTI---GSKSLGLLLGLALLLLGAyLLRALLNFLRIYL-NHVAEQKvvadLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 226 EQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAA 305
Cdd:cd18778 77 SDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 306 EKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLwwrrdlekdvYLVIRRVMA-- 383
Cdd:cd18778 157 AWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKA----------QLRAMKLWAif 226
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 37572301 384 ---------LGMqVLILNCGVQQILAGEVTRGGLLSFLLY 414
Cdd:cd18778 227 hplmefltsLGT-VLVLGFGGRLVLAGELTIGDLVAFLLY 265
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
467-680 |
1.69e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.22 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPEkpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLtEYDHH---YLHR 543
Cdd:PRK13636 6 LKVEELNYNYSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVVLVGQEP--VLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDfigemTNGINTEIGEKGGQLAVGQKQRLAIARALV 621
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALK-----RTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37572301 622 RNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQ-NADQVLVLKQGRLV 680
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
478-682 |
1.71e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.99 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 478 RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLtEYDHH---YLHRQVVLVGQEP-- 552
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVATVFQDPeq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 553 VLFSGSVKDNIAYGLRDCEDAQVmaaaqaacaddfigEMTNGINTEIGEKGGQ---------LAVGQKQRLAIARALVRN 623
Cdd:PRK13638 89 QIFYTDIDSDIAFSLRNLGVPEA--------------EITRRVDEALTLVDAQhfrhqpiqcLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37572301 624 PRVLILDEATSALD----AQCEQALQNWRSQGDRtMLVIAHRLHTV-QNADQVLVLKQGRLVEH 682
Cdd:PRK13638 155 ARYLLLDEPTAGLDpagrTQMIAIIRRIVAQGNH-VIISSHDIDLIyEISDAVYVLRQGQILTH 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
467-699 |
2.12e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.91 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYP-------------------RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQ---NLYQPTGG 524
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKST---LLKliaGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 525 QLLLDGE--PLTEydhhylhrqvVLVGQEPVLfsgSVKDNI-----AYGLRDCEdaqvmaaaqaacaddfIGEMTNGIN- 596
Cdd:COG1134 82 RVEVNGRvsALLE----------LGAGFHPEL---TGRENIylngrLLGLSRKE----------------IDEKFDEIVe 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 597 -TEIGEKGGQlAV-----GQKQRLAIARALVRNPRVLILDEATSALDAQ----CEQALQNWRSQGdRTMLVIAHRLHTVQ 666
Cdd:COG1134 133 fAELGDFIDQ-PVktyssGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRESG-RTVIFVSHSMGAVR 210
|
250 260 270
....*....|....*....|....*....|....
gi 37572301 667 N-ADQVLVLKQGRLVEHDQLRDGQDVYAHLVQQR 699
Cdd:COG1134 211 RlCDRAIWLEKGRLVMDGDPEEVIAAYEALLAGR 244
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
468-680 |
2.18e-20 |
|
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: 90.71 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFSYPRrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLH---RQ 544
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 545 VVLVGQEPVLFSG-SVKDNIAYGlrdcedaqvmaaaqaacaddFIGEMTN-----------------------GINTEIG 600
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSG--------------------RLGRRSTwrslfglfpkeekqralaalervGLLDKAY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 601 EKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALD-AQCEQALQNWRS---QGDRTMLViahRLHTVQ----NADQVL 672
Cdd:cd03256 140 QRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDpASSRQVMDLLKRinrEEGITVIV---SLHQVDlareYADRIV 216
|
....*...
gi 37572301 673 VLKQGRLV 680
Cdd:cd03256 217 GLKDGRIV 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
467-680 |
2.36e-20 |
|
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: 89.86 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTlhPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHylHRQVV 546
Cdd:cd03298 1 VRLDKIRFSYG---EQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNIAYGLrdcEDAQVMAAAQAACADDFIGEMtnGINTEIGEKGGQLAVGQKQRLAIARALVRNPR 625
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGL---SPGLKLTAEDRQAIEVALARV--GLAGLEKRLPGELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 626 VLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:cd03298 149 VLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
135-681 |
3.29e-20 |
|
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: 94.86 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 135 TLMKRLLKLSRPdlPFLIAAFFFLVVAVWGETLIprysGRVIDILGGDFDPDA-----FASAIFFMCLFSVGSSFSAGCR 209
Cdd:COG4615 2 NLLRLLLRESRW--LLLLALLLGLLSGLANAGLI----ALINQALNATGAALArllllFAGLLVLLLLSRLASQLLLTRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 210 GGSFLFtmsrinlRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSR---WLPFnaniLLRSLVKVVGLYFFMLQ 286
Cdd:COG4615 76 GQHAVA-------RLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQafvRLPE----LLQSVALVLGCLAYLAW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 287 VSPRLTFLSLLDLPLTIAaekVYNPRHQAVLKEIQDAvakagqvvREAVGGLQtvRSF-----GAEEQEVSR------YK 355
Cdd:COG4615 145 LSPPLFLLTLVLLGLGVA---GYRLLVRRARRHLRRA--------REAEDRLF--KHFralleGFKELKLNRrrrrafFD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 356 EALERCRQLWwrRDLEKDVYLVIRRVMALGmQVLILncGVQqilagevtrgGLLSFLL------YQEEVGQYVRNLVYMY 429
Cdd:COG4615 212 EDLQPTAERY--RDLRIRADTIFALANNWG-NLLFF--ALI----------GLILFLLpalgwaDPAVLSGFVLVLLFLR 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 430 GDMLSNVG----------AAEKV------FSYLDRKPNLPQPGILAPPWleGRVEFQDVSFSYPRRPEKP--VLQGLTFT 491
Cdd:COG4615 277 GPLSQLVGalptlsranvALRKIeelelaLAAAEPAAADAAAPPAPADF--QTLELRGVTYRYPGEDGDEgfTLGPIDLT 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 492 LHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYD-HHYlhRQ---VVLvgQEPVLFSGsvkdniAYGL 567
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNrEAY--RQlfsAVF--SDFHLFDR------LLGL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 568 RDcedaqvmaAAQAACADDFIGEMtngintEIGEK----GG-----QLAVGQKQRLAIARALVRNPRVLILDEATSALDA 638
Cdd:COG4615 425 DG--------EADPARARELLERL------ELDHKvsveDGrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDP 490
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 37572301 639 Q-----CEQALQNWRSQGdRTMLVIAHRLHTVQNADQVLVLKQGRLVE 681
Cdd:COG4615 491 EfrrvfYTELLPELKARG-KTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
467-680 |
5.44e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 89.76 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFsypRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQ----NLYQPTGGQLLLDGEPLTEYD----- 537
Cdd:COG1119 4 LELRNVTV---RRGGKTILDDISWTVKPGEHWAILGPNGAGKST---LLSlitgDLPPTYGNDVRLFGERRGGEDvwelr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 538 ----------HHYLH-----RQVVLVGqepvlFSGSVkdniayGL-RDCEDaqvmaaaqaacaddfigEMTN-------- 593
Cdd:COG1119 78 kriglvspalQLRFPrdetvLDVVLSG-----FFDSI------GLyREPTD-----------------EQRErarellel 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 594 -GINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALD-AQCEQ---ALQNWRSQGDRTMLVIAHRLHTVQNA 668
Cdd:COG1119 130 lGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDlGARELllaLLDKLAAEGAPTLVLVTHHVEEIPPG 209
|
250
....*....|...
gi 37572301 669 -DQVLVLKQGRLV 680
Cdd:COG1119 210 iTHVLLLKDGRVV 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
474-683 |
5.59e-20 |
|
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: 89.13 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 474 FSYPRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGE--PLTEYdHHYLHRQvvLVGQE 551
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsSLLGL-GGGFNPE--LTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 552 PVLFSGSVkdniaYGLRDCEdaqvmaaaqaacaddfIGEMTNGIN--TEIGEKG----GQLAVGQKQRLAIARALVRNPR 625
Cdd:cd03220 104 NIYLNGRL-----LGLSRKE----------------IDEKIDEIIefSELGDFIdlpvKTYSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37572301 626 VLILDEATSALDA----QCEQALQNWRSQGdRTMLVIAHRLHTV-QNADQVLVLKQGRLVEHD 683
Cdd:cd03220 163 ILLIDEVLAVGDAafqeKCQRRLRELLKQG-KTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
468-660 |
5.85e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.31 E-value: 5.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFSYP-RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDhhyLHRQVV 546
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG---ADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LvgQEPVLFSG-SVKDNIAYGLRDCEDAQVMAAAQAACADDFIGeMTNGINTEIGekggQLAVGQKQRLAIARALVRNPR 625
Cdd:COG4525 82 F--QKDALLPWlNVLDNVAFGLRLRGVPKAERRARAEELLALVG-LADFARRRIW----QLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 37572301 626 VLILDEATSALDAQC-EQA----LQNWRSQGdRTMLVIAH 660
Cdd:COG4525 155 FLLMDEPFGALDALTrEQMqellLDVWQRTG-KGVFLITH 193
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
460-680 |
6.85e-20 |
|
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: 89.31 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 460 PPWLEGRVEfqdvSFSYPRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGE-PLTEYDH 538
Cdd:cd03267 16 EPGLIGSLK----SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 539 HyLHRQVVLVGQE-------PVLFSGSVKDNIaYGLRDCEDAQVMAAaqaacaddfIGEMTNgINTEIGEKGGQLAVGQK 611
Cdd:cd03267 92 F-LRRIGVVFGQKtqlwwdlPVIDSFYLLAAI-YDLPPARFKKRLDE---------LSELLD-LEELLDTPVRQLSLGQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37572301 612 QRLAIARALVRNPRVLILDEATSALDAQCEQALQNWRSQGDR----TMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRergtTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
151-442 |
1.37e-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: 89.83 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVWGETLIPRYSGRVID--ILGGDFDPDAFASAIFFmcLFSVGSSFSAGCRGgsflFTMSRIN----LRI 224
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDeyIPNGDLSGLLIIALLFL--ALNLVNWVASRLRI----YLMAKVGqrilYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 225 REQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPfNANI-LLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTI 303
Cdd:cd18545 76 RQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLS-NGLInLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 304 AA----EKVYNPRHQAVLKEIQDAVAKagqvVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWR--RdLEKDVYLV 377
Cdd:cd18545 155 LVvfllRRRARKAWQRVRKKISNLNAY----LHESISGIRVIQSFAREDENEEIFDELNRENRKANMRavR-LNALFWPL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 378 IRRVMALGMqVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18545 230 VELISALGT-ALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
467-681 |
1.65e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 88.23 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLT--EYDHHYLHRQ 544
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 545 VVLVGQEPVLFSG-SVKDNIAYGLRdcEDAQVMAAAQAACADDFIGEMtnGINTEIGEKGGQLAVGQKQRLAIARALVRN 623
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGPL--RVRGASKEEAEKQARELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37572301 624 PRVLILDEATSALDAQCEQ-ALQNWRSQGDR--TMLVIAHRLHTVQN-ADQVLVLKQGRLVE 681
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHeVLKVMQDLAEEgmTMVIVTHEIGFAEKvASRLIFIDKGRIAE 216
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
190-414 |
2.69e-19 |
|
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: 89.16 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 190 SAIFFMCLFSVGSSFSAGCRGGSFLFTmSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANI 269
Cdd:cd18565 56 LGGLTVAAFLLESLFQYLSGVLWRRFA-QRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 270 LLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQ 349
Cdd:cd18565 135 IIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDF 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 350 EVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQVLILNCGVQQILAG------EVTRGGLLSFLLY 414
Cdd:cd18565 215 ERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFY 285
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
478-638 |
3.04e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.47 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 478 RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDH----HYL-HRQvvlvGQEP 552
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeacHYLgHRN----AMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 553 VLfsgSVKDNIAyglrdcedaqvmaaaqaacaddFIGEMTNGINTEIGE-------------KGGQLAVGQKQRLAIARA 619
Cdd:PRK13539 87 AL---TVAENLE----------------------FWAAFLGGEELDIAAaleavglaplahlPFGYLSAGQKRRVALARL 141
|
170
....*....|....*....
gi 37572301 620 LVRNPRVLILDEATSALDA 638
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDA 160
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
475-674 |
3.12e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 475 SYPRRPekpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLlldgeplteydHHYLHRQVVLVGQ---E 551
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 552 PVLFSGSVKDNIAYGLrdCEDAQVMAAAQAACADDFIGEMTN-GINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILD 630
Cdd:NF040873 67 PDSLPLTVRDLVAMGR--WARRGLWRRLTRDDRAAVDDALERvGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 37572301 631 EATSALDAQCEQA----LQNWRSQGdRTMLVIAHRLHTVQNADQVLVL 674
Cdd:NF040873 145 EPTTGLDAESRERiialLAEEHARG-ATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
481-681 |
4.27e-19 |
|
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: 86.04 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNL--YQPTGGQLLLDGEPLTEYDHHYLHRQVVLVG-QEPVLFSG 557
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFLAfQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 sVKdNIAYgLRDCEdaqvmaaaqaacaDDFIGemtnginteigekggqlavGQKQRLAIARALVRNPRVLILDEATSALD 637
Cdd:cd03217 92 -VK-NADF-LRYVN-------------EGFSG-------------------GEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 37572301 638 ----AQCEQALQNWRSQGdRTMLVIAH--RLHTVQNADQVLVLKQGRLVE 681
Cdd:cd03217 137 idalRLVAEVINKLREEG-KSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
489-681 |
6.58e-19 |
|
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: 87.31 E-value: 6.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 489 TFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYL----HRQVVLVGQEPVLFSG-SVKDNI 563
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 564 AYGLrdcEDAQVMAAAQAACADDFIGEMtnGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQA 643
Cdd:cd03294 124 AFGL---EVQGVPRAEREERAAEALELV--GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 37572301 644 LQN--WRSQGD--RTMLVIAHRL-HTVQNADQVLVLKQGRLVE 681
Cdd:cd03294 199 MQDelLRLQAElqKTIVFITHDLdEALRLGDRIAIMKDGRLVQ 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
467-680 |
8.36e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 8.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYprRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEP--VLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIgemtnGINTEIGEKGGQLAVGQKQRLAIARALVRNP 624
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 625 RVLILDEATSALDAQCEQALQNWRSQGDRT--MLVI--AHRLHTV-QNADQVLVLKQGRLV 680
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIfsTHQLDLVpEMADYIYVMDKGRIV 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
467-683 |
9.53e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.19 E-value: 9.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSY-PRRP-EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHY---- 540
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 541 LHRQVVLVGQ--EPVLFSGSVKDNIAYGLRDcedAQVMAAAQAACADDFIGEMtnGINTEIGEKGG-QLAVGQKQRLAIA 617
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKN---FGFSEDEAKEKALKWLKKV--GLSEDLISKSPfELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 618 RALVRNPRVLILDEATSALDA----QCEQALQNWRSQGdRTMLVIAHRLHTV-QNADQVLVLKQGRLVEHD 683
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPegrkEMMQLFKDYQKAG-HTVILVTHNMDDVaEYADDVLVLEHGKLIKHA 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
482-637 |
9.75e-19 |
|
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: 85.67 E-value: 9.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 482 KPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYD-HHYLHRQVVLVGQEPVLFSG-SV 559
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 560 KDNIAYGLrdcEDAQVMAAAQAACADDFIGEMtnGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALD 637
Cdd:cd03218 93 EENILAVL---EIRGLSKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
481-681 |
1.38e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.87 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQ------PTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVL 554
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 555 FSG-SVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEAT 633
Cdd:PRK14246 102 FPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 37572301 634 SALDAQCEQALQNWRSQ--GDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVE 681
Cdd:PRK14246 182 SMIDIVNSQAIEKLITElkNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
467-692 |
1.87e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.45 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPekpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYdhHYLHRQVV 546
Cdd:PRK10851 3 IEIANIKKSFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNgiNTEIGEK-GGQLAVGQKQRLAIARALVRNP 624
Cdd:PRK10851 78 FVFQHYALFRHmTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQ--LAHLADRyPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37572301 625 RVLILDEATSALDAQCEQALQNWRSQGDR----TMLVIAH-RLHTVQNADQVLVLKQGRLvehDQLRDGQDVY 692
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEelkfTSVFVTHdQEEAMEVADRVVVMSQGNI---EQAGTPDQVW 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
484-687 |
2.08e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.35 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQ-----PTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEP-VLFSG 557
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 SVKDNIAYGLRDCEDAQVMAAAQAACADDF-IGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSAL 636
Cdd:PRK14247 98 SIFENVALGLKLNRLVKSKKELQERVRWALeKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 37572301 637 DAQCEQALQNWRSQGDRTMLVIAHRLHTVQNA---DQVLVLKQGRLVEHDQLRD 687
Cdd:PRK14247 178 DPENTAKIESLFLELKKDMTIVLVTHFPQQAArisDYVAFLYKGQIVEWGPTRE 231
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
218-442 |
3.26e-18 |
|
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: 86.03 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 218 SRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLL 297
Cdd:cd18564 83 QRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 298 DLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWR-RDLEKDVYL 376
Cdd:cd18564 163 VAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRaARLQALLSP 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 377 VIRRVMALGMqVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18564 243 VVDVLVAVGT-ALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
482-645 |
3.51e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 87.20 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 482 KPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHylHRQVVLVGQEPVLFSG-SVK 560
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 561 DNIAYGLRDCEDAQVMAAAQaacaddfIGEMTNGINTE--IGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDA 638
Cdd:PRK11607 110 QNIAFGLKQDKLPKAEIASR-------VNEMLGLVHMQefAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
....*..
gi 37572301 639 QCEQALQ 645
Cdd:PRK11607 183 KLRDRMQ 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
469-660 |
3.74e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 469 FQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGeplteydhhylHRQVVLV 548
Cdd:COG0488 1 LENLSKSFG---GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 549 GQEPVLFSG-SVKDNIAYG---LRDCEDAQVMAAAQAACADDFIGEMTNgINTEIGEKGG-------------------- 604
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGdaeLRALEAELEELEAKLAEPDEDLERLAE-LQEEFEALGGweaearaeeilsglgfpeed 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 605 ------QLAVGQKQRLAIARALVRNPRVLILDEATSALDAQC----EQALQNWRSqgdrTMLVIAH 660
Cdd:COG0488 146 ldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKNYPG----TVLVVSH 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
470-687 |
1.08e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.29 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 470 QDVSFSYPRrpeKPVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQNLYQ--------PTGGQLLLDGE----PLTeyD 537
Cdd:PRK14239 9 SDLSVYYNK---KKALNSVSLDFYPNEITALIGPSGSGKST---LLRSINRmndlnpevTITGSIVYNGHniysPRT--D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 538 HHYLHRQVVLVGQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIA 617
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 618 RALVRNPRVLILDEATSALD----AQCEQALQNWRSqgDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEHDQLRD 687
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDpisaGKIEETLLGLKD--DYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQ 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
472-689 |
1.12e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.21 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 472 VSFSYPRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDhhyLHRQVVLvGQE 551
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG---AERGVVF-QNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 552 PVLFSGSVKDNIAYGLRdcedaqvMAAAQAACADDFIGEMTNGINTEIGEKG--GQLAVGQKQRLAIARALVRNPRVLIL 629
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQ-------LAGVEKMQRLEIAHQMLKKVGLEGAEKRyiWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 630 DEATSALDAQCEQALQN-----WRSQGdRTMLVIAHRL-HTVQNADQVLVLK--QGRLVEHDQLRDGQ 689
Cdd:PRK11248 153 DEPFGALDAFTREQMQTlllklWQETG-KQVLLITHDIeEAVFMATELVLLSpgPGRVVERLPLNFAR 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
482-681 |
1.59e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.22 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 482 KPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGG-----QLLLDGEPLTEY-DHHYLHRQVVLVGQEPVLF 555
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 556 SGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSA 635
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 37572301 636 LDAQCEQALQNW-RSQGDR-TMLVIAHRL-HTVQNADQVLVLKQGRLVE 681
Cdd:PRK14271 194 LDPTTTEKIEEFiRSLADRlTVIIVTHNLaQAARISDRAALFFDGRLVE 242
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
209-686 |
1.95e-17 |
|
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: 87.27 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 209 RGGSFLFTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVS 288
Cdd:TIGR01271 945 RGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQ 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 289 PrLTFLSLLDLPLTIAAEKVYNPRHQAVLKEIQ-DAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWr 367
Cdd:TIGR01271 1025 P-YIFIAAIPVAVIFIMLRAYFLRTSQQLKQLEsEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWF- 1102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 368 rdlekdVYLVIRR--VMALGM-------QVLILNCGVQQILAGEVtrGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVga 438
Cdd:TIGR01271 1103 ------LYLSTLRwfQMRIDIifvfffiAVTFIAIGTNQDGEGEV--GIILTLAMNILSTLQWAVNSSIDVDGLMRSV-- 1172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 439 aEKVFSYLDRKPNLPQPG------------ILAPPWLE------GRVEFQDVSFSYPRrPEKPVLQGLTFTLHPGTVTAL 500
Cdd:TIGR01271 1173 -SRVFKFIDLPQEEPRPSggggkyqlstvlVIENPHAQkcwpsgGQMDVQGLTAKYTE-AGRAVLQDLSFSVEGGQRVGL 1250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 501 VGPNGSGKST-VAALLQNLyqPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSGSVKDNIAYGLR--DCEDAQVMA 577
Cdd:TIGR01271 1251 LGRTGSGKSTlLSALLRLL--STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQwsDEEIWKVAE 1328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 578 AAQAACAddfIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNWRSQ--GDRTM 655
Cdd:TIGR01271 1329 EVGLKSV---IEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQsfSNCTV 1405
|
490 500 510
....*....|....*....|....*....|.
gi 37572301 656 LVIAHRLHTVQNADQVLVLKQGRLVEHDQLR 686
Cdd:TIGR01271 1406 ILSEHRVEALLECQQFLVIEGSSVKQYDSIQ 1436
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
188-681 |
2.30e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 87.10 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 188 FASAIFfmclfsVGSSFSAGCRGGSFLFTMsRINLRIREQLFSSLLRQDLGFFQETK----TGELNSRLSSDT------- 256
Cdd:PLN03130 343 YAFSIF------VGVVLGVLCEAQYFQNVM-RVGFRLRSTLVAAVFRKSLRLTHEGRkkftSGKITNLMTTDAealqqic 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 257 -SLMSRW-LPFnanillRSLVKVVGLYFfmlQVSPRLTFLSLLdLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREA 334
Cdd:PLN03130 416 qQLHTLWsAPF------RIIIAMVLLYQ---QLGVASLIGSLM-LVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEV 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 335 VGGLQTVRSFGAEEQEVSRYKEAleRCRQLWWRRDLEKDVYLVIRRVMALGMQVLILNCGVQQILAGEVTRG-GLLSFLL 413
Cdd:PLN03130 486 LAAMDTVKCYAWENSFQSKVQTV--RDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGDLTPArAFTSLSL 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 414 YQeevgqYVRNLVYMYGDMLSNVGAA-------EKVFSYLDR--KPNLP-QPGILAppwlegrVEFQDVSFSYPRRPEKP 483
Cdd:PLN03130 564 FA-----VLRFPLFMLPNLITQAVNAnvslkrlEELLLAEERvlLPNPPlEPGLPA-------ISIKNGYFSWDSKAERP 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGK-STVAALLQNLYQPTGGQLLLDGeplteydhhylhrQVVLVGQEPVLFSGSVKDN 562
Cdd:PLN03130 632 TLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRG-------------TVAYVPQVSWIFNATVRDN 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 563 IAYGLrDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQ 642
Cdd:PLN03130 699 ILFGS-PFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 37572301 643 ALQNW---RSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE 681
Cdd:PLN03130 778 QVFDKcikDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
485-680 |
2.44e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.20 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYqPTGGQLLLDGEPLTEYDHHYL-HRQVVLVGQEPVLFSGSVKDNI 563
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELaRHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 564 AYGLRDCEDAQVMAAAQAACADDFigemtnGINTEIGEKGGQLAVGQKQRLAIARALVR-----NP--RVLILDEATSAL 636
Cdd:COG4138 91 ALHQPAGASSEAVEQLLAQLAEAL------GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptiNPegQLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 37572301 637 DAQCEQALQNW----RSQGdRTMLVIAHRL-HTVQNADQVLVLKQGRLV 680
Cdd:COG4138 165 DVAQQAALDRLlrelCQQG-ITVVMSSHDLnHTLRHADRVWLLKQGKLV 212
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
481-681 |
2.58e-17 |
|
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: 81.92 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALL--QNLYQPTGGQLLLDGEPLTEYD-HHYLHRQVVLVGQEPVLFSG 557
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEpDERARAGLFLAFQYPEEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 -SVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTN--GINTEIGEKGgqLAV----GQKQRLAIARALVRNPRVLILD 630
Cdd:TIGR01978 92 vSNLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLAllDMDEEFLNRS--VNEgfsgGEKKRNEILQMALLEPKLAILD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 631 EATSALD-----AQCEQaLQNWRSQgDRTMLVIAH--RLHTVQNADQVLVLKQGRLVE 681
Cdd:TIGR01978 170 EIDSGLDidalkIVAEG-INRLREP-DRSFLIITHyqRLLNYIKPDYVHVLLDGRIVK 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
481-679 |
2.66e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.42 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEydhhyLHRQVVLVGQEPVLFS-GSV 559
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRLMFQDARLLPwKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 560 KDNIAYGLRDCEDAQVMAAAQAAcaddfigemtnGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQ 639
Cdd:PRK11247 99 IDNVGLGLKGQWRDAALQALAAV-----------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 37572301 640 CEQALQN-----WRSQGdRTMLVIAHRL-HTVQNADQVLVLKQGRL 679
Cdd:PRK11247 168 TRIEMQDlieslWQQHG-FTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
152-416 |
2.75e-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: 82.92 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 152 IAAFFFLVVAVWGETLIPRY-SGRVID--ILGGDFDpdafasAIFFMCLFSVGSSFSAGCRG-GSFLFTmSRINLRI--- 224
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLlLREIIDdaLPQGDLG------LLVLLALGMVAVAVASALLGvVQTYLS-ARIGQGVmyd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 225 -REQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTI 303
Cdd:cd18550 74 lRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 304 AAEKVYNPRHQAVLKEIQDAVAKAGQVVRE--AVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRV 381
Cdd:cd18550 154 LPTRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGL 233
|
250 260 270
....*....|....*....|....*....|....*
gi 37572301 382 MALGMQVLILNCGVQQILAGEVTRGGLLSFLLYQE 416
Cdd:cd18550 234 FTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLG 268
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
467-680 |
3.17e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.34 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 -LVGQEP-VLFSG-SVKDNIAYGLRD-CEDAQvmaaaqaacaddfigEMTNGINTEIGEKG---------GQLAVGQKQR 613
Cdd:PRK13644 80 gIVFQNPeTQFVGrTVEEDLAFGPENlCLPPI---------------EIRKRVDRALAEIGlekyrhrspKTLSGGQGQC 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 614 LAIARALVRNPRVLILDEATSALDAQCEQA-LQNWRS--QGDRTMLVIAHRLHTVQNADQVLVLKQGRLV 680
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAvLERIKKlhEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
219-414 |
4.03e-17 |
|
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: 82.50 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 219 RINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRwLPFNA--NILLrSLVKVVGLYFFMLQVSPRLTFLSL 296
Cdd:cd18549 72 RIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISE-LAHHGpeDLFI-SIITIIGSFIILLTINVPLTLIVF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 297 LDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERcrqlwwRRDLEKDVYl 376
Cdd:cd18549 150 ALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDR------FLESKKKAY- 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 37572301 377 virRVMAL---GM-------QVLILNCGVQQILAGEVTRGGLLSFLLY 414
Cdd:cd18549 223 ---KAMAYffsGMnfftnllNLVVLVAGGYFIIKGEITLGDLVAFLLY 267
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
467-680 |
4.68e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.69 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYprRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHH---YLHR 543
Cdd:PRK10908 2 IRFEHVSKAY--LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVVLVGQE-PVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIgekggQLAVGQKQRLAIARALVR 622
Cdd:PRK10908 80 QIGMIFQDhHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPI-----QLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37572301 623 NPRVLILDEATSALDAQCEQALQNWRSQGDR---TMLVIAHRLHTVQNAD-QVLVLKQGRLV 680
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
479-639 |
6.13e-17 |
|
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: 79.84 E-value: 6.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 479 RPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYlHRQVVLVGQEPVLFSG- 557
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIKTTl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 SVKDNIAYGLRDCEdaqvmaaaqaacaddfigemTNGINTEIGEKG---------GQLAVGQKQRLAIARALVRNPRVLI 628
Cdd:cd03231 89 SVLENLRFWHADHS--------------------DEQVEEALARVGlngfedrpvAQLSAGQQRRVALARLLLSGRPLWI 148
|
170
....*....|.
gi 37572301 629 LDEATSALDAQ 639
Cdd:cd03231 149 LDEPTTALDKA 159
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
485-680 |
6.59e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGeplTEYDH--HYLHRQ--VVLVGQE-PVLFSGSV 559
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---INYNKldHKLAAQlgIGIIYQElSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 560 KDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTN--GINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSAL- 636
Cdd:PRK09700 98 LENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLt 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 37572301 637 DAQCEQ---ALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:PRK09700 178 NKEVDYlflIMNQLRKEG-TAIVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
478-639 |
6.61e-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: 6.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 478 RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYlHRQVVLVGQEPVLFSG 557
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 -SVKDNIAYGLRDCEDAQVMAAAQAacaddfigemtnginTEIGEKG------GQLAVGQKQRLAIARALVRNPRVLILD 630
Cdd:TIGR01189 88 lSALENLHFWAAIHGGAQRTIEDAL---------------AAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILD 152
|
....*....
gi 37572301 631 EATSALDAQ 639
Cdd:TIGR01189 153 EPTTALDKA 161
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
481-687 |
6.93e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.69 E-value: 6.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTeydhhYLHRQvvLVG---QEPVLFSG 557
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRR--RIGylpEERGLYPK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 -SVKDNIAY-----GLRDCEDAQVmaaaqaacaddfIGEMTN--GINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLIL 629
Cdd:COG4152 86 mKVGEQLVYlarlkGLSKAEAKRR------------ADEWLErlGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 630 DEATSALD--AQ--CEQALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEH---DQLRD 687
Cdd:COG4152 154 DEPFSGLDpvNVelLKDVIRELAAKG-TTVIFSSHQMELVEElCDRIVIINKGRKVLSgsvDEIRR 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
467-680 |
8.55e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 81.25 E-value: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSY-PRRP-EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTE--YDHHYLH 542
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 543 RQVVLVGQEP--VLFSGSVKDNIAYGLRDcedaqvmaaaqaacaddfIGEMTNGINTEIGEKGG---------------Q 605
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPIN------------------LGLSEEEIENRVKRAMNivgldyedykdkspfE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 606 LAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQAL----QNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEIlnkiKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCE 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
467-683 |
8.57e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 8.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLdGEPLTE-Y---DHHYLH 542
Cdd:COG0488 316 LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIgYfdqHQEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 543 RqvvlvgqepvlfSGSVKDNIAYGLRDcedAQVMAAAQAACADDFIGEMtngINTEIGEkggqLAVGQKQRLAIARALVR 622
Cdd:COG0488 392 P------------DKTVLDELRDGAPG---GTEQEVRGYLGRFLFSGDD---AFKPVGV----LSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 623 NPRVLILDEATSALD----AQCEQALQNWrsQGdrTMLVIAHRLHTVQN-ADQVLVLKQGRLVEHD 683
Cdd:COG0488 450 PPNVLLLDEPTNHLDietlEALEEALDDF--PG--TVLLVSHDRYFLDRvATRILEFEDGGVREYP 511
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
461-678 |
1.05e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.39 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 461 PWLEGRVEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHY 540
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 541 LHRqVVLVGQ----EPVLfsgSVKDNIAYGLRDCEDAQVMAAAQAACADDFiGEMTNGINTEIGEKGGqlavGQKQRLAI 616
Cdd:PRK13537 79 RQR-VGVVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEF-AKLENKADAKVGELSG----GMKRRLTL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 617 ARALVRNPRVLILDEATSALDAQCE----QALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGR 678
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARhlmwERLRSLLARG-KTILLTTHFMEEAERlCDRLCVIEEGR 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
467-687 |
1.25e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 80.98 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPR-RP-EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEY--DHHYLH 542
Cdd:PRK13646 3 IRFDNVSYTYQKgTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 543 -RQVV-LVGQ--EPVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADdfigeMTNGINTEIGEKGG-QLAVGQKQRLAIA 617
Cdd:PRK13646 83 vRKRIgMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLL-----MDLGFSRDVMSQSPfQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 618 RALVRNPRVLILDEATSALDAQCEQA----LQNWRSQGDRTMLVIAHRLHTV-QNADQVLVLKQGRLVEHDQLRD 687
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQvmrlLKSLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKE 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
480-677 |
1.59e-16 |
|
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: 78.91 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 480 PEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLL----LDGEPLTEYDHHYLHRQVVLVGQEPVLF 555
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 556 SGSVKDNIAYGlRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSA 635
Cdd:cd03290 92 NATVEENITFG-SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 37572301 636 LDAQC-----EQALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQG 677
Cdd:cd03290 171 LDIHLsdhlmQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
484-699 |
2.38e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 79.41 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQL-----LLDG-EPLTEYDH--HYLHRQVVLVGQEPVLF 555
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKGliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 556 SG-SVKDNIAYGLRDCEDAQVMAAAqaacaddfigEMTNGINTEIGEKGGQ------LAVGQKQRLAIARALVRNPRVLI 628
Cdd:PRK11264 98 PHrTVLENIIEGPVIVKGEPKEEAT----------ARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 629 LDEATSALDAQ-CEQALQNWRS--QGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEHDqlrDGQDVYAHLVQQR 699
Cdd:PRK11264 168 FDEPTSALDPElVGEVLNTIRQlaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG---PAKALFADPQQPR 239
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
467-702 |
2.87e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 79.68 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSY-PRRP-EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLT----EYDHHY 540
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 541 LHRQVVLVGQ--EPVLFSGSVKDNIAYG-----LRDCEDAQVMAaaqaacaddfigEMTN--GINTEIGEKGG-QLAVGQ 610
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGpmnfgVSEEDAKQKAR------------EMIElvGLPEELLARSPfELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 611 KQRLAIARALVRNPRVLILDEATSALDAQCEQAL----QNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVE---- 681
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMmemfYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLqgtp 230
|
250 260
....*....|....*....|....*....
gi 37572301 682 HDQLRDGQDVYAH--------LVQQRLEA 702
Cdd:PRK13634 231 REIFADPDELEAIgldlpetvKFKRALEE 259
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
466-681 |
3.01e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 82.33 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 466 RVEFQDVSFSYPRR--PEKPVlqglTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYD-HHYLH 542
Cdd:PRK10522 322 TLELRNVTFAYQDNgfSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQpEDYRK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 543 rqvvlvgqepvLFSGSVKDniaYGLRDCEDAQVMAAAQAACADDFIG--EMTNGINTEIGE-KGGQLAVGQKQRLAIARA 619
Cdd:PRK10522 398 -----------LFSAVFTD---FHLFDQLLGPEGKPANPALVEKWLErlKMAHKLELEDGRiSNLKLSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 620 LVRNPRVLILDEATSALDAQCE----QALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE 681
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRrefyQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
485-678 |
3.31e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.90 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYqPTG---GQLLLDGEPL-------TEydhhylHRQVVLVGQEPVL 554
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELqasnirdTE------RAGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 555 FSG-SVKDNIayglrdcedaqvmaaaqaacaddFIG-EMTNG--------------------INTEIGEKGGQLAVGQKQ 612
Cdd:PRK13549 94 VKElSVLENI-----------------------FLGnEITPGgimdydamylraqkllaqlkLDINPATPVGNLGLGQQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 613 RLAIARALVRNPRVLILDEATSALDAQCEQAL----QNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGR 678
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLTESETAVLldiiRDLKAHG-IACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
488-695 |
3.70e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.47 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 488 LTFTLH--PGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEplteyDHHYL---HRQVVLVGQEPVLFSG-SVKD 561
Cdd:PRK10771 16 MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppsRRPVSMLFQENNLFSHlTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 562 NIAYGLrdcEDAQVMAAAQAACADDFIGEMtnGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCE 641
Cdd:PRK10771 91 NIGLGL---NPGLKLNAAQREKLHAIARQM--GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37572301 642 QALQNWRSQ--GDR--TMLVIAHRLH-TVQNADQVLVLKQGRLV---EHDQLRDGQDVYAHL 695
Cdd:PRK10771 166 QEMLTLVSQvcQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAwdgPTDELLSGKASASAL 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
467-678 |
5.18e-16 |
|
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: 75.56 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGeplteydhhylhrqvv 546
Cdd:cd03221 1 IELENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 lvgqepvlfsgsvKDNIAYgLRdcedaqvmaaaqaacaddfigemtnginteigekggQLAVGQKQRLAIARALVRNPRV 626
Cdd:cd03221 62 -------------TVKIGY-FE------------------------------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 37572301 627 LILDEATSALDAQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGR 678
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
485-677 |
5.31e-16 |
|
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: 77.89 E-value: 5.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHylhRQVVLvgQEPVLFSG-SVKDNI 563
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD---RMVVF--QNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 564 AYGLrDCEDAQVMAAAQAACADDFIGEMtnGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQC--- 640
Cdd:TIGR01184 76 ALAV-DRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTrgn 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 37572301 641 --EQALQNWRSQGdRTMLVIAHRL-HTVQNADQVLVLKQG 677
Cdd:TIGR01184 153 lqEELMQIWEEHR-VTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
470-680 |
7.10e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 7.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 470 QDVSFSYPRRPekpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVG 549
Cdd:PRK10575 15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 550 QE-PVLFSGSVKDNIA------------YGLRDCEDAQVMAAAQaacaddfigemtnGINTEIGEKGGQLAVGQKQRLAI 616
Cdd:PRK10575 92 QQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEAISLV-------------GLKPLAHRLVDSLSGGERQRAWI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 617 ARALVRNPRVLILDEATSALDA--QCE-QALQNWRSQgDRTMLVIAhRLHTVQNA----DQVLVLKQGRLV 680
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIahQVDvLALVHRLSQ-ERGLTVIA-VLHDINMAarycDYLVALRGGEMI 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
467-674 |
7.32e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 75.65 E-value: 7.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLlldgeplteydHHYLHRQVV 546
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSGSVKDNIAYGLRDcedaqvmaaaqaacaddfigemtnginteigekggQLAVGQKQRLAIARALVRNPRV 626
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPWDD-----------------------------------VLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 37572301 627 LILDEATSALDAQCEQAL-QNWRSQGdRTMLVIAHRLHTVQNADQVLVL 674
Cdd:cd03223 113 VFLDEATSALDEESEDRLyQLLKELG-ITVISVGHRPSLWKFHDRVLDL 160
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
151-414 |
1.19e-15 |
|
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: 78.21 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVWGETLIPRYSGRVID--ILGGDFdpDAFASAIFFMCLFSVGSSFSAGCRGgsflFTMSRINLR----I 224
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDegIANGDL--SYILRTGLLMLLLALLGLIAGILAG----YFAAKASQGfgrdL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 225 REQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLpfnaNILLRSLVK----VVGLYFFMLQVSPRLTFLSLLDLP 300
Cdd:cd18548 75 RKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFV----MMLLRMLVRapimLIGAIIMAFRINPKLALILLVAIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 301 LTIAAekVY------NPRHQAVLKEIqDAVakaGQVVREAVGGLQTVRSFGAEEQEVSRYKEALErcrqlwwrrDLeKDV 374
Cdd:cd18548 151 ILALV--VFlimkkaIPLFKKVQKKL-DRL---NRVVRENLTGIRVIRAFNREDYEEERFDKAND---------DL-TDT 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 37572301 375 YLVIRRVMALGMQV--LILNCGV--------QQILAGEVTRGGLLSFLLY 414
Cdd:cd18548 215 SLKAGRLMALLNPLmmLIMNLAIvailwfggHLINAGSLQVGDLVAFINY 264
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
448-677 |
1.22e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 80.62 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 448 RKPNLPQPGILAPPwlEGRVEFQDVSFSYPRrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQ---NLYQPTGG 524
Cdd:COG4178 346 DALPEAASRIETSE--DGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKST---LLRaiaGLWPYGSG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 525 QLLL-DGEplteydhhylhrQVVLVGQEPVLFSGSVKDNIAYG--------------LRDCEdaqvmaaaqaacaddfIG 589
Cdd:COG4178 419 RIARpAGA------------RVLFLPQRPYLPLGTLREALLYPataeafsdaelreaLEAVG----------------LG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 590 EMTNGINTEiGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQAL-QNWRSQGDRTMLV-IAHRLHTVQN 667
Cdd:COG4178 471 HLAERLDEE-ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALyQLLREELPGTTVIsVGHRSTLAAF 549
|
250
....*....|
gi 37572301 668 ADQVLVLKQG 677
Cdd:COG4178 550 HDRVLELTGD 559
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
467-678 |
3.23e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTeyDHHYLHR-QV 545
Cdd:PRK13536 42 IDLAGVSKSYG---DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARaRI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 546 VLVGQEPVL-FSGSVKDN-IAYGlRDCEDAQVMAAAQAACADDFiGEMTNGINTEIGEKGGqlavGQKQRLAIARALVRN 623
Cdd:PRK13536 117 GVVPQFDNLdLEFTVRENlLVFG-RYFGMSTREIEAVIPSLLEF-ARLESKADARVSDLSG----GMKRRLTLARALIND 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 624 PRVLILDEATSALDAQCE----QALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGR 678
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARhliwERLRSLLARG-KTILLTTHFMEEAERlCDRLCVLEAGR 249
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
487-694 |
3.58e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.44 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 487 GLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLH---RQVVLVGQEPvLFS----GSV 559
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrSDIQMIFQDP-LASlnprMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 560 KDNIAYGLRDC--EDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGqlavGQKQRLAIARALVRNPRVLILDEATSALD 637
Cdd:PRK15079 118 GEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSG----GQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37572301 638 ----AQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEhdqLRDGQDVYAH 694
Cdd:PRK15079 194 vsiqAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE---LGTYDEVYHN 252
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
467-680 |
3.64e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.70 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYprRPEKP----VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHY-- 540
Cdd:PRK13643 2 IKFEKVNYTY--QPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKei 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 541 --LHRQVVLVGQEP--VLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGemtngINTEIGEKGG-QLAVGQKQRLA 615
Cdd:PRK13643 80 kpVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVG-----LADEFWEKSPfELSGGQMRRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 616 IARALVRNPRVLILDEATSALDAQCE-QALQNWRS--QGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARiEMMQLFESihQSGQTVVLVTHLMDDVADyADYVYLLEKGHII 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
467-684 |
5.85e-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: 74.78 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRrPEKPV--LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDH----HY 540
Cdd:COG4181 9 IELRGLTKTVGT-GAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdaraRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 541 LHRQVVLVGQ-EPVLFSGSVKDNIAY-----GLRDCEDAQVmaaaqaacaddfigemtnginTEIGEKG---------GQ 605
Cdd:COG4181 88 RARHVGFVFQsFQLLPTLTALENVMLplelaGRRDARARAR---------------------ALLERVGlghrldhypAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 606 LAVGQKQRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE 681
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDaatgEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
...
gi 37572301 682 HDQ 684
Cdd:COG4181 227 DTA 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
485-680 |
5.97e-15 |
|
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: 74.33 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEyDHHYLHRQVVLVGQEPVLfsgsvkDNIA 564
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV------DDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 565 YGLRDCEDAQVMAAAQAACADDFIGEMTNGIntEIGEKGGQLAV----GQKQRLAIARALVRNPRVLILDEATSALDAQC 640
Cdd:cd03265 89 TGWENLYIHARLYGVPGAERRERIDELLDFV--GLLEAADRLVKtysgGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 37572301 641 EQALqnWR------SQGDRTMLVIAHRLHTV-QNADQVLVLKQGRLV 680
Cdd:cd03265 167 RAHV--WEyieklkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRII 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
448-680 |
8.69e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 78.67 E-value: 8.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 448 RKPNLPQPGILAPPWLEGRVEFQDVSFSYPRrpekpvlqgltftlhpGTVTALVGPNGSGKSTvaaLLQNL---YQPTGG 524
Cdd:PTZ00243 655 RSAKTPKMKTDDFFELEPKVLLRDVSVSVPR----------------GKLTVVLGATGSGKST---LLQSLlsqFEISEG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 525 QLLLDgeplteydhhylhRQVVLVGQEPVLFSGSVKDNIAY-----------GLRDCEDAQVmaaaqaacaddfIGEMTN 593
Cdd:PTZ00243 716 RVWAE-------------RSIAYVPQQAWIMNATVRGNILFfdeedaarladAVRVSQLEAD------------LAQLGG 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 594 GINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQC-EQALQNW---RSQGdRTMLVIAHRLHTVQNAD 669
Cdd:PTZ00243 771 GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVEECflgALAG-KTRVLATHQVHVVPRAD 849
|
250
....*....|.
gi 37572301 670 QVLVLKQGRLV 680
Cdd:PTZ00243 850 YVVALGDGRVE 860
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
479-681 |
1.38e-14 |
|
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: 78.06 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 479 RPEKPVLQGLTFTLHPGTVTALVGPNGSGKST-VAALLQNLYQPTGgqllldgeplteydHHYLHRQVVLVGQEPVLFSG 557
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEMDKVEG--------------HVHMKGSVAYVPQQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 SVKDNIAYGlRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALD 637
Cdd:TIGR00957 714 SLRENILFG-KALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 37572301 638 AQC-----EQALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE 681
Cdd:TIGR00957 793 AHVgkhifEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISE 841
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
151-414 |
2.06e-14 |
|
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: 74.45 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVWGETLIPRYSGRVID--ILGGDFDPDAFASAIFFMC-----LFSVGSSFSAGCRGGSFLFTmsrinLR 223
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDsgVRAGDLGVLLLAAAAYLAVvlagwVAQRAQTRLTGRTGERLLYD-----LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 224 IReqLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTI 303
Cdd:cd18546 76 LR--VFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 304 AAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMA 383
Cdd:cd18546 154 LATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLG 233
|
250 260 270
....*....|....*....|....*....|.
gi 37572301 384 LGMQVLILNCGVQQILAGEVTRGGLLSFLLY 414
Cdd:cd18546 234 NLATAAVLLVGAWRVAAGTLTVGVLVAFLLY 264
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
484-685 |
3.46e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 72.54 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYD------------------HHYLHRQV 545
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakaelrnqklgfiyqfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 546 VLVG-QEPVLFSGSVKDNIAYGLRdcedaqvmaaaqaacaddfigEMTN--GINTEIGEKGGQLAVGQKQRLAIARALVR 622
Cdd:PRK11629 104 ALENvAMPLLIGKKKPAEINSRAL---------------------EMLAavGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 623 NPRVLILDEATSALDAQCE----QALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVEHDQL 685
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNAdsifQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
477-680 |
4.27e-14 |
|
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: 71.52 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 477 PRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTG---GQLLLDGEPLTEYDHHYlHRQVVLVGQE-- 551
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKY-PGEIIYVSEEdv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 552 --PVLfsgSVKDNIAYGLRdCEDaqvmaaaqaacaddfiGEMTNGINteigekggqlaVGQKQRLAIARALVRNPRVLIL 629
Cdd:cd03233 94 hfPTL---TVRETLDFALR-CKG----------------NEFVRGIS-----------GGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 630 DEATSALDA----QCEQALQnwrsqgdrtmlVIAHRLHTV------QNA-------DQVLVLKQGRLV 680
Cdd:cd03233 143 DNSTRGLDSstalEILKCIR-----------TMADVLKTTtfvslyQASdeiydlfDKVLVLYEGRQI 199
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
475-631 |
5.08e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 71.98 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 475 SYPRRPekpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHH--------YLhrqvv 546
Cdd:COG1137 12 SYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHkrarlgigYL----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 lvGQEPVLFSG-SVKDNIAYGLrdcEDAQVMAAAQAACADDFIGEMtnGInTEIGE-KGGQLAVGQKQRLAIARALVRNP 624
Cdd:COG1137 84 --PQEASIFRKlTVEDNILAVL---ELRKLSKKEREERLEELLEEF--GI-THLRKsKAYSLSGGERRRVEIARALATNP 155
|
....*..
gi 37572301 625 RVLILDE 631
Cdd:COG1137 156 KFILLDE 162
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
481-700 |
5.34e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVA-ALLQNLYQP----TGGQLLLDGEPLTEYDHHYLHR----QVVLVGQE 551
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 552 PVLfSGSVKDNIAYGLRDCEDAQVMAAAQAACaddfiGEMTN-----GIN---TEIGEKGGQLAVGQKQRLAIARALVRN 623
Cdd:PRK15134 101 PMV-SLNPLHTLEKQLYEVLSLHRGMRREAAR-----GEILNcldrvGIRqaaKRLTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 624 PRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTV-QNADQVLVLKQGRLVEHDQLRDGQDVYAHLVQQ 698
Cdd:PRK15134 175 PELLIADEPTTALDvsvqAQILQLLRELQQELNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
|
..
gi 37572301 699 RL 700
Cdd:PRK15134 255 KL 256
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
478-680 |
5.93e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.08 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 478 RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNlYQPTG----GQLLLDGEPLTEYDHH----YLHRQVVLVG 549
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKGvkgsGSVLLNGMPIDAKEMRaisaYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 550 ----QEPVLFSGSVK--------------DNI--AYGLRDCEdaqvmaaaqaacaddfigemtngiNTEIGEKGGQ--LA 607
Cdd:TIGR00955 113 tltvREHLMFQAHLRmprrvtkkekrervDEVlqALGLRKCA------------------------NTRIGVPGRVkgLS 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 608 VGQKQRLAIARALVRNPRVLILDEATSALDA----QCEQALQNWrSQGDRTMLVIAHR--LHTVQNADQVLVLKQGRLV 680
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLDSfmaySVVQVLKGL-AQKGKTIICTIHQpsSELFELFDKIILMAEGRVA 246
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
469-692 |
6.76e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 70.74 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 469 FQDVSFSYP-RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQNLYQPT-----GGQLLLDGEPLTEydhhYLH 542
Cdd:cd03232 6 WKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGRPLDK----NFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 543 RQVVLVGQEPVLFSGS-VKDNIAYG--LRDcedaqvmaaaqaacaddfigemtnginteigekggqLAVGQKQRLAIARA 619
Cdd:cd03232 79 RSTGYVEQQDVHSPNLtVREALRFSalLRG------------------------------------LSVEQRKRLTIGVE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 620 LVRNPRVLILDEATSALDAQCE----QALQNWRSQGdRTMLVIAHRLHTV--QNADQVLVLKQGrlvehdqlrdGQDVY 692
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAynivRFLKKLADSG-QAILCTIHQPSASifEKFDRLLLLKRG----------GKTVY 190
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
468-680 |
7.14e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.15 E-value: 7.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFSYPRRPEK-PVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHR--- 543
Cdd:PRK10535 6 ELKDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 -------------------QVVLVgqePVLFSGSVKDniayglrdcedaqvmaaAQAACADDFIGEMtnGINTEIGEKGG 604
Cdd:PRK10535 86 ehfgfifqryhllshltaaQNVEV---PAVYAGLERK-----------------QRLLRAQELLQRL--GLEDRVEYQPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 605 QLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQA----LQNWRSQGdRTMLVIAHRLHTVQNADQVLVLKQGRLV 680
Cdd:PRK10535 144 QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEvmaiLHQLRDRG-HTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
488-680 |
7.58e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 488 LTFTLHPGTVTALVGPNGSGKSTVAALLQNLYqPTGGQLLLDGEPLTEYDHHYL-HRQVVLVGQEPVLFSGSVKDNIAYG 566
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 567 LRDcedaqvmaAAQAACADDFIGEMTN--GINTEIGEKGGQLAVGQKQRLAIARALVR-----NP--RVLILDEATSALD 637
Cdd:PRK03695 94 QPD--------KTRTEAVASALNEVAEalGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 37572301 638 -AQ---CEQALQNWRSQGdRTMLVIAHRL-HTVQNADQVLVLKQGRLV 680
Cdd:PRK03695 166 vAQqaaLDRLLSELCQQG-IAVVMSSHDLnHTLRHADRVWLLKQGKLL 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
489-681 |
8.20e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.91 E-value: 8.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 489 TFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLH----RQVVLVGQEPVLFSG-SVKDNI 563
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 564 AYGLRDCEDAQVMAAAQAACADDFIG--EMTNGINTEigekggqLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCE 641
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGleNYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 37572301 642 QALQN----WRSQGDRTMLVIAHRL-HTVQNADQVLVLKQGRLVE 681
Cdd:PRK10070 201 TEMQDelvkLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQ 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
481-682 |
9.37e-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: 74.34 E-value: 9.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGKS-TVAALLQNLYQP---TGGQLLLDGEPLTEYDHHYLHR----QVVLVGQEP 552
Cdd:COG4172 22 TVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 553 V-----LFSgsVKDNIA------YGLRDCEDAQVmaaaqaacaddfIGEMTN--GI-NTE--IGEKGGQLAVGQKQRLAI 616
Cdd:COG4172 102 MtslnpLHT--IGKQIAevlrlhRGLSGAAARAR------------ALELLErvGIpDPErrLDAYPHQLSGGQRQRVMI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 617 ARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEH 682
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDvtvqAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQ 238
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
171-411 |
1.41e-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: 71.71 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 171 YSGRVID--ILGGDFDP-DAFASAIFFMCLFSVGSSFSAGcrggSFLFTMS-RINLRIREQLFSSLLRQDLGFFQETKTG 246
Cdd:cd18570 24 FFQILIDdiIPSGDINLlNIISIGLILLYLFQSLLSYIRS----YLLLKLSqKLDIRLILGYFKHLLKLPLSFFETRKTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 247 ELNSRLS---------SDTSLmsrwlpfnaNILLRSLVKVVGLyFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVL 317
Cdd:cd18570 100 EIISRFNdankireaiSSTTI---------SLFLDLLMVIISG-IILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 318 KEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQVLILNCGVQQ 397
Cdd:cd18570 170 REVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYL 249
|
250
....*....|....
gi 37572301 398 ILAGEVTRGGLLSF 411
Cdd:cd18570 250 VIKGQLSLGQLIAF 263
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
151-411 |
1.48e-13 |
|
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: 71.85 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFfflVVAVWGeTLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIREQLFS 230
Cdd:cd18782 8 LALSF---VVQLLG-LANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 231 SLLRQDLGFFQETKTGELNSRLsSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYN 310
Cdd:cd18782 84 HLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 311 PRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQVLI 390
Cdd:cd18782 163 PILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLV 242
|
250 260
....*....|....*....|.
gi 37572301 391 LNCGVQQILAGEVTRGGLLSF 411
Cdd:cd18782 243 LWVGAYLVLRGELTLGQLIAF 263
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
485-683 |
1.80e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.97 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQ--PTG---GQLLLDGEPL--TEYDHHYLHRQVVLVGQEPVLFSG 557
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 SVKDNIAYGLRdcedaqvmaaaqaacADDFIGEMTNGINT---------EIGEK----GGQLAVGQKQRLAIARALVRNP 624
Cdd:PRK14243 106 SIYDNIAYGAR---------------INGYKGDMDELVERslrqaalwdEVKDKlkqsGLSLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 625 RVLILDEATSALDA----QCEQALQNWRSQgdRTMLVIAHRLhtvQNADQVLVL-------------KQGRLVEHD 683
Cdd:PRK14243 171 EVILMDEPCSALDPistlRIEELMHELKEQ--YTIIIVTHNM---QQAARVSDMtaffnveltegggRYGYLVEFD 241
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
467-638 |
2.05e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 69.99 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPR-RPEKPVLQGLTFTLHPGTVTALVGPNGSGKST----VAALLQNLYQpTGGQLLLDGEP--------- 532
Cdd:cd03234 4 LPWWDVGLKAKNwNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPrkpdqfqkc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 533 -------------LTEYDHhyLHRQVVLVGqePVLFSGSVKDNIA--YGLRDCEdaqvmaaaqaacaddfigemtngiNT 597
Cdd:cd03234 83 vayvrqddillpgLTVRET--LTYTAILRL--PRKSSDAIRKKRVedVLLRDLA------------------------LT 134
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 37572301 598 EIG-EKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDA 638
Cdd:cd03234 135 RIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
485-689 |
2.36e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.90 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYqPTG---GQLLLDGEPL-------TEydhhylHRQVVLVGQE--- 551
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVCrfkdirdSE------ALGIVIIHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 552 -PVLfsgSVKDNIayglrdcedaqvmaaaqaacaddFIGemtnginTEIGEKG--------------------------- 603
Cdd:NF040905 90 iPYL---SIAENI-----------------------FLG-------NERAKRGvidwnetnrrarellakvgldespdtl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 604 -GQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQN----WRSQGdRTMLVIAHRLHTV-QNADQVLVLKQG 677
Cdd:NF040905 137 vTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDllleLKAQG-ITSIIISHKLNEIrRVADSITVLRDG 215
|
250
....*....|..
gi 37572301 678 RLVEHDQLRDGQ 689
Cdd:NF040905 216 RTIETLDCRADE 227
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
209-361 |
3.10e-13 |
|
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: 71.02 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 209 RGGSFLFTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVS 288
Cdd:cd18605 62 RAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQL 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 289 PrltFLSLLDLPLTIAAEKVYNP-RHQA-VLKEIqDAVAKaGQV---VREAVGGLQTVRSFGAEEQEVSRYKEALERC 361
Cdd:cd18605 142 P---WLLLLLLPLAFIYYRIQRYyRATSrELKRL-NSVNL-SPLythFSETLKGLVTIRAFRKQERFLKEYLEKLENN 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
467-682 |
3.24e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.11 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:COG4604 2 IEIKNVSKRYG---GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNIAYG----------------------------LRDCedaqvmaaaqaacaddFIGEmtngint 597
Cdd:COG4604 79 ILRQENHINSRlTVRELVAFGrfpyskgrltaedreiideaiayldledLADR----------------YLDE------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 598 eigekggqLAVGQKQRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLhtvqN-----A 668
Cdd:COG4604 136 --------LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGKTVVIVLHDI----NfascyA 203
|
250
....*....|....
gi 37572301 669 DQVLVLKQGRLVEH 682
Cdd:COG4604 204 DHIVAMKDGRVVAQ 217
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
467-680 |
3.56e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 70.50 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPE---KPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHR 543
Cdd:PRK13633 5 IKCKNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVV-LVGQEP--VLFSGSVKDNIAYGLRDcedaqvmaaaqaacaddfIGEMTNGINTEIGE---KGGQ----------LA 607
Cdd:PRK13633 85 NKAgMVFQNPdnQIVATIVEEDVAFGPEN------------------LGIPPEEIRERVDEslkKVGMyeyrrhaphlLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 608 VGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNWRSQGDR----TMLVIAHRLHTVQNADQVLVLKQGRLV 680
Cdd:PRK13633 147 GGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkygiTIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
467-693 |
4.06e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSyprRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:PRK09536 4 IDVSDLSVE---FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVL-FSGSVKDNIAYGlRDCEDAQVMAAaqaacaddfiGEMTNGINTEIGEKGG----------QLAVGQKQRLA 615
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMG-RTPHRSRFDTW----------TETDRAAVERAMERTGvaqfadrpvtSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 616 IARALVRNPRVLILDEATSALDAQCE-QALQNWRSQGD--RTMLVIAHRLH-TVQNADQVLVLKQGRL---------VEH 682
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDdgKTAVAAIHDLDlAARYCDELVLLADGRVraagppadvLTA 229
|
250
....*....|.
gi 37572301 683 DQLRDGQDVYA 693
Cdd:PRK09536 230 DTLRAAFDART 240
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
216-426 |
5.39e-13 |
|
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: 70.14 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 216 TMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSD---------TSLMSRWLPFNAnillrsLVKVVGLYFFMlq 286
Cdd:cd18554 73 IANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDveqtkdfitTGLMNIWLDMIT------IIIAICIMLVL-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 287 vSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEvsryKEALERCRQLWW 366
Cdd:cd18554 145 -NPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHE----QKQFDKRNGHFL 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 367 RRDL-----EKDVYLVIRRVMALGmQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLV 426
Cdd:cd18554 220 TRALkhtrwNAKTFSAVNTITDLA-PLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLV 283
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
191-359 |
6.59e-13 |
|
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: 70.00 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 191 AIFFMCLfSVGSSFSAGCRGGSFLFTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANIL 270
Cdd:cd18558 62 AYYYLII-GAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 271 LRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQE 350
Cdd:cd18558 141 FQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKE 220
|
....*....
gi 37572301 351 VSRYKEALE 359
Cdd:cd18558 221 ETRYAQNLE 229
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
467-638 |
6.65e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 70.64 E-value: 6.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRpeKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHylHRQVV 546
Cdd:PRK11650 4 LKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA--DRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQEPVLFSG-SVKDNIAYGLRdcedaqvmaaaqaacaddfIGEMTNG-INT---------EIGE----KGGQLAVGQK 611
Cdd:PRK11650 80 MVFQNYALYPHmSVRENMAYGLK-------------------IRGMPKAeIEErvaeaarilELEPlldrKPRELSGGQR 140
|
170 180
....*....|....*....|....*..
gi 37572301 612 QRLAIARALVRNPRVLILDEATSALDA 638
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
479-639 |
7.71e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 479 RPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYlHRQVVLVGQEPvlfsgS 558
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHQP-----G 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 559 VKD--------NIAYGLRDCEDAqvmaaaqaacaddfigEMTNGINTEIGEKG------GQLAVGQKQRLAIARALVRNP 624
Cdd:PRK13538 85 IKTeltalenlRFYQRLHGPGDD----------------EALWEALAQVGLAGfedvpvRQLSAGQQRRVALARLWLTRA 148
|
170
....*....|....*
gi 37572301 625 RVLILDEATSALDAQ 639
Cdd:PRK13538 149 PLWILDEPFTAIDKQ 163
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
494-678 |
1.40e-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: 65.86 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 494 PGTVTALVGPNGSGKSTVA-ALLQNLYQPTGGQLLLDGEPLTEYDHHYLHrqvvlvgqepvlfsgsvkdniayglrdced 572
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLArALARELGPPGGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 573 aqvmaaaqaacaddfigemtngiNTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQ------- 645
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 37572301 646 --NWRSQGDRTMLVIAHRLHTVQNA------DQVLVLKQGR 678
Cdd:smart00382 108 llLLKSEKNLTVILTTNDEKDLGPAllrrrfDRRIVLLLIL 148
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
151-445 |
1.44e-12 |
|
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: 68.68 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVWGETLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIREQLFS 230
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 231 SLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYn 310
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYY- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 311 prhQAVLKEIQ--DAVAKAG--QVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWrrdlekdVYLVIRRVMALGM 386
Cdd:cd18580 160 ---LRTSRQLRrlESESRSPlySHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFY-------LLLAVQRWLGLRL 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 387 QVL--ILNCGV--------QQILAGEVtrgGL-LSFLLyqeEVGQYVRNLVYMYGDMLSNVGAAEKVFSY 445
Cdd:cd18580 230 DLLgaLLALVVallavllrSSISAGLV---GLaLTYAL---SLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
482-679 |
2.29e-12 |
|
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: 65.92 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 482 KPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQ-VVLVgqePvlfsgsvK 560
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYV---P-------E 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 561 DNIAYGLrdcedaqvmaaaqaacaddfIGEMTNGINTEIGEkggQLAVGQKQRLAIARALVRNPRVLILDEATSALD--- 637
Cdd:cd03215 83 DRKREGL--------------------VLDLSVAENIALSS---LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDvga 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 37572301 638 -AQCEQALQNWRSQGdRTMLVIAHRLHTV-QNADQVLVLKQGRL 679
Cdd:cd03215 140 kAEIYRLIRELADAG-KAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
481-680 |
2.92e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.70 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVLFSG-SV 559
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 560 KDNIAYGlRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQ 639
Cdd:PRK10253 99 QELVARG-RYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 37572301 640 CEQALQNWRSQGDR----TMLVIAHRLH-TVQNADQVLVLKQGRLV 680
Cdd:PRK10253 178 HQIDLLELLSELNRekgyTLAAVLHDLNqACRYASHLIALREGKIV 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
467-676 |
4.55e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRRPekpVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 L---VGQEPVLFSGSVKDNIAYGLRDCEDAQVmaaaqaacaddfigemtnginteIGEKGGQLAVGQKQRLAIARALVRN 623
Cdd:PRK09544 82 LpltVNRFLRLRPGTKKEDILPALKRVQAGHL-----------------------IDAPMQKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 624 PRVLILDEATSALDAQCEQAL----QNWRSQGDRTMLVIAHRLHTVQ-NADQVLVLKQ 676
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHDLHLVMaKTDEVLCLNH 196
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
478-681 |
4.68e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.92 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 478 RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGE----------PLTEYDHHYLH---RQ 544
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgQLKVADKNQLRllrTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 545 VVLVGQEPVLFSG-SVKDNI------AYGLRDCEDAQVMAAAQAACaddfigemtnGINTEI-GEKGGQLAVGQKQRLAI 616
Cdd:PRK10619 94 LTMVFQHFNLWSHmTVLENVmeapiqVLGLSKQEARERAVKYLAKV----------GIDERAqGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 617 ARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRLVE 681
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDpelvGEVLRIMQQLAEEG-KTMVVVTHEMGFARHvSSHVIFLHQGKIEE 232
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
483-678 |
5.39e-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: 65.92 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 483 PVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLL--DGEPL-----TEYDHHYLHRQVV-LVGQ---- 550
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlaqaSPREILALRRRTIgYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 551 -----------EPVLFSGsVKDNIAYGLrdcedaqvmaaaqaacaddfIGEMTNGINteIGEKGGQLAV-----GQKQRL 614
Cdd:COG4778 105 iprvsaldvvaEPLLERG-VDREEARAR--------------------ARELLARLN--LPERLWDLPPatfsgGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 615 AIARALVRNPRVLILDEATSALDAQCEQA----LQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGR 678
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVvvelIEEAKARG-TAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
481-637 |
8.08e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 66.26 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQEPVL---FSG 557
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 SVKDN--IAY------GLRdcedaqvmAAAQAACADDF---IGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRV 626
Cdd:COG1101 98 TIEENlaLAYrrgkrrGLR--------RGLTKKRRELFrelLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKL 169
|
170
....*....|.
gi 37572301 627 LILDEATSALD 637
Cdd:COG1101 170 LLLDEHTAALD 180
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
483-677 |
1.94e-11 |
|
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: 67.63 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 483 PVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGeplteydhhylhrQVVLVGQEPVLFSGSVKDN 562
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 563 IAYGLRDCEDAQVMAAAQAACADDfIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQ 642
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQLEED-IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190
....*....|....*....|....*....|....*...
gi 37572301 643 ALQN---WRSQGDRTMLVIAHRLHTVQNADQVLVLKQG 677
Cdd:TIGR01271 586 EIFEsclCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
481-681 |
1.98e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.81 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALL--QNLYQPTGGQLLLDGEPLTEYD-HHYLHRQVVLVGQEPVLFSG 557
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 -SVKDNIAYGLRDCEDAQVMAAAQAACADDFIGE-----------MTNGINteIGEKGgqlavGQKQRLAIARALVRNPR 625
Cdd:PRK09580 93 vSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEkiallkmpedlLTRSVN--VGFSG-----GEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37572301 626 VLILDEATSALD-------AQCEQALQNwrsqGDRTMLVIAH--RLHTVQNADQVLVLKQGRLVE 681
Cdd:PRK09580 166 LCILDESDSGLDidalkivADGVNSLRD----GKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
151-411 |
2.49e-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: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVwgetLIPRYSGRVID--ILGGDFDP-DAFASAIFFMCLFSVGSSFSagcRGGSFLFTMSRINLRIREQ 227
Cdd:cd18555 8 LLLSLLLQLLTL----LIPILTQYVIDnvIVPGNLNLlNVLGIGILILFLLYGLFSFL---RGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 228 LFSSLLRQDLGFFQETKTGELNSRLSSDTSLmsrwlpfnANILLRSLVK-------VVGLYFFMLQVSPRLTFLSLLdLP 300
Cdd:cd18555 81 FFEHLLKLPYSFFENRSSGDLLFRANSNVYI--------RQILSNQVISliidlllLVIYLIYMLYYSPLLTLIVLL-LG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 301 LTIAAEKVYNPR--HQAVLKEIQdAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDLEKDVYLVI 378
Cdd:cd18555 152 LLIVLLLLLTRKkiKKLNQEEIV-AQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSI 230
|
250 260 270
....*....|....*....|....*....|...
gi 37572301 379 RRVMALGMQVLILNCGVQQILAGEVTRGGLLSF 411
Cdd:cd18555 231 SSSIQFIAPLLILWIGAYLVINGELTLGELIAF 263
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
484-682 |
2.82e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 65.26 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLL---------DGEPLTEY-------DHHYLHRQVVL 547
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELITNpyskkikNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 548 VGQEP--VLFSGSVKDNIAYGlrdcEDAQVMAAAQAACADDFIGEMTnGINTEIGEKGG-QLAVGQKQRLAIARALVRNP 624
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFG----PVALGVKKSEAKKLAKFYLNKM-GLDDSYLERSPfGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37572301 625 RVLILDEATSALDAQCE----QALQNWRSQGdRTMLVIAHRL-HTVQNADQVLVLKQGRLVEH 682
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEhemmQLILDAKANN-KTVFVITHTMeHVLEVADEVIVMDKGKILKT 257
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
465-681 |
3.39e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.64 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 465 GRVEFQDVSFSYPRRP--EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG-------EPLTE 535
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 536 YDHhyLHRQVVLVGQEP--VLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGqlavGQKQR 613
Cdd:PRK13645 85 VKR--LRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSG----GQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37572301 614 LAIARALVRNPRVLILDEATSALDAQCEQALQNW-----RSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVE 681
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLferlnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
480-700 |
5.19e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.57 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 480 PEKPVLQGLTFTLHPGTVTALVGPNGSGKS-TVAALLQNL---YQPTGGQLLLDGEPLTEYDHHylHRQVVLVGQEPVLF 555
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALR--GRKIATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 556 SGSVKDNIAYGLRDCEDAQVMAAAQAAC--------------ADDFIGEMTnginteigekGGQLavgqkQRLAIARALV 621
Cdd:PRK10418 92 FNPLHTMHTHARETCLALGKPADDATLTaaleavglenaarvLKLYPFEMS----------GGML-----QRMMIALALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 622 RNPRVLILDEATSALDAqCEQA-----LQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEHDQLRDGQDVYAHL 695
Cdd:PRK10418 157 CEAPFIIADEPTTDLDV-VAQArildlLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
....*
gi 37572301 696 VQQRL 700
Cdd:PRK10418 236 VTRSL 240
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
472-677 |
6.24e-11 |
|
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: 63.72 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 472 VSFSYPRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGeplteydhhylhrQVVLVGQE 551
Cdd:cd03291 40 LFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 552 PVLFSGSVKDNIAYGLRDCEDAQVMAAAQAACADDfIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDE 631
Cdd:cd03291 107 SWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEED-ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 37572301 632 ATSALDAQCEQALQN---WRSQGDRTMLVIAHRLHTVQNADQVLVLKQG 677
Cdd:cd03291 186 PFGYLDVFTEKEIFEscvCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
467-683 |
9.88e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.59 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPRrpeKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV 546
Cdd:PRK11614 6 LSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQE--PVLFSGSVKDNIAYGlrdcedAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVRNP 624
Cdd:PRK11614 83 AIVPEgrRVFSRMTVEENLAMG------GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37572301 625 RVLILDEATSALDA----QCEQALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVEHD 683
Cdd:PRK11614 157 RLLLLDEPSLGLAPiiiqQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLED 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
485-680 |
1.05e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.46 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYqPTG---GQLLLDGEPLTEYDHHYLHRQ-VVLVGQEPVLFSG-SV 559
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 560 KDNIAYGlrdCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKG---GQLAVGQKQRLAIARALVRNPRVLILDEATSAL 636
Cdd:TIGR02633 96 AENIFLG---NEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTrpvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 37572301 637 DAQCEQALQNW---RSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:TIGR02633 173 TEKETEILLDIirdLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
485-687 |
1.56e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLT-EYDHHYLHRQVVLVGQE-PVLFSGSVKDN 562
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 563 IAYGLRDCEDAQVMAAAQAACADDFIGEMtnGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSAL-DAQCE 641
Cdd:PRK10982 94 MWLGRYPTKGMFVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtEKEVN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 37572301 642 QALQNWRSQGDR--TMLVIAHRLHTV-QNADQVLVLKQGRLVEHDQLRD 687
Cdd:PRK10982 172 HLFTIIRKLKERgcGIVYISHKMEEIfQLCDEITILRDGQWIATQPLAG 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
478-661 |
1.67e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 478 RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLY--QPTGGQLLLDGEPLTeydhhylhRQVVLVgqEPVLF 555
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG--------REASLI--DAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 556 SGSVKDNIAYgLRDCedaqvmaaaqaacaddfigemtnGINTEIG--EKGGQLAVGQKQRLAIARALVRNPRVLILDEAT 633
Cdd:COG2401 109 KGDFKDAVEL-LNAV-----------------------GLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|...
gi 37572301 634 SALDAQCEQAL-----QNWRSQGdRTMLVIAHR 661
Cdd:COG2401 165 SHLDRQTAKRVarnlqKLARRAG-ITLVVATHH 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
485-681 |
1.82e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.11 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGE---PLTEYDHHYLHRQVVLVGQEPVLF---SGS 558
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYASldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 559 VKDNIAYGLRdcedaqvmaaaqaaCADDFIGEMTNGINTEIGEKGG-----------QLAVGQKQRLAIARALVRNPRVL 627
Cdd:PRK10261 420 VGDSIMEPLR--------------VHGLLPGKAAAARVAWLLERVGllpehawryphEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 628 ILDEATSALDAQCEQALQNWRSQGDRTM----LVIAHRLHTVQN-ADQVLVLKQGRLVE 681
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFgiayLFISHDMAVVERiSHRVAVMYLGQIVE 544
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
484-681 |
2.03e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.78 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQ-----PTGGQLLLDGEPL--TEYDHHYLHRQVVLVGQEPVLFS 556
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 557 G-SVKDNIAYGLR-----DCEDAQVMAAAQAACADDFIGEMTNGINteigEKGGQLAVGQKQRLAIARALVRNPRVLILD 630
Cdd:PRK14267 99 HlTIYDNVAIGVKlnglvKSKKELDERVEWALKKAALWDEVKDRLN----DYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 631 EATSALD----AQCEQALqnWRSQGDRTMLVIAHR-LHTVQNADQVLVLKQGRLVE 681
Cdd:PRK14267 175 EPTANIDpvgtAKIEELL--FELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIE 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
501-679 |
2.06e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.12 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 501 VGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHylHRQVVLVGQEPVLFSG-SVKDNIAYGLRdcedaqvmaaa 579
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMVFQSYALYPHlSVAENMSFGLK----------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 580 qaacaddfigeMTNGINTEIGEKGGQ-----------------LAVGQKQRLAIARALVRNPRVLILDEATSALDA---- 638
Cdd:PRK11000 102 -----------LAGAKKEEINQRVNQvaevlqlahlldrkpkaLSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrv 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 37572301 639 QCEQALQNWRSQGDRTMLVIAH-RLHTVQNADQVLVLKQGRL 679
Cdd:PRK11000 171 QMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRV 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
484-682 |
2.14e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.57 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG------EPLTEYDHHYLHRQVVLVGQE----PV 553
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 554 LfsgSVKDNI------AYGLRDCEDAQVMAAAQAACaddfigemtngintEIGEKGG----QLAVGQKQRLAIARALVRN 623
Cdd:PRK11124 97 L---TVQQNLieapcrVLGLSKDQALARAEKLLERL--------------RLKPYADrfplHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37572301 624 PRVLILDEATSALD----AQCEQALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEH 682
Cdd:PRK11124 160 PQVLLFDEPTAALDpeitAQIVSIIRELAETG-ITQVIVTHEVEVARKtASRVVYMENGHIVEQ 222
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
465-686 |
2.69e-10 |
|
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: 61.79 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 465 GRVEFQDVSFSYpRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTV-AALLQNLYqpTGGQLLLDGEPLTEYDHHYLHR 543
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDGVSWNSVPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVVLVGQEPVLFSGSVKDNI-AYGLRDCEdaQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARALVR 622
Cdd:cd03289 78 AFGVIPQKVFIFSGTFRKNLdPYGKWSDE--EIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 623 NPRVLILDEATSALDAQCEQALQNWRSQ--GDRTMLVIAHRLHTVQNADQVLVLKQGRLVEHDQLR 686
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQafADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQ 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
482-679 |
2.70e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.26 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 482 KPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLtEYDHHYLHRQVVLVGQEPVLFSG-SVK 560
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 561 DNIAYGLRdcedAQVMAAAQAACADDFIGEMTnGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQC 640
Cdd:TIGR01257 1022 EHILFYAQ----LKGRSWEEAQLEMEAMLEDT-GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 37572301 641 EQA----LQNWRSqgDRTMLVIAHRLHTVQN-ADQVLVLKQGRL 679
Cdd:TIGR01257 1097 RRSiwdlLLKYRS--GRTIIMSTHHMDEADLlGDRIAIISQGRL 1138
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
479-681 |
3.89e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.95 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 479 RPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGE----------PLTEYDHHYLHR----Q 544
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHvrgaD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 545 VVLVGQEPV-----LFSgsVKDNIAYGLRDCEDAQVMAAAQAACADDFIGEMTNGiNTEIGEKGGQLAVGQKQRLAIARA 619
Cdd:PRK10261 106 MAMIFQEPMtslnpVFT--VGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 620 LVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVE 681
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
484-682 |
3.92e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.68 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYD-HHYLHRQVVLVGQEPVLFSG-SVKD 561
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 562 NIAYGL---RDCEDAQVMAAAQAACADDFIGEMTNGInteigekGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDA 638
Cdd:PRK10895 98 NLMAVLqirDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 37572301 639 ----QCEQALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRLVEH 682
Cdd:PRK10895 171 isviDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAH 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
467-631 |
9.47e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 60.16 E-value: 9.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSyprRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLH---R 543
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYtvrK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVVLVGQEPVLFSG-SVKDNIAYGLRDCEDAQVMaaaqaacaddfIGEMTNGINTE-IGEKGG------QLAVGQKQRLA 615
Cdd:PRK11831 85 RMSMLFQSGALFTDmNVFDNVAYPLREHTQLPAP-----------LLHSTVMMKLEaVGLRGAaklmpsELSGGMARRAA 153
|
170
....*....|....*.
gi 37572301 616 IARALVRNPRVLILDE 631
Cdd:PRK11831 154 LARAIALEPDLIMFDE 169
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
485-695 |
1.42e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.17 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLL---DGEP-----LTEYDHHYLHRQVVlvgqepvlfs 556
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLrdlyaLSEAERRRLLRTEW---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 557 GSVKDNIAYGLRdcedaqvmaaaQAACADDFIGE--MTNGINT--EIGEKGGQ------------------LAVGQKQRL 614
Cdd:PRK11701 92 GFVHQHPRDGLR-----------MQVSAGGNIGErlMAVGARHygDIRATAGDwlerveidaariddlpttFSGGMQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 615 AIARALVRNPRVLILDEATSALDAQCeQA-----LQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEH---DQ- 684
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSV-QArlldlLRGLVRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESgltDQv 239
|
250
....*....|.
gi 37572301 685 LRDGQDVYAHL 695
Cdd:PRK11701 240 LDDPQHPYTQL 250
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
451-665 |
1.46e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.51 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 451 NLPQPGI----LAPPWLEGRVEFQDVSFSYPRrpekpvlqgltftlhpGTVTALVGPNGSGKSTVAALLQNLYQPTGGQL 526
Cdd:PRK15056 1 MMQQAGIvvndVTVTWRNGHTALRDASFTVPG----------------GSIAALVGVNGSGKSTLFKALMGFVRLASGKI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 527 LLDGEPLTEYDHHYLhrqVVLVGQE-------PVLfsgsVKDNIAYG-------LRDCEDAQVMAAAQAACADdfigEMT 592
Cdd:PRK15056 65 SILGQPTRQALQKNL---VAYVPQSeevdwsfPVL----VEDVVMMGryghmgwLRRAKKRDRQIVTAALARV----DMV 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 593 NGINTEIGEKGGqlavGQKQRLAIARALVRNPRVLILDEATSALDAQCE----QALQNWRSQGdRTMLVIAHRLHTV 665
Cdd:PRK15056 134 EFRHRQIGELSG----GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEariiSLLRELRDEG-KTMLVSTHNLGSV 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
487-681 |
2.04e-09 |
|
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: 60.59 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 487 GLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQL-LLDGEP---LTEYDHHYLHRQVVLVG---QEPVLFS-GS 558
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEwvdMTKPGPDGRGRAKRYIGilhQEYDLYPhRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 559 VKDNI--AYGLRDCEDAQVMAAAQAACADDFIGEMTNgintEIGEK-GGQLAVGQKQRLAIARALVRNPRVLILDEATSA 635
Cdd:TIGR03269 382 VLDNLteAIGLELPDELARMKAVITLKMVGFDEEKAE----EILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 37572301 636 LD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVE 681
Cdd:TIGR03269 458 MDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVK 508
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
481-692 |
2.22e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGEP----------LTEYDHHYLHRQV-- 545
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnfTGTILANNRKPtkqilkrtgfVTQDDILYPHLTVre 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 546 ------------VLVGQEPVLFSGSVKDNIayGLRDCEdaqvmaaaqaacaddfigemtngiNTEIGE---KGgqLAVGQ 610
Cdd:PLN03211 160 tlvfcsllrlpkSLTKQEKILVAESVISEL--GLTKCE------------------------NTIIGNsfiRG--ISGGE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 611 KQRLAIARALVRNPRVLILDEATSALDAQCEQALQnwrsqgdRTMLVIAHRLHTV------------QNADQVLVLKQGR 678
Cdd:PLN03211 212 RKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV-------LTLGSLAQKGKTIvtsmhqpssrvyQMFDSVLVLSEGR 284
|
250
....*....|....
gi 37572301 679 LVEHDQLRDGQDVY 692
Cdd:PLN03211 285 CLFFGKGSDAMAYF 298
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
479-687 |
2.24e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.07 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 479 RPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTV----AALLQNLYQPTG----GQLLLDGEPLTEYDHHYLHR-QVVLVG 549
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLlkalAGDLTGGGAPRGarvtGDVTLNGEPLAAIDAPRLARlRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 550 QEPVLFSGSVKDNIAYGlRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIARAL--------- 620
Cdd:PRK13547 91 AAQPAFAFSAREIVLLG-RYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37572301 621 VRNPRVLILDEATSALD-AQCEQALQNWRS---QGDRTMLVIAHRLH-TVQNADQVLVLKQGRLVEHDQLRD 687
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDlAHQHRLLDTVRRlarDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPAD 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
468-693 |
2.39e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFSYPRRPEKPV-LQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQNLYQP------TGGQLLLDGEPLTEYdhhy 540
Cdd:TIGR00956 761 HWRNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERvttgviTGGDRLVNGRPLDSS---- 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 541 LHRQVVLVGQEPV-LFSGSVKDNIAYG--LRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGQLAVGQKQRLAIA 617
Cdd:TIGR00956 834 FQRSIGYVQQQDLhLPTSTVRESLRFSayLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIG 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 618 RALVRNPRVLI-LDEATSALDAQCE----QALQNWRSQGdRTMLVIAHRLHTV--QNADQVLVLKQGrlvehdqlrdGQD 690
Cdd:TIGR00956 914 VELVAKPKLLLfLDEPTSGLDSQTAwsicKLMRKLADHG-QAILCTIHQPSAIlfEEFDRLLLLQKG----------GQT 982
|
...
gi 37572301 691 VYA 693
Cdd:TIGR00956 983 VYF 985
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
488-687 |
3.38e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.97 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 488 LTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGEPLTEYDHHYLHR----QVVLVGQEP-------- 552
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKlraeQISMIFQDPmtslnpym 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 553 --------VL-----------FSGSVK--DNIAyglrdcedaqvmaaaqaacaddfIGEMTNGINTEIGEKGGqlavGQK 611
Cdd:PRK09473 115 rvgeqlmeVLmlhkgmskaeaFEESVRmlDAVK-----------------------MPEARKRMKMYPHEFSG----GMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 612 QRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEHDQLR 686
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNAR 247
|
.
gi 37572301 687 D 687
Cdd:PRK09473 248 D 248
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
485-689 |
3.84e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLT--------EYDHHYLHRQVVLVGQEpvlfs 556
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqEAGIGIIHQELNLIPQL----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 557 gSVKDNIayglrdcedaqvmaaaqaacaddFIG-EMTN---------------------GINTEIGEKGGQLAVGQKQRL 614
Cdd:PRK10762 95 -TIAENI-----------------------FLGrEFVNrfgridwkkmyaeadkllarlNLRFSSDKLVGELSIGEQQMV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 615 AIARALVRNPRVLILDEATSAL-DAQCEQ---ALQNWRSQGdRTMLVIAHRLHTV-QNADQVLVlkqgrlvehdqLRDGQ 689
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALtDTETESlfrVIRELKSQG-RGIVYISHRLKEIfEICDDVTV-----------FRDGQ 218
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
186-411 |
5.65e-09 |
|
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: 57.89 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 186 DAFASAIFFMCLFSVGSSfsaGCRGGSFLFTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSrwlpF 265
Cdd:cd18588 42 DVLAIGLLVVALFEAVLS---GLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARVRELESIRQ----F 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 266 NANILLRSLVKVVGLYFF---MLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVR 342
Cdd:cd18588 115 LTGSALTLVLDLVFSVVFlavMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVK 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 343 SFGAEEQEVSRYKEALerCRQLwwrrdlekDVYLVIRRVMALGMQ----------VLILNCGVQQILAGEVTRGGLLSF 411
Cdd:cd18588 195 SLAVEPQFQRRWEELL--ARYV--------KASFKTANLSNLASQivqliqklttLAILWFGAYLVMDGELTIGQLIAF 263
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
150-442 |
6.44e-09 |
|
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: 57.87 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 150 FLIAAFFFLVVAVwGETLIPRYSGRVID--ILGGDFDpdAFASAIFFMCLFSVGSSFSagcrggSFLFTM------SRIN 221
Cdd:cd18540 4 LILLIILMLLVAL-LDAVFPLLTKYAIDhfITPGTLD--GLTGFILLYLGLILIQALS------VFLFIRlagkieMGVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 222 LRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPL 301
Cdd:cd18540 75 YDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 302 tIAAEKVYnprhqavlkeIQDAVAKAGQVVR-----------EAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRRDL 370
Cdd:cd18540 155 -LAVVSIY----------FQKKILKAYRKVRkinsritgafnEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAAR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37572301 371 EKDVYLVIrrVMALG--MQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVYMYGDMLSNVGAAEKV 442
Cdd:cd18540 224 LSALFLPI--VLFLGsiATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
481-681 |
1.02e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.57 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 481 EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQN--LYQPTGGQLLLDGEPLTEYD-HHYLHRQVVLVGQEPVLFSG 557
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEpEERAHLGIFLAFQYPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 558 -SVKD--NIAYGLRdcEDAQVMAAAQAACADDFIGEMTNGINTEI---------GEKGgqlavGQKQRLAIARALVRNPR 625
Cdd:CHL00131 99 vSNADflRLAYNSK--RKFQGLPELDPLEFLEIINEKLKLVGMDPsflsrnvneGFSG-----GEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37572301 626 VLILDEATSALDAqceQALQ------NWRSQGDRTMLVIAH--RLHTVQNADQVLVLKQGRLVE 681
Cdd:CHL00131 172 LAILDETDSGLDI---DALKiiaegiNKLMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
433-679 |
1.61e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 433 LSNVGAAEKVFSYLDRKPNLPQPGILAPPWLegrVEFQDVSFSYPRRPekPVLQGLTFTLHPGTVTALVGPNGSGKSTVA 512
Cdd:PLN03073 478 LDRLGHVDAVVNDPDYKFEFPTPDDRPGPPI---ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTIL 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 513 ALLQNLYQPTGGQLLLDGE-PLTEYDHHylHRQVVLVGQEPVLFsgsvkdniaygLRDCedaqvmaaaqaacaddFIGEM 591
Cdd:PLN03073 553 KLISGELQPSSGTVFRSAKvRMAVFSQH--HVDGLDLSSNPLLY-----------MMRC----------------FPGVP 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 592 TNGINTEIGEKG--GQLAV--------GQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNWRSQGDRTMLVIAHR 661
Cdd:PLN03073 604 EQKLRAHLGSFGvtGNLALqpmytlsgGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHD 683
|
250
....*....|....*....
gi 37572301 662 LHTVQNA-DQVLVLKQGRL 679
Cdd:PLN03073 684 EHLISGSvDELWVVSEGKV 702
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
465-680 |
1.83e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.34 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 465 GRvefqDVSFSYPRR---PEKPVL--QGLT---------FTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG 530
Cdd:COG1129 238 GR----ELEDLFPKRaaaPGEVVLevEGLSvggvvrdvsFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 531 EPLTEYD-HHYLHRQVVLV----GQEPVLFSGSVKDNIA---------YGLRDcedaqvmAAAQAACADDFIGEM---TN 593
Cdd:COG1129 314 KPVRIRSpRDAIRAGIAYVpedrKGEGLVLDLSIRENITlasldrlsrGGLLD-------RRRERALAEEYIKRLrikTP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 594 GINTEIGekggQLAVGQKQRLAIARALVRNPRVLILDEATSALD--AQCE--QALQNWRSQGdRTMLVIAHRLHTV-QNA 668
Cdd:COG1129 387 SPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEiyRLIRELAAEG-KAVIVISSELPELlGLS 461
|
250
....*....|..
gi 37572301 669 DQVLVLKQGRLV 680
Cdd:COG1129 462 DRILVMREGRIV 473
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
480-661 |
2.24e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.45 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 480 PEKPVL-QGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYdhhylhrqvvlVGQEPVLFSGS 558
Cdd:TIGR00954 462 PNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFY-----------VPQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 559 VKDNIAY----------GLRDCEDAQVMAAAqaacaddfigEMTNGINTEIGEKGGQ-----LAVGQKQRLAIARALVRN 623
Cdd:TIGR00954 531 LRDQIIYpdssedmkrrGLSDKDLEQILDNV----------QLTHILEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHK 600
|
170 180 190
....*....|....*....|....*....|....*...
gi 37572301 624 PRVLILDEATSALDAQCEQALQNWRSQGDRTMLVIAHR 661
Cdd:TIGR00954 601 PQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHR 638
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
466-689 |
2.64e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.86 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 466 RVEFQDVSFSY-PRRP-EKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQ---LLLDGEPLTEYDHHY 540
Cdd:PRK13651 2 QIKVKNIVKIFnKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 541 ---------------------LHRQVVLVGQ--EPVLFSGSVKDNIAYGLRDcedAQVMAAAQAACADDFIgEMTnGINT 597
Cdd:PRK13651 82 kvleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVS---MGVSKEEAKKRAAKYI-ELV-GLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 598 EIGEKGG-QLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQA----LQNWRSQGdRTMLVIAHRL-HTVQNADQV 671
Cdd:PRK13651 157 SYLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEileiFDNLNKQG-KTIILVTHDLdNVLEWTKRT 235
|
250
....*....|....*...
gi 37572301 672 LVLKQGRLVehdqlRDGQ 689
Cdd:PRK13651 236 IFFKDGKII-----KDGD 248
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
192-442 |
3.25e-08 |
|
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: 55.64 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 192 IFFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSD---TSLMSRwlpfNA- 267
Cdd:cd18568 45 LIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQENqkiRRFLTR----SAl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 268 NILLRSLVKVVGLyFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAE 347
Cdd:cd18568 121 TTILDLLMVFIYL-GLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 348 EQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLVY 427
Cdd:cd18568 200 RPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVG 279
|
250
....*....|....*
gi 37572301 428 MYGDMLSNVGAAEKV 442
Cdd:cd18568 280 LWDELQETRISVERL 294
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
497-685 |
4.04e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.65 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 497 VTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLteYDHH---YL---HRQVVLVGQEPVLFSG-SVKDNIAYGLRD 569
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL--FDAEkgiCLppeKRRIGYVFQDARLFPHyKVRGNLRYGMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 570 cedaqvmaaaqaACADDF--IGEMTnGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNW 647
Cdd:PRK11144 104 ------------SMVAQFdkIVALL-GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 37572301 648 RSQGDRT----MLVIAHRLHTV-QNADQVLVLKQGRLVEHDQL 685
Cdd:PRK11144 171 LERLAREinipILYVSHSLDEIlRLADRVVVLEQGKVKAFGPL 213
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
151-426 |
5.43e-08 |
|
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: 54.77 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 151 LIAAFFFLVVAVwgetLIPRYSGRVID--ILGGDFD-PDAFASAIFFMCLFSVGSSFsagCRGGSFLFTMSRINLRIREQ 227
Cdd:cd18567 8 LLLSLALELFAL----ASPLYLQLVIDevIVSGDRDlLTVLAIGFGLLLLLQALLSA---LRSWLVLYLSTSLNLQWTSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 228 LFSSLLRQDLGFFQETKTGELNSRLSSDTSLmsrwlpfnANILLRSLVK-------VVGLYFFMLQVSPRLTFLSLLDLP 300
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRFGSLDEI--------QQTLTTGFVEalldglmAILTLVMMFLYSPKLALIVLAAVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 301 LTIAAEKV-YNPRHQAVLKEIQDAvAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRqlwwRRDLEKDVYLVIR 379
Cdd:cd18567 153 LYALLRLAlYPPLRRATEEQIVAS-AKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAI----NADIRLQRLQILF 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 37572301 380 R-----VMALGmQVLILNCGVQQILAGEVTRGGLLSFLLYQEEVGQYVRNLV 426
Cdd:cd18567 228 SaanglLFGLE-NILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLI 278
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
189-432 |
5.67e-08 |
|
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: 54.83 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 189 ASAIFFMCLFSVGSSFSagcRGGSFLFTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSL---MSRWLpF 265
Cdd:cd18783 45 TIGVVIALLFEGILGYL---RRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQIERIrqfLTGQL-F 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 266 NANILLRSLVKVVGLYFFMlqvSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFg 345
Cdd:cd18783 121 GTLLDATSLLVFLPVLFFY---SPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSL- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 346 aeeqevsrykeALERCRqlwwRRDLEKDVYLVIRRVMALG----------------MQVLILNCGVQQILAGEVTRGGLL 409
Cdd:cd18783 197 -----------ALEPRQ----RREWDERVARAIRARFAVGrlsnwpqtltgpleklMTVGVIWVGAYLVFAGSLTVGALI 261
|
250 260
....*....|....*....|...
gi 37572301 410 SFLLYQEEVGQYVRNLVYMYGDM 432
Cdd:cd18783 262 AFNMLAGRVAGPLVQLAGLVQEY 284
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
477-680 |
7.55e-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: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 477 PRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVVLVGQE----- 551
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVFGQRsqlww 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 552 --PVLFSGSVKDNIaYGLRDCEDAQVmaaaqaacaddfIGEMTNGIntEIGEKGG----QLAVGQKQRLAIARALVRNPR 625
Cdd:COG4586 110 dlPAIDSFRLLKAI-YRIPDAEYKKR------------LDELVELL--DLGELLDtpvrQLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 626 VLILDEATSALDAQCEQALQNW-----RSQGdRTMLVIAHRLHTVQN-ADQVLVLKQGRLV 680
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFlkeynRERG-TTILLTSHDMDDIEAlCDRVIVIDHGRII 234
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
471-669 |
7.78e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 7.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 471 DVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEyDHHYLHRQVVLVGQ 550
Cdd:PRK13540 6 ELDFDYH---DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 551 E----PVLfsgSVKDNIAYGLRDCEDAQVmaaaqaacaddfIGEMTNGINTE--IGEKGGQLAVGQKQRLAIARALVRNP 624
Cdd:PRK13540 82 RsginPYL---TLRENCLYDIHFSPGAVG------------ITELCRLFSLEhlIDYPCGLLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 37572301 625 RVLILDEATSALDAQCEQA----LQNWRSQGDrTMLVIAHRLHTVQNAD 669
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTiitkIQEHRAKGG-AVLLTSHQDLPLNKAD 194
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
484-689 |
8.50e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.63 E-value: 8.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHH----YLHRQVVLVGQEPVLF-SGS 558
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEarakLRAKHVGFVFQSFMLIpTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 559 VKDNIAY-----GLRDCEDAQVMAAAQAACaddfigemtnGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILDEAT 633
Cdd:PRK10584 105 ALENVELpallrGESSRQSRNGAKALLEQL----------GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 634 SALDaqceqalqnwRSQGDRtmlvIAHRLHTVqNADQVLVLKqgrLVEHD-----------QLRDGQ 689
Cdd:PRK10584 175 GNLD----------RQTGDK----IADLLFSL-NREHGTTLI---LVTHDlqlaarcdrrlRLVNGQ 223
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
459-637 |
1.28e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 459 APPWLEGrvefQDVSFSyprRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDH 538
Cdd:PRK13543 8 APPLLAA----HALAFS---RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 539 hylHRQVVLVGQEPVLFSG-SVKDNIAY--GLRDCEDAqvmaaaqaacaddfigEMTNGINTEIGEKG------GQLAVG 609
Cdd:PRK13543 81 ---SRFMAYLGHLPGLKADlSTLENLHFlcGLHGRRAK----------------QMPGSALAIVGLAGyedtlvRQLSAG 141
|
170 180
....*....|....*....|....*...
gi 37572301 610 QKQRLAIARALVRNPRVLILDEATSALD 637
Cdd:PRK13543 142 QKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
482-681 |
2.74e-07 |
|
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: 53.65 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 482 KPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNL--YQPTGGQLL----------------LDGEP-------LTEY 536
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPcpvcggtLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 537 DHHY------------------LHRQVVLVGQEPVLfsgsvkDNIAYGLRDCEDAQVMAAAQAACADdfigEMTNgINTE 598
Cdd:TIGR03269 93 EVDFwnlsdklrrrirkriaimLQRTFALYGDDTVL------DNVLEALEEIGYEGKEAVGRAVDLI----EMVQ-LSHR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 599 IGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQC----EQALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLV 673
Cdd:TIGR03269 162 ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTaklvHNALEEAVKASGISMVLTSHWPEVIEDlSDKAIW 241
|
....*...
gi 37572301 674 LKQGRLVE 681
Cdd:TIGR03269 242 LENGEIKE 249
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
489-662 |
3.83e-07 |
|
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: 51.98 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 489 TFTLH------PGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLllDGEP-----LTEYD----HHYLHR---------- 543
Cdd:cd03236 14 SFKLHrlpvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--DDPPdwdeiLDEFRgselQNYFTKllegdvkviv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 544 QVVLVGQEPVLFSGSVKDNIA----YGLRD--CEDAqvmaaaqaacaddfigEMTNGINTEIGekggQLAVGQKQRLAIA 617
Cdd:cd03236 92 KPQYVDLIPKAVKGKVGELLKkkdeRGKLDelVDQL----------------ELRHVLDRNID----QLSGGELQRVAIA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 37572301 618 RALVRNPRVLILDEATSALDAQceQALQNWR-----SQGDRTMLVIAHRL 662
Cdd:cd03236 152 AALARDADFYFFDEPSSYLDIK--QRLNAARlirelAEDDNYVLVVEHDL 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
494-662 |
3.88e-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: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 494 PGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLllDGEPltEYD-----------HHYLHR------QVVL----VGQEP 552
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEP--SWDevlkrfrgtelQDYFKKlangeiKVAHkpqyVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 553 VLFSGSVKD--------NIAYGLRDcedaqvmaaaqaacaddfIGEMTNGINTEIGE-KGGQLavgqkQRLAIARALVRN 623
Cdd:COG1245 174 KVFKGTVREllekvderGKLDELAE------------------KLGLENILDRDISElSGGEL-----QRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 37572301 624 PRVLILDEATSALD-------AQCEQALqnwrSQGDRTMLVIAHRL 662
Cdd:COG1245 231 ADFYFFDEPSSYLDiyqrlnvARLIREL----AEEGKYVLVVEHDL 272
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
474-673 |
4.42e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 51.64 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 474 FSYPRRpeKPVLQGLTFTLHPGT-----VTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTeYDHHYLHRQvvlv 548
Cdd:cd03237 1 YTYPTM--KKTLGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKAD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 549 gqepvlFSGSVKDNIAYGLRDcedaqvmaaaqAACADDFIGEMTNGINTE--IGEKGGQLAVGQKQRLAIARALVRNPRV 626
Cdd:cd03237 74 ------YEGTVRDLLSSITKD-----------FYTHPYFKTEIAKPLQIEqiLDREVPELSGGELQRVAIAACLSKDADI 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 37572301 627 LILDEATSALDAqcEQ------ALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLV 673
Cdd:cd03237 137 YLLDEPSAYLDV--EQrlmaskVIRRFAENNEKTAFVVEHDIIMIDYlADRLIV 188
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
491-662 |
4.56e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 491 TLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLllDGEPltEYD-----------HHYLHR------QVVL----VG 549
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--EEEP--SWDevlkrfrgtelQNYFKKlyngeiKVVHkpqyVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 550 QEPVLFSGSVKDNIA----YGLRDcEDAQVMaaaqaacaddfigEMTNGINTEIGE-KGGQLavgqkQRLAIARALVRNP 624
Cdd:PRK13409 171 LIPKVFKGKVRELLKkvdeRGKLD-EVVERL-------------GLENILDRDISElSGGEL-----QRVAIAAALLRDA 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 37572301 625 RVLILDEATSALD-------AQCEQALQNwrsqgDRTMLVIAHRL 662
Cdd:PRK13409 232 DFYFFDEPTSYLDirqrlnvARLIRELAE-----GKYVLVVEHDL 271
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
154-408 |
1.07e-06 |
|
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: 50.96 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 154 AFFFLVVAVWGETLIPRYSGRVIDILGGDfDPDAFASAIFFM---CLFSVGSSFSAGCRGGSFLFTMSRINLRIREQLFS 230
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSAP-ASALLAVPLLLLlayGLARILSSLFNELRDALFARVSQRAVRRLALRVFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 231 SLLRQDLGFFQETKTGELNS---RLSSDTSLMSRWLPFNA--NILLRSLVKVVGLYFFmlqvSPRLTFLSLLDLPLTIAA 305
Cdd:cd18582 80 HLHSLSLRFHLSRKTGALSRaieRGTRGIEFLLRFLLFNIlpTILELLLVCGILWYLY----GWSYALITLVTVALYVAF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 306 EKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQLWWRrdlekdvylVIRRVMALG 385
Cdd:cd18582 156 TIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVK---------SQTSLALLN 226
|
250 260 270
....*....|....*....|....*....|..
gi 37572301 386 M-QVLILNCG--------VQQILAGEVTRGGL 408
Cdd:cd18582 227 IgQALIISLGltaimllaAQGVVAGTLTVGDF 258
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
605-681 |
1.68e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 605 QLAVGQKQRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTV-QNADQVLVLKQGRL 679
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqAQIIELLLELQQKENMALVLITHDLALVaEAAHKIIVMYAGQV 232
|
..
gi 37572301 680 VE 681
Cdd:PRK11022 233 VE 234
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
452-660 |
1.71e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 452 LPQP-GILAPPWL---EGRVEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYqPTG---- 523
Cdd:PRK10938 242 LPEPdEPSARHALpanEPRIVLNNGVVSYN---DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQGysnd 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 524 ----GQLLLDGEPLTEYDHH--YLHRQVVL---VgqepvlfSGSVKDNIAYGLRDCedaqvmaaaqaacaddfIG----- 589
Cdd:PRK10938 318 ltlfGRRRGSGETIWDIKKHigYVSSSLHLdyrV-------STSVRNVILSGFFDS-----------------IGiyqav 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 590 -----EMTN------GINTEIGEKGGQ-LAVGQkQRLA-IARALVRNPRVLILDEATSALDAQCEQALQNWR----SQGD 652
Cdd:PRK10938 374 sdrqqKLAQqwldilGIDKRTADAPFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVdvliSEGE 452
|
....*...
gi 37572301 653 RTMLVIAH 660
Cdd:PRK10938 453 TQLLFVSH 460
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
485-687 |
1.86e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.81 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQvvLVGQEPVLFSgsvkdNIA 564
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQ--LTGIENIEFK-----MLC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 565 YGLRDCEdaqvmaaaqaacaddfIGEMTNGI--NTEIGEKGGQ----LAVGQKQRLAIARALVRNPRVLILDEATSALDA 638
Cdd:PRK13546 113 MGFKRKE----------------IKAMTPKIieFSELGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEALSVGDQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 37572301 639 ----QCEQALQNWRSQgDRTMLVIAHRLHTVQN-ADQVLVLKQGRLVEHDQLRD 687
Cdd:PRK13546 177 tfaqKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDD 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
467-646 |
1.97e-06 |
|
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: 51.09 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLdGEPLteydhhylhrQVV 546
Cdd:TIGR03719 323 IEAENLTKAFG---DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 LVGQ--EPVLFSGSVKDNIAYGLrdcedaqvmaaaqaacaddfiGEMTNGiNTEIGE---------KG-------GQLAV 608
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGGL---------------------DIIKLG-KREIPSrayvgrfnfKGsdqqkkvGQLSG 446
|
170 180 190
....*....|....*....|....*....|....*...
gi 37572301 609 GQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQN 646
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEE 484
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
605-681 |
3.55e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.42 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 605 QLAVGQKQRLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGDRTMLVIAHRLHTV-QNADQVLVLKQGRL 679
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEpttqAQIFRLLTRLNQNNNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
..
gi 37572301 680 VE 681
Cdd:PRK15093 238 VE 239
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
470-680 |
9.12e-06 |
|
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: 48.78 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 470 QDVSFSYPrrPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLldgePLTEYDHHYLHrqvvlvg 549
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR----PQPGIKVGYLP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 550 QEPVL-FSGSVKDNIAYGLRDC-------EDAQVMAAAQAACADDFIGEMTNgINTEIGEKGG-----QLAV-------- 608
Cdd:TIGR03719 75 QEPQLdPTKTVRENVEEGVAEIkdaldrfNEISAKYAEPDADFDKLAAEQAE-LQEIIDAADAwdldsQLEIamdalrcp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 609 -----------GQKQRLAIARALVRNPRVLILDEATSALDAQC----EQALQNWrsQGdrTMLVIAHRLHTVQNADQ-VL 672
Cdd:TIGR03719 154 pwdadvtklsgGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQEY--PG--TVVAVTHDRYFLDNVAGwIL 229
|
....*...
gi 37572301 673 VLKQGRLV 680
Cdd:TIGR03719 230 ELDRGRGI 237
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
484-693 |
9.17e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 484 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNlyQPTGG----QLLLDGEP--------LTEY-DHHYLHRQVVLVgQ 550
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyiegDIRISGFPkkqetfarISGYcEQNDIHSPQVTV-R 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 551 EPVLFSgsvkdniAYgLRDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKG-GQLAVGQKQRLAIARALVRNPRVLIL 629
Cdd:PLN03140 972 ESLIYS-------AF-LRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 630 DEATSALDAQCE----QALQNWRSQGdRTMLVIAHR--LHTVQNADQVLVLKQGrlvehdqlrdGQDVYA 693
Cdd:PLN03140 1044 DEPTSGLDARAAaivmRTVRNTVDTG-RTVVCTIHQpsIDIFEAFDELLLMKRG----------GQVIYS 1102
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
473-637 |
9.63e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 473 SFSYprrpeKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLqnlyqpTGGQLLLDGEPLTEYDhhylhrqvVLVG--- 549
Cdd:PRK11147 12 SFSD-----APLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL------NGEVLLDDGRIIYEQD--------LIVArlq 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 550 QEPVL-FSGSVKDNIAYGL--------------RDCEDAQVMAAAQAACADDFIGEMTNG--INTEIGEKGGQLAV---- 608
Cdd:PRK11147 73 QDPPRnVEGTVYDFVAEGIeeqaeylkryhdisHLVETDPSEKNLNELAKLQEQLDHHNLwqLENRINEVLAQLGLdpda 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 37572301 609 -------GQKQRLAIARALVRNPRVLILDEATSALD 637
Cdd:PRK11147 153 alsslsgGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
604-679 |
9.88e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 9.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 604 GQLAVGQKQRLAIARALVRNPRVLILDEATSALD--AQCE--QALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGRL 679
Cdd:PRK10762 394 GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgAKKEiyQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
604-679 |
1.62e-05 |
|
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: 47.90 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 604 GQLAVGQKQRLAIARALVRNPRVLILDEATSALD--AQCE-QALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRL 679
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDvgAKYEiYKLINQLAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
188-356 |
1.66e-05 |
|
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: 47.56 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 188 FASAIFFMCLFSVgssfsagCRGGSFLFTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNA 267
Cdd:cd18599 64 YGGSILVILLLSL-------IRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 268 NILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNpRHQAVLKEIqDAVAKAGQV--VREAVGGLQTVRSFG 345
Cdd:cd18599 137 ENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIFR-RAIRELKRL-ENISRSPLFshLTATIQGLSTIHAFN 214
|
170
....*....|.
gi 37572301 346 AEEQEVSRYKE 356
Cdd:cd18599 215 KEKEFLSKFKK 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
485-679 |
1.77e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 46.93 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 485 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLY---QPTGGQLLLDGEPL------------TEYDHHYLHRQVVLVG 549
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVqregrlardirkSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 550 QEPVLfsgsvkDNIAYGL-------RDCEDAQVMAAAQAACADDFIGEMTNGINTEIGEKGGqlavGQKQRLAIARALVR 622
Cdd:PRK09984 100 RLSVL------ENVLIGAlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSG----GQQQRVAIARALMQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37572301 623 NPRVLILDEATSALDAQCEQ-ALQNWR--SQGDRTMLVIAhrLHTVQNA----DQVLVLKQGRL 679
Cdd:PRK09984 170 QAKVILADEPIASLDPESARiVMDTLRdiNQNDGITVVVT--LHQVDYAlrycERIVALRQGHV 231
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
150-359 |
1.87e-05 |
|
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: 47.22 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 150 FLIAAFFFLVVAvwgetliPRYSGRVIDIL--GGDFDPDAFASAIFFMCLFSVGSSFSAGCRGGSFLFTMSRINLRIREQ 227
Cdd:cd18560 4 LLILGKACNVLA-------PLFLGRAVNALtlAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 228 LFSSLLRQDLGFFQETKTGE----LNSRLSSDTSLMSrWLPFN-ANILLRSLVKVVglyFFMLQVSPRLTFLSLLDLPL- 301
Cdd:cd18560 77 TFAHLHSLSLDWHLSKKTGEvvriMDRGTESANTLLS-YLVFYlVPTLLELIVVSV---VFAFHFGAWLALIVFLSVLLy 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37572301 302 TIAAEKVYNPRhqavlKEIQDAVAKA-GQVVREAVGGL---QTVRSFGAEEQEVSRYKEALE 359
Cdd:cd18560 153 GVFTIKVTEWR-----TKFRRAANKKdNEAHDIAVDSLlnfETVKYFTNEKYEVDRYGEAVK 209
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
191-412 |
2.07e-05 |
|
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: 47.16 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 191 AIFFMCLFSVGSSFsagCRGGSFLFTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTS----LMSRWLpfn 266
Cdd:cd18779 47 GLAALVLTQLLAGL---LRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSSNATirelLTSQTL--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 267 aNILLRSLVkVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGA 346
Cdd:cd18779 121 -SALLDGTL-VLGYLALLFAQSPLLGLVVLGLAALQVALLLATRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGA 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 347 EEQEVSRYKEALERCRQLWWRRDLEKDVYLVIRRVMALGMQVLILNCGVQQILAGEVTRGGLLSFL 412
Cdd:cd18779 199 EDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALN 264
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
167-414 |
2.19e-05 |
|
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: 46.75 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 167 LIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSfsagcrGG-SFLFTMSRINLR--IREQL----FSSLLRQDLGF 239
Cdd:cd18583 14 LVPRQLGIIVDSLSGGSGKSPWKEIGLYVLLRFLQSG------GGlGLLRSWLWIPVEqySYRALstaaFNHVMNLSMDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 240 FQETKTGELNSRLSSDTSLMS--RWLPFN-----ANIllrslvkVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPR 312
Cdd:cd18583 88 HDSKKSGEVLKAIEQGSSINDllEQILFQivpmiIDL-------VIAIVYLYYLFDPYMGLIVAVVMVLYVWSTIKLTSW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 313 HQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSRYKEALERCRQlwwrrdLEKDVYLviRRVMALGMQVLILN 392
Cdd:cd18583 161 RTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQK------AERKYLF--SLNLLNAVQSLILT 232
|
250 260 270
....*....|....*....|....*....|
gi 37572301 393 CG--------VQQILAGEVTRGGLLSFLLY 414
Cdd:cd18583 233 LGllagcflaAYQVSQGQATVGDFVTLLTY 262
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
479-679 |
2.87e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 479 RPEKPVLQ----------GLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDhhylhrqvvlV 548
Cdd:PRK15439 263 AAGAPVLTvedltgegfrNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS----------T 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 549 GQEpvLFSGSV---KDNIAYGLR-DCEDAQVMAAAQAACADDFIGEMTN-----------GIN-TEIGEKGGQLAVGQKQ 612
Cdd:PRK15439 333 AQR--LARGLVylpEDRQSSGLYlDAPLAWNVCALTHNRRGFWIKPAREnavleryrralNIKfNHAEQAARTLSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37572301 613 RLAIARALVRNPRVLILDEATSALD----AQCEQALQNWRSQGdRTMLVIAHRLHTV-QNADQVLVLKQGRL 679
Cdd:PRK15439 411 KVLIAKCLEASPQLLIVDEPTRGVDvsarNDIYQLIRSIAAQN-VAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
443-681 |
3.60e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 443 FSYLDRKP-NLPQPgilappwlegRVEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQP 521
Cdd:PRK10636 298 FHFSFRAPeSLPNP----------LLKMEKVSAGYG---DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 522 TGGQL-LLDGEPLTEYDHHYLHrqvVLVGQEPVL--FSGSVKDNIAYGLRDcedaqvmaaaqAACADDFIGEmtngintE 598
Cdd:PRK10636 365 VSGEIgLAKGIKLGYFAQHQLE---FLRADESPLqhLARLAPQELEQKLRD-----------YLGGFGFQGD-------K 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 599 IGEKGGQLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNWRSQGDRTMLVIAHRLHTVQNADQVLVLKQGR 678
Cdd:PRK10636 424 VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDG 503
|
...
gi 37572301 679 LVE 681
Cdd:PRK10636 504 KVE 506
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
465-684 |
4.45e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.44 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 465 GRvEFQDVsFSYPRRPEKPV---LQGL---------TFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEP 532
Cdd:PRK11288 239 GR-EIGDI-YGYRPRPLGEVrlrLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKP 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 533 LTEYD-HHYLHRQVVLV----GQEPVLFSGSVKDNIAYGLRDCEDAQVMAAAQ---AACADDFIGEM---TNGINTEIge 601
Cdd:PRK11288 317 IDIRSpRDAIRAGIMLCpedrKAEGIIPVHSVADNINISARRHHLRAGCLINNrweAENADRFIRSLnikTPSREQLI-- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 602 kgGQLAVGQKQRLAIARALVRNPRVLILDEATSALD--AQCE--QALQNWRSQGdRTMLVIAHRLHTVQN-ADQVLVLKQ 676
Cdd:PRK11288 395 --MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDvgAKHEiyNVIYELAAQG-VAVLFVSSDLPEVLGvADRIVVMRE 471
|
250
....*....|.
gi 37572301 677 GRL---VEHDQ 684
Cdd:PRK11288 472 GRIageLAREQ 482
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
468-660 |
1.09e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 468 EFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDgeplTEYDHHYL--HRQV 545
Cdd:PRK11147 321 EMENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEVAYFdqHRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 546 VlvgqEPvlfSGSVKDNIAYGLRDCedaqvmaaaqaacaddfigeMTNGINTEI---------GEKGGQLAV-----GQK 611
Cdd:PRK11147 394 L----DP---EKTVMDNLAEGKQEV--------------------MVNGRPRHVlgylqdflfHPKRAMTPVkalsgGER 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 37572301 612 QRLAIARALVRNPRVLILDEATSALDAQC----EQALQNWrsQGdrTMLVIAH 660
Cdd:PRK11147 447 NRLLLARLFLKPSNLLILDEPTNDLDVETlellEELLDSY--QG--TVLLVSH 495
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
605-663 |
1.34e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 1.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 37572301 605 QLAVGQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNWRSQGDRTMLVIAHRLH 663
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRH 213
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
491-675 |
2.56e-04 |
|
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: 41.96 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 491 TLHPGTVTALVGPNGSGKSTVA-ALLqnlyqptggqLLLDGEPLTEYDHHYLHRQVVlVGQEPVLFSGSVKdniayglrd 569
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILdAIG----------LALGGAQSATRRRSGVKAGCI-VAAVSAELIFTRL--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 570 cedaqvmaaaqaacaddfigemtnginteigekggQLAVGQKQRLAIARALV---RNPRVL-ILDEATSALDAQCEQALQ 645
Cdd:cd03227 77 -----------------------------------QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALA 121
|
170 180 190
....*....|....*....|....*....|...
gi 37572301 646 NW---RSQGDRTMLVIAHRLHTVQNADQVLVLK 675
Cdd:cd03227 122 EAileHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
604-679 |
3.39e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 604 GQLAVGQKQRLAIARALVRNPRVLILDEATSALD--AQCE-QALQNWRSQGDRTMLVIAHRLHTVQN-ADQVLVLKQGRL 679
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgAKYEiYKLINQLVQQGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
204-446 |
3.45e-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: 43.36 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 204 FSAGCRGGSFLFTMSRI----NLRIREQLFSSLLRQDL----GFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLV 275
Cdd:cd18559 45 GALAILQGITVFQYSMAvsigGIFASRAVHLDLYHKALrspiSFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 276 KVVGLYFFMLQVSPRLTFLSLLDLpLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEqevsRYK 355
Cdd:cd18559 125 NVIGLYLLILLAGPMAAVGIPLGL-LYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEE----AFI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 356 EALERCrqlwwrRDLEKDVYLVIRRVMALGMQV-LILNCGVQ-QILAGEVTRGGLLSF----LLYQEEVGQYVRNLVYMY 429
Cdd:cd18559 200 RQVDAK------RDNELAYLPSIVYLRALAVRLwCVGPCIVLfASFFAYVSRHSLAGLvalkVFYSLALTTYLNWPLNMS 273
|
250
....*....|....*..
gi 37572301 430 GDMLSNVGAAEKVFSYL 446
Cdd:cd18559 274 PEVITNIVAAEVSLERS 290
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
467-526 |
3.78e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 3.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37572301 467 VEFQDVSFSYPRRpekpVL-QGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQL 526
Cdd:PRK11819 325 IEAENLSKSFGDR----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
196-360 |
5.28e-04 |
|
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: 42.59 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 196 CLFSVGSSFSAGCRGGSFLFTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWLPFNANILLRSLV 275
Cdd:cd18602 57 AGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 276 KVVGLYFFMLQVSPrltFLSLLDLPLTIAA---EKVYnprhQAVLKEIQ--DAVAKaGQVV---REAVGGLQTVRSFGAE 347
Cdd:cd18602 137 LCLSAIIVNAIVTP---YFLIALIPIIIVYyflQKFY----RASSRELQrlDNITK-SPVFshfSETLGGLTTIRAFRQQ 208
|
170
....*....|...
gi 37572301 348 EQEVSRYKEALER 360
Cdd:cd18602 209 ARFTQQMLELIDR 221
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
606-674 |
6.66e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 6.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 606 LAVGQKQRLAIARAL---VRNPRVLILDEATSALDA----QCEQALQNWRSQGdRTMLVIAHRLHTVQNADQVLVL 674
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHThdikALIYVLQSLTHQG-HTVVIIEHNMHVVKVADYVLEL 884
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
497-678 |
7.09e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.44 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 497 VTALVGPNGSGKSTV-AALLQNLYqptgGQLlldgePLTEYDHHYLhRQVVLVGQEpvlfSGSVKdnIAYGLRDCEDAQV 575
Cdd:cd03240 24 LTLIVGQNGAGKTTIiEALKYALT----GEL-----PPNSKGGAHD-PKLIREGEV----RAQVK--LAFENANGKKYTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 576 MAAAQAACADDFI--GEmtngINTEIGEKGGQLAVGQKQ------RLAIARALVRNPRVLILDEATSALDA-QCEQAL-- 644
Cdd:cd03240 88 TRSLAILENVIFChqGE----SNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLae 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 37572301 645 --QNWRSQGDRTMLVIAHRLHTVQNADQVL-VLKQGR 678
Cdd:cd03240 164 iiEERKSQKNFQLIVITHDEELVDAADHIYrVEKDGR 200
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
486-515 |
7.96e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.96 E-value: 7.96e-04
10 20 30
....*....|....*....|....*....|....
gi 37572301 486 QGLTFTLHPGTVTALVGPNGSGKST----VAALL 515
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTlldaIQTLL 46
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
604-637 |
8.36e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 8.36e-04
10 20 30
....*....|....*....|....*....|....
gi 37572301 604 GQLAVGQKQRLAIARALVRNPRVLILDEATSALD 637
Cdd:NF033858 396 DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
190-349 |
9.19e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 41.68 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 190 SAIFFM---CLFSVGSSFSAGCRGGSFLF---TMSRinlRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTSLMSRWL 263
Cdd:cd18604 41 SVLYYLgiyALISLLSVLLGTLRYLLFFFgslRASR---KLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 264 PFNANILLRSLVKVVGLYFFMLQVSPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEiqDAVAKAG--QVVREAVGGLQTV 341
Cdd:cd18604 118 ADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLRASRELKRL--ESVARSPilSHFGETLAGLVTI 195
|
....*...
gi 37572301 342 RSFGAEEQ 349
Cdd:cd18604 196 RAFGAEER 203
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
156-360 |
1.04e-03 |
|
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: 41.85 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 156 FFLVVAVWG-ETLIPRYSGRVIDILGGDFDPDAFASAIFFMCLFSVGSSFSAGCRGGSFLFTMSR----------INLRI 224
Cdd:cd18581 2 LLLLAAGRVvNVLVPILYKKIVDSLTPDSADSPLAFPWALILLYVFLKFLQGGGSGSVGLLSNLRsflwipvqqfTTREI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 225 REQLFSSLLRQDLGFFQETKTGE----LNSRLSSDTSLMSrWLPFnaNILLRSLVKVVGLYFFMLQVSPRL---TFLSL- 296
Cdd:cd18581 82 SVKLFAHLHSLSLRWHLSRKTGEvlrvMDRGTSSINSLLS-YVLF--NIGPTIADIIIAIIYFAIAFNPWFgliVFVTMa 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 297 LDLPLTIAAEKvYNPRHQAVLKEiQDAVAKAgqvvrEAVGGL---QTVRSFGAEEQEVSRYKEALER 360
Cdd:cd18581 159 LYLILTIIITE-WRTKFRREMNK-LDNEKRA-----KAVDSLlnfETVKYYNAERFEVERYRRAIDD 218
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
606-674 |
1.32e-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: 42.31 E-value: 1.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37572301 606 LAVGQKQRLAIARALVR---NPRVLILDEATSALD----AQCEQALQNWRSQGDrTMLVIAHRLHTVQNADQVLVL 674
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHfddiKKLLEVLQRLVDKGN-TVVVIEHNLDVIKTADYIIDL 904
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
490-674 |
1.38e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 490 FTLHPGTVTALVGPNGSGKSTVA-ALLQNLyqptggqLLLDGEPLTEYDH---------------HYLHRQVVLVGQEPV 553
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALArALAGEL-------PLLSGERQSQFSHitrlsfeqlqklvsdEWQRNNTDMLSPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 554 LFSGSVKDNIAYGLRD---CEDAQVMAaaqaacaddfigemtnGINTEIGEKGGQLAVGQKQRLAIARALVRNPRVLILD 630
Cdd:PRK10938 97 DTGRTTAEIIQDEVKDparCEQLAQQF----------------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 37572301 631 EATSALDAQCEQALqnwrsqgdrtmlviAHRLHTVQNADQVLVL 674
Cdd:PRK10938 161 EPFDGLDVASRQQL--------------AELLASLHQSGITLVL 190
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
207-411 |
1.67e-03 |
|
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: 41.03 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 207 GCRGGSFLFTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRL------------SSDTSLMSrwLPFnanillrsl 274
Cdd:cd18566 60 LLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLnsleqirefltgQALLALLD--LPF--------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 275 vkvVGLYFFMLQV-SPRLTFLSLLDLPLTIAAEKVYNPRHQAVLKEIQDAVAKAGQVVREAVGGLQTVRSFGAEEQEVSR 353
Cdd:cd18566 129 ---VLIFLGLIWYlGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRR 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37572301 354 YKEALERCrqlwwrrdlEKDVYLVIRR---VMALG------MQVLILNCGVQQILAGEVTRGGLLSF 411
Cdd:cd18566 206 YERLQANA---------AYAGFKVAKInavAQTLGqlfsqvSMVAVVAFGALLVINGDLTVGALIAC 263
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
467-524 |
1.87e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 1.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 37572301 467 VEFQDVSFSYPrrpEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGG 524
Cdd:PRK15064 320 LEVENLTKGFD---NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
478-530 |
2.09e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 2.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 37572301 478 RRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG 530
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG 62
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
599-674 |
3.77e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.91 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 599 IGEKGGQLAVGQKQRLAIARALVR---NPRVLILDEATSALDAQCEQ----ALQNWRSQGDrTMLVIAHRLHTVQNADQV 671
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKklleVLQRLVDKGN-TVVVIEHNLDVIKCADWI 241
|
...
gi 37572301 672 LVL 674
Cdd:cd03271 242 IDL 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
475-637 |
4.08e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 40.40 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 475 SYPRRPEKPVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGEPLTEYDHHYLHRQVV-------- 546
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVayipedrl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 547 ---LVGqepvlfSGSVKDNIAYGLRDCEDAQVMAAAQAACADDF----IGEM---TNGINTEIgekgGQLAVGQKQRLAI 616
Cdd:COG3845 344 grgLVP------DMSVAENLILGRYRRPPFSRGGFLDRKAIRAFaeelIEEFdvrTPGPDTPA----RSLSGGNQQKVIL 413
|
170 180
....*....|....*....|.
gi 37572301 617 ARALVRNPRVLILDEATSALD 637
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLD 434
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
609-660 |
4.11e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 4.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 37572301 609 GQKQRLAIARALVRNPRVLILDEATSALDAQCEQALQNWRSQGDRTMLVIAH 660
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSH 399
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
495-662 |
4.19e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 38.71 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 495 GTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGeplteydhhylhrqvVLVGQEPVLFSGSvkdniayglrdcedaq 574
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG---------------ITPVYKPQYIDLS---------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37572301 575 vmaaaqaacaddfigemtnginteigekGGQLavgqkQRLAIARALVRNPRVLILDEATSALDAQ----CEQALQNWRSQ 650
Cdd:cd03222 74 ----------------------------GGEL-----QRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEE 120
|
170
....*....|..
gi 37572301 651 GDRTMLVIAHRL 662
Cdd:cd03222 121 GKKTALVVEHDL 132
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
485-519 |
8.54e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.86 E-value: 8.54e-03
10 20 30
....*....|....*....|....*....|....*.
gi 37572301 485 LQGLTFTLHPGtVTALVGPNGSGKST-VAALLQNLY 519
Cdd:pfam13476 9 FRDQTIDFSKG-LTLITGPNGSGKTTiLDAIKLALY 43
|
|
| |
