|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
23-588 |
6.80e-172 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 500.46 E-value: 6.80e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 23 HPLRTLGYLLRPDRRRLTLAVLVFAVKHIPVWLLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLNYPLHMYFSKLSS 102
Cdd:COG1132 7 KLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 103 LAIRRTGTELRGALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVALPL 182
Cdd:COG1132 87 RLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 183 FIVVVPLAALLVRSLRGRIRADNEAFRVEVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGR 262
Cdd:COG1132 167 VLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 263 FGSLSWILLNVMAVAFLSGSALVAYYGlfGISPGDVVMISTFFTGLTASLTALLNLMPIVSRGLESVRSVGEVLQAP-DL 341
Cdd:COG1132 247 FFPLMELLGNLGLALVLLVGGLLVLSG--SLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPpEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 342 EVNEGKRDAGEVTGTFTFDEVGFRYPDAaEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGED 421
Cdd:COG1132 325 PDPPGAVPLPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 422 IAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGmDGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQK 501
Cdd:COG1132 404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYG-RPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 502 QRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL 562
|
....*..
gi 2764013554 582 AGTGPYA 588
Cdd:COG1132 563 ARGGLYA 569
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-588 |
1.92e-132 |
|
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: 403.83 E-value: 1.92e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 11 RKPPLDHAYVGEHPLRTLGYLLRPDRRRLTLAVLVFAVKHIPVWLLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLN 90
Cdd:COG2274 130 PTPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 91 YPLHMYFSKLSSLAIRRTGTELRGALCHRMQHLSIGYHSRVSAEVLQTKVvRDVDALETMLQQTAQNGLGAVMTLLGGLA 170
Cdd:COG2274 210 GLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 171 VIGFQAPVALPLFIVVVPLAALLVR-SLRGRIRADNEAFRVEVEQLSARVgEMTTLIPITRAHALERTALRRVDSSLQRV 249
Cdd:COG2274 289 VLFFYSPPLALVVLLLIPLYVLLGLlFQPRLRRLSREESEASAKRQSLLV-ETLRGIETIKALGAESRFRRRWENLLAKY 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 250 LTAGFRLDMLGGRFGSLSwILLNVMAVAFLSGsaLVAYYGLFG-ISPGDVVMISTFFTGLTASLTALLNLMPIVSRGLES 328
Cdd:COG2274 368 LNARFKLRRLSNLLSTLS-GLLQQLATVALLW--LGAYLVIDGqLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 329 VRSVGEVLQAP-DLEVNEGKRDAGEVTGTFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGF 407
Cdd:COG2274 445 LERLDDILDLPpEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 408 IRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGmDGEVPDEKIREALAAANALEFVDRMPQGVET 487
Cdd:COG2274 525 YEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLG-DPDATDEEIIEAARLAGLHDFIEALPMGYDT 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 488 VVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVME 567
Cdd:COG2274 604 VVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLD 683
|
570 580
....*....|....*....|.
gi 2764013554 568 RGRLVEVGTHEELLAGTGPYA 588
Cdd:COG2274 684 KGRIVEDGTHEELLARKGLYA 704
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
26-588 |
2.47e-110 |
|
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: 342.08 E-value: 2.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 26 RTLGYLlRPDRRRLTLAVLVFAVKHIPVWLLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLL----NYPLHMYFSKLS 101
Cdd:TIGR02203 4 RLWSYV-RPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLrgicSFVSTYLLSWVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 102 SLAIRrtgtELRGALCHRMQHLSIGYHSRVSAEVLQTKVVRDV--------DALETMLQQTaqnglgavMTLLGGLAVIg 173
Cdd:TIGR02203 83 NKVVR----DIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSeqvasaatDAFIVLVRET--------LTVIGLFIVL- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 174 FQAPVALPLFIVVV-PLAALLVRSLRGRIRADNEAFRVEVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTA 252
Cdd:TIGR02203 150 LYYSWQLTLIVVVMlPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 253 GFRLDMLGGRFGSLSWIL--LNVMAVAFLSGSALVAYYglfgISPGDVVMISTFFTGLTASLTALLNLMPIVSRGLESVR 330
Cdd:TIGR02203 230 AMKMTSAGSISSPITQLIasLALAVVLFIALFQAQAGS----LTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 331 SVGEVLQAPDlEVNEGKRDAGEVTGTFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRP 410
Cdd:TIGR02203 306 SLFTLLDSPP-EKDTGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 411 TAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGMDGEVPDEKIREALAAANALEFVDRMPQGVETVVG 490
Cdd:TIGR02203 385 DSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 491 ARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGR 570
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
570
....*....|....*...
gi 2764013554 571 LVEVGTHEELLAGTGPYA 588
Cdd:TIGR02203 545 IVERGTHNELLARNGLYA 562
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
358-588 |
7.08e-106 |
|
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: 318.71 E-value: 7.08e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDAAEHSV-RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSV 436
Cdd:cd03249 2 EFKNVSFRYPSRPDVPIlKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 437 VPQESILFEGSIRENVSYGmDGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRV 516
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYG-KPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 517 LVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGPYA 588
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYA 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
358-588 |
8.26e-106 |
|
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: 318.41 E-value: 8.26e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVV 437
Cdd:cd03251 2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 PQESILFEGSIRENVSYGMDGEvPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVL 517
Cdd:cd03251 82 SQDVFLFNDTVAENIAYGRPGA-TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 518 VLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGPYA 588
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
26-585 |
5.57e-98 |
|
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: 309.77 E-value: 5.57e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 26 RTLGYLLRPDRRRLTLAV---LVFAVKHIP-VWLLplvtARIID-IVVDHKPVSALWWNTAAVLVVLLLNYPLHMYFSKL 100
Cdd:COG4988 6 KRLKRLARGARRWLALAVllgLLSGLLIIAqAWLL----ASLLAgLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 101 SSLAIRRTGTELRGALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQ----QTAQnglgAVMTLLGGLAVIGFQA 176
Cdd:COG4988 82 AFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFArylpQLFL----AALVPLLILVAVFPLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 177 PVALPLFIVVVPLAALLVRSLRGRIRADNEAFRVEVEQLSA----RVGEMTTLipitRAHALERTALRRVDSSLQRvlta 252
Cdd:COG4988 158 WLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGhfldRLRGLTTL----KLFGRAKAEAERIAEASED---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 253 gFRLdmlggrfgslswILLNVMAVAFLSGS----------ALVAYYGLFGISPGDVvmisTFFTGLTASLTALLNLMPIv 322
Cdd:COG4988 230 -FRK------------RTMKVLRVAFLSSAvleffaslsiALVAVYIGFRLLGGSL----TLFAALFVLLLAPEFFLPL- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 323 sR-----------GLESVRSVGEVLQAPDLEVNEGKRDAGEVTG-TFTFDEVGFRYPDAAEhSVRDFSLSVRAGETVALV 390
Cdd:COG4988 292 -RdlgsfyharanGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 391 GGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGmDGEVPDEKIREALA 470
Cdd:COG4988 370 GPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLG-RPDASDEELEAALE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 471 AANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVV 550
Cdd:COG4988 449 AAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILI 528
|
570 580 590
....*....|....*....|....*....|....*
gi 2764013554 551 AHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTG 585
Cdd:COG4988 529 THRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
24-588 |
1.21e-96 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 306.63 E-value: 1.21e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 24 PLRTLGYLLRPDRRRLTLAvLVFAVKHIPVWL-LPLVTARIIDIVVDHKPVSALwwNTA---AVLVVLLLNYPLHMYFSK 99
Cdd:TIGR02204 5 PLAALWPFVRPYRGRVLAA-LVALLITAAATLsLPYAVRLMIDHGFSKDSSGLL--NRYfafLLVVALVLALGTAARFYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 100 LSSLAiRRTGTELRGALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVA 179
Cdd:TIGR02204 82 VTWLG-ERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 180 LPLFIVVVPLAALLVRSLRGRIRADNEAFRVEVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRldml 259
Cdd:TIGR02204 161 TSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQ---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 260 ggRFGSLSWILLNVMAVAFlSGSALVAYYG----LFG-ISPGDV---VMISTFFTGLTASLTALLNLmpiVSRGLESVRS 331
Cdd:TIGR02204 237 --RIRTRALLTAIVIVLVF-GAIVGVLWVGahdvIAGkMSAGTLgqfVFYAVMVAGSIGTLSEVWGE---LQRAAGAAER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 332 VGEVLQA-PDLEVNEGKRD-AGEVTGTFTFDEVGFRYPDAAEH-SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFI 408
Cdd:TIGR02204 311 LIELLQAePDIKAPAHPKTlPVPLRGEIEFEQVNFAYPARPDQpALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 409 RPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGMDgEVPDEKIREALAAANALEFVDRMPQGVETV 488
Cdd:TIGR02204 391 DPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRP-DATDEEVEAAARAAHAHEFISALPEGYDTY 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 489 VGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMER 568
Cdd:TIGR02204 470 LGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQ 549
|
570 580
....*....|....*....|
gi 2764013554 569 GRLVEVGTHEELLAGTGPYA 588
Cdd:TIGR02204 550 GRIVAQGTHAELIAKGGLYA 569
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-588 |
1.66e-93 |
|
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: 299.43 E-value: 1.66e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 5 PPPSAVRKPPLDHAYVGEHPLRTLGYLLRPDRRRLTLAVLVFAVKHIPVWLLPLVTARIIDIVVDHKPVSALwwntAAVL 84
Cdd:COG5265 2 PSARAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAAL----LVVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 85 VVLLLNYPL------------HMYFSKLSSLAIRRTGTElrgALCHrMQHLSIGYH-SRVSAEVlqTKVV-RDVDALETM 150
Cdd:COG5265 78 VGLLLAYGLlrllsvlfgelrDALFARVTQRAVRRLALE---VFRH-LHALSLRFHlERQTGGL--SRDIeRGTKGIEFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 151 LQQTAQNGLGAVMTLLGGLAVIGFQAPV--ALPLFIVVVPLAALLVRSLRGRIRadneaFRVEVEQLSARVGemttlipi 228
Cdd:COG5265 152 LRFLLFNILPTLLEIALVAGILLVKYDWwfALITLVTVVLYIAFTVVVTEWRTK-----FRREMNEADSEAN-------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 229 TRA-HAL-----------ERTALRRVDSSLQRVLTAGFRLdmlggrFGSLSWilLNVM-AVAFLSGSALVAYYGLFGI-- 293
Cdd:COG5265 219 TRAvDSLlnyetvkyfgnEAREARRYDEALARYERAAVKS------QTSLAL--LNFGqALIIALGLTAMMLMAAQGVva 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 294 ---SPGDVVMISTFFTGLTASLtallNLMPIVSRG--------------LESVRSVGEVLQAPDLEVNEGkrdagevtgT 356
Cdd:COG5265 291 gtmTVGDFVLVNAYLIQLYIPL----NFLGFVYREirqaladmermfdlLDQPPEVADAPDAPPLVVGGG---------E 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 357 FTFDEVGFRYpDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSV 436
Cdd:COG5265 358 VRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 437 VPQESILFEGSIRENVSYGMDGeVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRV 516
Cdd:COG5265 437 VPQDTVLFNDTIAYNIAYGRPD-ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPI 515
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 517 LVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGPYA 588
Cdd:COG5265 516 LIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYA 587
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
355-585 |
1.81e-90 |
|
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: 278.73 E-value: 1.81e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 355 GTFTFDEVGFRYpDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFL 434
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 435 SVVPQESILFEGSIRENVSYGmDGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDP 514
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTG 585
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
359-588 |
5.27e-86 |
|
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: 267.56 E-value: 5.27e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 359 FDEVGFRYPDAAEhSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVP 438
Cdd:cd03253 3 FENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 439 QESILFEGSIRENVSYGMDGeVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLV 518
Cdd:cd03253 82 QDTVLFNDTIGYNIRYGRPD-ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 519 LDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGPYA 588
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYA 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-591 |
8.79e-85 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 276.07 E-value: 8.79e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 26 RTLGYLLRPDRRRLTLAV--LVFAVKHIpvwLLPLVTARIIDIVVDHK---PVSALW-----WNTAA-VLVVLllnyplh 94
Cdd:PRK13657 9 RVLQYLGAEKRLGILLAVanVLLAAATF---AEPILFGRIIDAISGKGdifPLLAAWagfglFNIIAgVLVAR------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 95 myfsKLSSLAIRRTGTELRGALCHRMQhLSIGYHS-RVSAEVLQTkVVRDVDALETMLQQTAQNGLGAVMTLLGGLAV-- 171
Cdd:PRK13657 79 ----HADRLAHRRRLAVLTEYFERIIQ-LPLAWHSqRGSGRALHT-LLRGTDALFGLWLEFMREHLATLVALVVLLPLal 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 172 -IGFQ-APVALPLFIVVVPLAALLVRSlrgriradNEAFRVEVEQ----LSARV----GEMTTLIPITRAHAlERTALRR 241
Cdd:PRK13657 153 fMNWRlSLVLVVLGIVYTLITTLVMRK--------TKDGQAAVEEhyhdLFAHVsdaiGNVSVVQSYNRIEA-ETQALRD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 242 VdssLQRVLTAgfrldmlggRFGSLSW-ILLNV---------MAVAFLSGSALVAYyGLFGIspGDVVMISTFFTGLTAS 311
Cdd:PRK13657 224 I---ADNLLAA---------QMPVLSWwALASVlnraastitMLAILVLGAALVQK-GQLRV--GEVVAFVGFATLLIGR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 312 LTALLNLMPIVSRGLESVRSVGEVLQA-PDLEVNEGKRDAGEVTGTFTFDEVGFRYPDAAEhSVRDFSLSVRAGETVALV 390
Cdd:PRK13657 289 LDQVVAFINQVFMAAPKLEEFFEVEDAvPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQ-GVEDVSFEAKPGQTVAIV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 391 GGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGMDGEVpDEKIREALA 470
Cdd:PRK13657 368 GPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDAT-DEEMRAAAE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 471 AANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVV 550
Cdd:PRK13657 447 RAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFII 526
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2764013554 551 AHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGPYATTL 591
Cdd:PRK13657 527 AHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
358-570 |
2.93e-82 |
|
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: 255.39 E-value: 2.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVV 437
Cdd:cd03228 2 EFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 PQESILFEGSIRENVsygmdgevpdekirealaaanalefvdrmpqgvetvvgargarLSGGQKQRLAIARALVRDPRVL 517
Cdd:cd03228 82 PQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 518 VLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGR 570
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
132-592 |
1.00e-81 |
|
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: 267.40 E-value: 1.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 132 SAEVLqTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAP-------VALPLFIVVVPLAALLVRSLRGRIRAD 204
Cdd:COG4987 111 SGDLL-NRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPalalvlaLGLLLAGLLLPLLAARLGRRAGRRLAA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 205 NEAfrveveQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILLNVMAVAflsgsAL 284
Cdd:COG4987 190 ARA------ALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVA-----VL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 285 VAYYGLFGISPGDVVMISTFFTGLTASLTALLNLMPIVS---RGLESVRSVGEVLQAPDLEVNEGKRDAGEVTGTFTFDE 361
Cdd:COG4987 259 WLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQhlgRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELED 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 362 VGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQES 441
Cdd:COG4987 339 VSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRP 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 442 ILFEGSIRENVSYGmDGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDE 521
Cdd:COG4987 419 HLFDTTLRENLRLA-RPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDE 497
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 522 ATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGPYATTLQ 592
Cdd:COG4987 498 PTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
293-588 |
3.29e-80 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 263.80 E-value: 3.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 293 ISPGDVVMISTFFTGLTASLTALLNLMPIVSRGLESVRSVGEVLqapDLEV--NEGKRDAGEVTGTFTFDEVGFRYPDAA 370
Cdd:PRK11176 279 LTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAIL---DLEQekDEGKRVIERAKGDIEFRNVTFTYPGKE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 371 EHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRE 450
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIAN 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 451 NVSYGMDGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQS 530
Cdd:PRK11176 436 NIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 531 EALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGPYA 588
Cdd:PRK11176 516 ERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
358-588 |
3.33e-79 |
|
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: 250.10 E-value: 3.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRY-PDAAEhSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSV 436
Cdd:cd03252 2 TFEHVRFRYkPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 437 VPQESILFEGSIRENVSYGMDGeVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRV 516
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPG-MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 517 LVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGPYA 588
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-588 |
5.78e-77 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 258.50 E-value: 5.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 5 PPPSAVRKPPLDHAYVGEHPLRTLGYLlRPDRRRLTLAVLVFAVKHIPVWLLPLVTARIIDIVVDHKPVSALwwnTAAVL 84
Cdd:TIGR00958 130 SAGASEKEAEQGQSETADLLFRLLGLS-GRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPAL---ASAIF 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 85 VVLLlnyplhmyFSKLSSL-----------AIRRTGTELRGALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQ 153
Cdd:TIGR00958 206 FMCL--------LSIASSVsaglrggsfnyTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 154 TAQNGLGAVMTLLGGLAVIGFQAPVALPLFIVVVPLAALLVRSLRGRIRADNEAFRVEVEQLSARVGEMTTLIPITRAHA 233
Cdd:TIGR00958 278 NVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 234 LERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILLNVMAVAFLS-GSALVayygLFG-ISPGDVVMISTFFTGLTAS 311
Cdd:TIGR00958 358 AEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYyGGQLV----LTGkVSSGNLVSFLLYQEQLGEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 312 LTALLNLMPIVSRGLESVRSVGEVL-QAPDLEVNEGKRDAGeVTGTFTFDEVGFRYPDAAEHSV-RDFSLSVRAGETVAL 389
Cdd:TIGR00958 434 VRVLSYVYSGMMQAVGASEKVFEYLdRKPNIPLTGTLAPLN-LEGLIEFQDVSFSYPNRPDVPVlKGLTFTLHPGEVVAL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 390 VGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGMDgEVPDEKIREAL 469
Cdd:TIGR00958 513 VGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLT-DTPDEEIMAAA 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 470 AAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERlmRGRTVFV 549
Cdd:TIGR00958 592 KAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLL 669
|
570 580 590
....*....|....*....|....*....|....*....
gi 2764013554 550 VAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGPYA 588
Cdd:TIGR00958 670 IAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
55-588 |
3.35e-72 |
|
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: 244.87 E-value: 3.35e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 55 LLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLNyplhMYFSKLSSLAIRRTGT----ELRGALCHRMQHLSIGYHSR 130
Cdd:TIGR03797 154 LVPIATGILIGTAIPDADRSLLVQIALALLAAAVGA----AAFQLAQSLAVLRLETrmdaSLQAAVWDRLLRLPVSFFRQ 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 131 VSAEVLQTKVvrdvDALETMLQQTAQNGLGAVMTLLGGLAVIG--FQAPVALPLFIVVVPLAALLVRSLRGRIRADNEAF 208
Cdd:TIGR03797 230 YSTGDLASRA----MGISQIRRILSGSTLTTLLSGIFALLNLGlmFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERR 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 209 RVEVE-QLSARVGEMTTLIPITRAHALERTALRRVDS--SLQRVLTAGFR-----LDMLGGRFGSLSWILLNVMAVAFLS 280
Cdd:TIGR03797 306 LLELSgKISGLTVQLINGISKLRVAGAENRAFARWAKlfSRQRKLELSAQrienlLTVFNAVLPVLTSAALFAAAISLLG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 281 GSAL-----VAYYGLFGISPGDVvmistffTGLTASLTALLNLMPIVSRGLEsvrsvgeVLQAPDlEVNEGKRDAGEVTG 355
Cdd:TIGR03797 386 GAGLslgsfLAFNTAFGSFSGAV-------TQLSNTLISILAVIPLWERAKP-------ILEALP-EVDEAKTDPGKLSG 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 356 TFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLS 435
Cdd:TIGR03797 451 AIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLG 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 436 VVPQESILFEGSIRENVSyGMDGEVPDEKIREALAAANALEfVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPR 515
Cdd:TIGR03797 531 VVLQNGRLMSGSIFENIA-GGAPLTLDEAWEAARMAGLAED-IRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPR 608
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 516 VLVLDEATSALDNQSEALVQEALERLmrGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGPYA 588
Cdd:TIGR03797 609 ILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFA 679
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
41-588 |
3.11e-71 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 242.93 E-value: 3.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 41 LAVLVFA--------VKHIPVWLLPLVTARIIdivvdhkpvsalwwnTAAVLVVLLLnypLHMYFskLSSLAIRrTGTEL 112
Cdd:TIGR03796 171 LVIPAFSqifvdeilVQGRQDWLRPLLLGMGL---------------TALLQGVLTW---LQLYY--LRRLEIK-LAVGM 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 113 RGALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLggLAVIGFQAPVALPLFIVVVPLAAL 192
Cdd:TIGR03796 230 SARFLWHILRLPVRFFAQRHAGDIASRVQLNDQVAEFLSGQLATTALDAVMLVF--YALLMLLYDPVLTLIGIAFAAINV 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 193 LVRSLRGRIRAD-NEAFRVEVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILL 271
Cdd:TIGR03796 308 LALQLVSRRRVDaNRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLT 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 272 NVMAVAFLSGSALVAYYGlfGISPGDVVMISTFFTGLTASLTALLNL---MPIVSRGLESVRsvgEVLQAP-DLEVNEGK 347
Cdd:TIGR03796 388 SLNSALILVVGGLRVMEG--QLTIGMLVAFQSLMSSFLEPVNNLVGFggtLQELEGDLNRLD---DVLRNPvDPLLEEPE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 348 RDAG------EVTGTFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGED 421
Cdd:TIGR03796 463 GSAAtsepprRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIP 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 422 IAGLDLRTYRRFLSVVPQESILFEGSIRENVSYgMDGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQK 501
Cdd:TIGR03796 543 REEIPREVLANSVAMVDQDIFLFEGTVRDNLTL-WDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 502 QRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERlmRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:TIGR03796 622 QRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELW 699
|
....*..
gi 2764013554 582 AGTGPYA 588
Cdd:TIGR03796 700 AVGGAYA 706
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
353-571 |
7.33e-71 |
|
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: 227.74 E-value: 7.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 353 VTGTFTFDEVGFRYPDAAEHSV-RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYR 431
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 432 RFLSVVPQESILFEGSIRENVSYGMdGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALV 511
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAYGL-QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 512 RDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRL 571
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
355-572 |
2.07e-69 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 223.62 E-value: 2.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 355 GTFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFL 434
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 435 SVVPQESILFEGSIRENVSYGmDGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDP 514
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLG-APLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLV 572
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
40-566 |
2.29e-69 |
|
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: 233.72 E-value: 2.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 40 TLAVLVFAvkhipvWLLplvtARIID-IVVDHKPVSALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRTGTELRGALCH 118
Cdd:TIGR02857 16 ALLIIAQA------WLL----ARVVDgLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 119 RMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVALPLFIVVVPLAALLVRSLR 198
Cdd:TIGR02857 86 AVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILIG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 199 GRIRADNEAFRVEVEQLSARVGEMTTLIPITRAhalertaLRRVDSSLQRVLTAGfrlDMLGGRfgslswiLLNVMAVAF 278
Cdd:TIGR02857 166 WAAQAAARKQWAALSRLSGHFLDRLRGLPTLKL-------FGRAKAQAAAIRRSS---EEYRER-------TMRVLRIAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 279 LSGS----------ALVAYYGLFGISPGDVvmisTFFTGLTASLTALLNLMPI---------VSRGLESVRSVGEVLQAP 339
Cdd:TIGR02857 229 LSSAvlelfatlsvALVAVYIGFRLLAGDL----DLATGLFVLLLAPEFYLPLrqlgaqyhaRADGVAAAEALFAVLDAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 340 DLEVNEGKRDAGEVTGTFTFDEVGFRYPDAAEhSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDG 419
Cdd:TIGR02857 305 PRPLAGKAPVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 420 EDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGmDGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGG 499
Cdd:TIGR02857 384 VPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLA-RPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGG 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 500 QKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVM 566
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
355-576 |
2.49e-69 |
|
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: 223.52 E-value: 2.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 355 GTFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFL 434
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 435 SVVPQESILFEGSIRENvsygMD--GEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVR 512
Cdd:cd03244 81 SIIPQDPVLFSGTIRSN----LDpfGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2764013554 513 DPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGT 576
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
378-598 |
5.80e-62 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 215.09 E-value: 5.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 378 SLSVRAGETVALVGGSGAGKSTVLNLVIGFIrPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGmD 457
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG-N 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 458 GEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEA 537
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 538 LERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGPYATTLQPRAYSR 598
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEEI 588
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
362-571 |
3.84e-59 |
|
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: 195.13 E-value: 3.84e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 362 VGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQES 441
Cdd:cd03246 6 VSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 442 ILFEGSIRENVsygmdgevpdekirealaaanalefvdrmpqgvetvvgargarLSGGQKQRLAIARALVRDPRVLVLDE 521
Cdd:cd03246 86 ELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 522 ATSALDNQSEALVQEALERL-MRGRTVFVVAHRLSTIQDADRIVVMERGRL 571
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
32-582 |
2.75e-57 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 201.42 E-value: 2.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 32 LRPDRRRLTLAVLVFAVKHIPVWLLPLVTARIIDIVVDHKPVSALWWNTAAVLVVlllnYPLHMYFSKLSSLAIRRTGTE 111
Cdd:TIGR01842 1 LAKVKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGL----YLFLGLLDALRSFVLVRIGEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 112 LRGALCHRMQHLSIGYH-SRVSAEVLQTkvVRDVDALETMLQQTAQNGLgavmtllgglavigFQAPVaLPLFIVVVPL- 189
Cdd:TIGR01842 77 LDGALNQPIFAASFSATlRRGSGDGLQA--LRDLDQLRQFLTGPGLFAF--------------FDAPW-MPIYLLVCFLl 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 190 -----------AALLVRSLRGRIRADNEAFRVEVEQLSAR---VGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFR 255
Cdd:TIGR01842 140 hpwigilalggAVVLVGLALLNNRATKKPLKEATEASIRAnnlADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 256 LDMLGGRFGSLSWILLNVMAVAFLSGSALVAYYGlfGISPGDVVMISTFFTGLTASLTALLNLMPIVSRGLESVRSVGEV 335
Cdd:TIGR01842 220 ASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDG--EITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNEL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 336 LQapdlevNEGKRDAG----EVTGTFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPT 411
Cdd:TIGR01842 298 LA------NYPSRDPAmplpEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 412 AGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYgMDGEVPDEKIREALAAANALEFVDRMPQGVETVVGA 491
Cdd:TIGR01842 372 SGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGP 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 492 RGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERL-MRGRTVFVVAHRLSTIQDADRIVVMERGR 570
Cdd:TIGR01842 451 GGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGR 530
|
570
....*....|..
gi 2764013554 571 LVEVGTHEELLA 582
Cdd:TIGR01842 531 IARFGERDEVLA 542
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
152-582 |
2.95e-57 |
|
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: 201.90 E-value: 2.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 152 QQTAQNGLGAVMTL---LGGLAVIG-FQAPVAlPLFIVVV----PL--------AALLV-------RSLRGRIRADNEAF 208
Cdd:COG4618 112 GGAAAQALRDLDTLrqfLTGPGLFAlFDLPWA-PIFLAVLflfhPLlgllalvgALVLValallneRLTRKPLKEANEAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 209 RVEVEQLSA--RVGEmttlipITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILLNVMAVAFLSGSALVA 286
Cdd:COG4618 191 IRANAFAEAalRNAE------VIEAMGMLPALRRRWQRANARALALQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 287 YYGLfgISPGdvVMI-STFFTGLTasltallnLMPIVS-----RGLESVRS----VGEVLQApdLEVNEGKRDAGEVTGT 356
Cdd:COG4618 265 IQGE--ITPG--AMIaASILMGRA--------LAPIEQaiggwKQFVSARQayrrLNELLAA--VPAEPERMPLPRPKGR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 357 FTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSV 436
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 437 VPQESILFEGSIRENVSyGMdGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRV 516
Cdd:COG4618 411 LPQDVELFDGTIAENIA-RF-GDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRL 488
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 517 LVLDEATSALDNQSEALVQEALERL-MRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLA 582
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
171-588 |
1.57e-54 |
|
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: 196.88 E-value: 1.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 171 VIGFQAPVALPLFIVVVPLAALLVRSLRGRIRADNEAFRVEVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVL 250
Cdd:TIGR01193 289 FLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 251 TAGFRL---DMLGGRFGSLSWILLNVmaVAFLSGSALVAYYGlfgISPGDVVMISTFFTGLTASLTALLNLMPIVSRGLE 327
Cdd:TIGR01193 369 NKSFKYqkaDQGQQAIKAVTKLILNV--VILWTGAYLVMRGK---LTLGQLITFNALLSYFLTPLENIINLQPKLQAARV 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 328 SVRSVGEVLQAPDLEVNEGKRDAGE-VTGTFTFDEVGFRYPDAAEhSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIG 406
Cdd:TIGR01193 444 ANNRLNEVYLVDSEFINKKKRTELNnLNGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVG 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 407 FIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGMDGEVPDEKIREALAAANALEFVDRMPQGVE 486
Cdd:TIGR01193 523 FFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQ 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 487 TVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEalvQEALERL--MRGRTVFVVAHRLSTIQDADRIV 564
Cdd:TIGR01193 603 TELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLlnLQDKTIIFVAHRLSVAKQSDKII 679
|
410 420
....*....|....*....|....
gi 2764013554 565 VMERGRLVEVGTHEELLAGTGPYA 588
Cdd:TIGR01193 680 VLDHGKIIEQGSHDELLDRNGFYA 703
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
27-587 |
2.73e-53 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 191.47 E-value: 2.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 27 TLGYLL---RPDRRRLTLAVLVFAVKHIPVWLLPLVTARIIDIVV--DHKPVSALWWNTAAVLVVLLLNYPLHMY----F 97
Cdd:PRK10790 10 TLKRLLaygSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVakGNLPLGLVAGLAAAYVGLQLLAAGLHYAqsllF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 98 SKLSSLAIRRTGTELRGALCHrmQHLS------IGYH-SRVSAEvlqTKVVRD--VDALETMLQQTAqnglgavmtLLGG 168
Cdd:PRK10790 90 NRAAVGVVQQLRTDVMDAALR--QPLSafdtqpVGQLiSRVTND---TEVIRDlyVTVVATVLRSAA---------LIGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 169 LAVIGFQ-----APVALPLFIVVVPLAAL-------LVRSLRGRIRADNEAFRVEVEQLS--------ARVGEmtTLIPI 228
Cdd:PRK10790 156 MLVAMFSldwrmALVAIMIFPAVLVVMVIyqrystpIVRRVRAYLADINDGFNEVINGMSviqqfrqqARFGE--RMGEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 229 TRAHALERTALRRVDSSLQRVLtagfrldmlggrfgslswilLNVMAVAFLSGSALvayygLFGISPGDVVMIS------ 302
Cdd:PRK10790 234 SRSHYMARMQTLRLDGFLLRPL--------------------LSLFSALILCGLLM-----LFGFSASGTIEVGvlyafi 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 303 TFFTGLTASLTALLNLMPIVSRGLESVRSVGEVLQAPdlEVNEGKRDAGEVTGTFTFDEVGFRYPDaaEHSV-RDFSLSV 381
Cdd:PRK10790 289 SYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGP--RQQYGNDDRPLQSGRIDIDNVSFAYRD--DNLVlQNINLSV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 382 RAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGMDgeVP 461
Cdd:PRK10790 365 PSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD--IS 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 462 DEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALeRL 541
Cdd:PRK10790 443 EEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AA 521
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2764013554 542 MRGRTVFVV-AHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGPY 587
Cdd:PRK10790 522 VREHTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
374-584 |
4.10e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 178.72 E-value: 4.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGlDLRTYRRFLSVVPQESILFEG-SIRENV 452
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYPDlTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 S-----YGMDGEVPDEKIRealaaanalEFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:COG1131 95 RffarlYGLPRKEARERID---------ELLELF--GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 528 NQSEALVQEALERLM-RGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLAGT 584
Cdd:COG1131 164 PEARRELWELLRELAaEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
357-582 |
2.40e-51 |
|
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: 176.37 E-value: 2.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 357 FTFDEVGFRYPDAaEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSV 436
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 437 VPQ--ESILFEGSIRENVSYG-----MDGEVPDEKIREALAAANALEFVDRMPQgvetvvgargaRLSGGQKQRLAIARA 509
Cdd:COG1122 80 VFQnpDDQLFAPTVEEDVAFGpenlgLPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 510 LVRDPRVLVLDEATSALDNQSEALVQEALERL-MRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
354-576 |
1.71e-50 |
|
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: 173.37 E-value: 1.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 354 TGTFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRF 433
Cdd:cd03369 4 HGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 434 LSVVPQESILFEGSIRENVSygMDGEVPDEKIREALaaanalefvdRMPQGvetvvgarGARLSGGQKQRLAIARALVRD 513
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLD--PFDEYSDEEIYGAL----------RVSEG--------GLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 514 PRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGT 576
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
359-570 |
3.33e-49 |
|
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: 169.96 E-value: 3.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 359 FDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVP 438
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 439 Q--ESILFEGSIRENVSYG-----MDGEVPDEKIREALAAANALEFVDRMPQgvetvvgargaRLSGGQKQRLAIARALV 511
Cdd:cd03225 82 QnpDDQFFGPTVEEEVAFGlenlgLPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 512 RDPRVLVLDEATSALDNQSEALVQEALERLMR-GRTVFVVAHRLSTIQD-ADRIVVMERGR 570
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
310-592 |
6.75e-49 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 178.87 E-value: 6.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 310 ASLTALLNLMPI------VSRGLESVRSVGEVL-QAPDLEVNEgKRDAGEVTGTFTFDEVGFRYPDAAEHSVRDFSLSVR 382
Cdd:PRK11160 286 AALAAFEALMPVagafqhLGQVIASARRINEITeQKPEVTFPT-TSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 383 AGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGMDgEVPD 462
Cdd:PRK11160 365 AGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAP-NASD 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 463 EKIREALAAANALEFVDRmPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLM 542
Cdd:PRK11160 444 EALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA 522
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2764013554 543 RGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGPYATTLQ 592
Cdd:PRK11160 523 QNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
338-582 |
1.74e-48 |
|
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: 176.63 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 338 APDLEVNEGKRDAGEVTGT--FTFDEVGFRYPDAAEHS---VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTA 412
Cdd:COG1123 240 VPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTS 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 413 GRILLDGEDIAGL---DLRTYRRFLSVVPQ--ESILFEG-SIRENVSYGMD--GEVPDEKIREAlaaanalefVDRMPQG 484
Cdd:COG1123 320 GSILFDGKDLTKLsrrSLRELRRRVQMVFQdpYSSLNPRmTVGDIIAEPLRlhGLLSRAERRER---------VAELLER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 485 V---ETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDnqseALVQEALERLMR------GRTVFVVAHRLS 555
Cdd:COG1123 391 VglpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQILNLLRdlqrelGLTYLFISHDLA 466
|
250 260
....*....|....*....|....*...
gi 2764013554 556 TIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:COG1123 467 VVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
25-554 |
8.02e-48 |
|
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: 175.24 E-value: 8.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 25 LRTLGYLLRPDRRRLTLAVLVFAVKHIPVWLLPLVTARIIDIVVDHKPVSALwwNTAAVLVVLL-LNYPLHMYFSKLSSL 103
Cdd:TIGR02868 1 LLRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPPVLYL--SVAAVAVRAFgIGRAVFRYLERLVGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 104 -AIRRTGTELRGALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVALPL 182
Cdd:TIGR02868 79 dAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 183 FIVVVPLAALLVRSLRGRI-RADNEAFRVEVEQLSARVgeMTTLipitrAHALERTALRRVDSSLQRVLTAGFRLDMLGG 261
Cdd:TIGR02868 159 LAAGLLLAGFVAPLVSLRAaRAAEQALARLRGELAAQL--TDAL-----DGAAELVASGALPAALAQVEEADRELTRAER 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 262 RFGSLSWILLNVMAVAFLSGSALVAYYGLFGISPGDVV-MISTFFTGLTASLTALLNLMPIVSRGLESVRSVGEVL---- 336
Cdd:TIGR02868 232 RAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLApVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIvevl 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 337 -QAPDLEVNEGKRDAGEVTG--TFTFDEVGFRYPDAAEhSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAG 413
Cdd:TIGR02868 312 dAAGPVAEGSAPAAGAVGLGkpTLELRDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 414 RILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGmDGEVPDEKIREALAAANALEFVDRMPQGVETVVGARG 493
Cdd:TIGR02868 391 EVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA-RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGG 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 494 ARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRL 554
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
363-571 |
1.91e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 164.99 E-value: 1.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 363 GFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESI 442
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 443 LFEGSIRENVS--YGMDGEVPDEkirealaaanalefvDRMPQGVETV------VGARGARLSGGQKQRLAIARALVRDP 514
Cdd:COG4619 85 LWGGTVRDNLPfpFQLRERKFDR---------------ERALELLERLglppdiLDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRL 571
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
314-587 |
2.86e-46 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 171.82 E-value: 2.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 314 ALLNLMPIVSRGLESVRSVGEVLQAPdLEVNEGKRDAGEVTGTFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGS 393
Cdd:PRK10789 272 ALAWMFNIVERGSAAYSRIRAMLAEA-PVVKDGSEPVPEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPT 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 394 GAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGMDGEVPDEkIREALAAAN 473
Cdd:PRK10789 351 GSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQE-IEHVARLAS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 474 ALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHR 553
Cdd:PRK10789 430 VHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHR 509
|
250 260 270
....*....|....*....|....*....|....
gi 2764013554 554 LSTIQDADRIVVMERGRLVEVGTHEELLAGTGPY 587
Cdd:PRK10789 510 LSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
374-575 |
2.71e-45 |
|
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: 159.61 E-value: 2.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRtyRRFLSVVPQESILFEG-SIRENV 452
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPHlTVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 SYGM-DGEVPDEKIREALAAANALEfvdrmpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSE 531
Cdd:cd03259 94 AFGLkLRGVPKAEIRARVRELLELV-------GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2764013554 532 ALVQEALERLMR--GRTVFVVAHRLS-TIQDADRIVVMERGRLVEVG 575
Cdd:cd03259 167 EELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
362-575 |
5.53e-45 |
|
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: 159.21 E-value: 5.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 362 VGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD---LRTYRRFLSVVP 438
Cdd:cd03257 9 VSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 439 QESIL-------FEGSIRE--NVSYGMDGEVPDEKIREALAAA--NALEFVDRMPqgvetvvgargARLSGGQKQRLAIA 507
Cdd:cd03257 89 QDPMSslnprmtIGEQIAEplRIHGKLSKKEARKEAVLLLLVGvgLPEEVLNRYP-----------HELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 508 RALVRDPRVLVLDEATSALDNQSEALVQEALERL--MRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVG 575
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
375-587 |
1.82e-44 |
|
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: 158.22 E-value: 1.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD---LRTYRRFLSVVPQESILFEG-SIRE 450
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRIGMLFQGGALFDSlTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 451 NVSYGMD--GEVPDEKIRealaaanalefvDRmpqgVETV---VGARGAR------LSGGQKQRLAIARALVRDPRVLVL 519
Cdd:COG1127 102 NVAFPLRehTDLSEAEIR------------EL----VLEKlelVGLPGAAdkmpseLSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 520 DEATSALDNQSEALVQEALERL--MRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLAGTGPY 587
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELrdELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLASDDPW 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
358-574 |
1.84e-44 |
|
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: 157.63 E-value: 1.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDAAE--HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTyrrflS 435
Cdd:cd03293 2 EVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR-----G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 436 VVPQESILFE-GSIRENVSYGMDGE-VPDEKIREALAAANALE----FVDRMPqgvetvvgargARLSGGQKQRLAIARA 509
Cdd:cd03293 77 YVFQQDALLPwLTVLDNVALGLELQgVPKAEARERAEELLELVglsgFENAYP-----------HQLSGGMRQRVALARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 510 LVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLS-TIQDADRIVVMER--GRLVEV 574
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
358-580 |
2.52e-44 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 161.42 E-value: 2.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDAaeHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAglDLRTYRRFLSVV 437
Cdd:COG3842 7 ELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT--GLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 PQESILFEG-SIRENVSYG--MDGeVPDEKIREAlaaanalefVDRMpqgVETV-VGARGAR----LSGGQKQRLAIARA 509
Cdd:COG3842 83 FQDYALFPHlTVAENVAFGlrMRG-VPKAEIRAR---------VAEL---LELVgLEGLADRyphqLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 510 LVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRlstiQD-----ADRIVVMERGRLVEVGTHEEL 580
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHD----QEealalADRIAVMNDGRIEQVGTPEEI 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
356-585 |
3.35e-44 |
|
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: 157.71 E-value: 3.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 356 TFTFDEVgfrypdaaeHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGlDLRTYRRFLS 435
Cdd:COG4555 8 SKKYGKV---------PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 436 VVPQESILFEG-SIRENVSY-----GMDGEVPDEKIREALAAANALEFVDRmpqgvetvvgaRGARLSGGQKQRLAIARA 509
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYfaelyGLFDEELKKRIEELIELLGLEEFLDR-----------RVGELSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 510 LVRDPRVLVLDEATSALDNQSEALVQEALERLM-RGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLAGTG 585
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
364-582 |
8.75e-44 |
|
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: 156.20 E-value: 8.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 364 FRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGL---DLRTYRRFLSVVPQE 440
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 441 SILFEG-SIRENVSY-----GMDGEVPDEKIREALAaanaleFVdrmpqGVETVVGARGARLSGGQKQRLAIARALVRDP 514
Cdd:cd03258 91 FNLLSSrTVFENVALpleiaGVPKAEIEERVLELLE------LV-----GLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
362-592 |
9.52e-44 |
|
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: 156.50 E-value: 9.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 362 VGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQES 441
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 442 ilfEGSI--RENVsygmdGEVPDEKIREALAAANALEfVDRMPQGV---ETVVGARGARLSGGQKQRLAIARALVRDPRV 516
Cdd:COG1124 89 ---YASLhpRHTV-----DRILAEPLRIHGLPDREER-IAELLEQVglpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 517 LVLDEATSALD--NQSEALvqEALERLM--RGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLAGTG-PYATT 590
Cdd:COG1124 160 LLLDEPTSALDvsVQAEIL--NLLKDLReeRGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAGPKhPYTRE 237
|
..
gi 2764013554 591 LQ 592
Cdd:COG1124 238 LL 239
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
127-585 |
1.26e-43 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 167.85 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 127 YHSRVSAEVLQtKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVAL----PLFIVVVPlAALLVRSLRGRIR 202
Cdd:PLN03232 1001 FHTNPTGRVIN-RFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLwaimPLLILFYA-AYLYYQSTSREVR 1078
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 203 ADNEAFRVEVeqlSARVGEMTTLIPITRAH-ALERTAL---RRVDSSLQRVLTA-------GFRLDMLGGrfgSLSWILL 271
Cdd:PLN03232 1079 RLDSVTRSPI---YAQFGEALNGLSSIRAYkAYDRMAKingKSMDNNIRFTLANtssnrwlTIRLETLGG---VMIWLTA 1152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 272 NVMAVAFLSGSALVAYYGLFGispgdvvMISTFFTGLTASLTALLNLMPIVSRGLESVRSVGEVL----QAPDLEVNEGK 347
Cdd:PLN03232 1153 TFAVLRNGNAENQAGFASTMG-------LLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIdlpsEATAIIENNRP 1225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 348 RDAGEVTGTFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDL 427
Cdd:PLN03232 1226 VSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGL 1305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 428 RTYRRFLSVVPQESILFEGSIRENVSygMDGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIA 507
Cdd:PLN03232 1306 TDLRRVLSIIPQSPVLFSGTVRFNID--PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLA 1383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 508 RALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTG 585
Cdd:PLN03232 1384 RALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
375-587 |
1.70e-43 |
|
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: 155.35 E-value: 1.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGL---DLRTYRRFLSVVPQESILFEG-SIRE 450
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRRRMGMLFQSGALFDSlTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 451 NVSYG--MDGEVPDEKIREALAAANAL----EFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDPRVLVLDEATS 524
Cdd:cd03261 97 NVAFPlrEHTRLSEEEIREIVLEKLEAvglrGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 525 ALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLAGTGPY 587
Cdd:cd03261 166 GLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
308-585 |
2.77e-43 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 166.84 E-value: 2.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 308 LTASLTALLNLMPIVSRGLESVRSVGEVLQAPDLE--VNEGKRD--AGEVTGTFTFDEVGFRY-PDAAE--HSVrdfSLS 380
Cdd:PLN03130 1185 ITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAplVIENNRPppGWPSSGSIKFEDVVLRYrPELPPvlHGL---SFE 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 381 VRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENvsygMD--G 458
Cdd:PLN03130 1262 ISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN----LDpfN 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 459 EVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEAL 538
Cdd:PLN03130 1338 EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTI 1417
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2764013554 539 ERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTG 585
Cdd:PLN03130 1418 REEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
358-574 |
4.18e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 155.25 E-value: 4.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDAAEHS--VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRtyrrfLS 435
Cdd:COG1116 9 ELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----RG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 436 VVPQESILFE-GSIRENVSYGMDGE-VPDEKIREAlaaanalefVDRMpqgVETV--VGARGAR---LSGGQKQRLAIAR 508
Cdd:COG1116 84 VVFQEPALLPwLTVLDNVALGLELRgVPKAERRER---------AREL---LELVglAGFEDAYphqLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 509 ALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAH------RLstiqdADRIVVMER--GRLVEV 574
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVEE 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
357-575 |
6.57e-43 |
|
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: 151.70 E-value: 6.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 357 FTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDlRTYRRFLSV 436
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 437 VPQESILFEGSIRENVsygmdgevpdekirealaaanalefvdrmpqgvetvvgarGARLSGGQKQRLAIARALVRDPRV 516
Cdd:cd03247 80 LNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 517 LVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVG 575
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
374-571 |
6.74e-43 |
|
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: 151.40 E-value: 6.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIaGLDLRTYRRFLSVVPQESILFEG-SIRENV 452
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRRIGYLPEEPSLYENlTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 sygmdgevpdekirealaaanalefvdrmpqgvetvvgargaRLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEA 532
Cdd:cd03230 95 ------------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2764013554 533 LVQEALERLM-RGRTVFVVAHRLSTIQD-ADRIVVMERGRL 571
Cdd:cd03230 133 EFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
359-573 |
8.93e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 153.28 E-value: 8.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 359 FDEVGFRYPDAAE--HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD---LRTYRR- 432
Cdd:COG1136 7 LRNLTKSYGTGEGevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARLRRr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 433 FLSVVPQESILFEG-SIRENVSY-----GMDGEVPDEKIREAlaaanalefVDRMpqGVETVVGARGARLSGGQKQRLAI 506
Cdd:COG1136 87 HIGFVFQFFNLLPElTALENVALplllaGVSRKERRERAREL---------LERV--GLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 507 ARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQDADRIVVMERGRLVE 573
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
112-585 |
1.86e-42 |
|
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: 164.35 E-value: 1.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 112 LRGALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVALplfIVVVPLAA 191
Cdd:TIGR00957 1040 LHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAA---VIIPPLGL 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 192 LLVRSLRGRIRADNEAFRVEVEQLS---ARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRlDMLGGRFGSLSW 268
Cdd:TIGR00957 1117 LYFFVQRFYVASSRQLKRLESVSRSpvySHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYP-SIVANRWLAVRL 1195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 269 ILLNVMAVAFlsgSALVAYYGLFGISPGDVVMISTFFTGLTASLTALLNLMPIVSRGLESVRSVGEV----LQAPdLEVN 344
Cdd:TIGR00957 1196 ECVGNCIVLF---AALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYseteKEAP-WQIQ 1271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 345 EGKRDAG-EVTGTFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTvlnLVIGFIR---PTAGRILLDGE 420
Cdd:TIGR00957 1272 ETAPPSGwPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSS---LTLGLFRineSAEGEIIIDGL 1348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 421 DIAGLDLRTYRRFLSVVPQESILFEGSIRENvsygMD--GEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSG 498
Cdd:TIGR00957 1349 NIAKIGLHDLRFKITIIPQDPVLFSGSLRMN----LDpfSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSV 1424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 499 GQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHE 578
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPS 1504
|
....*..
gi 2764013554 579 ELLAGTG 585
Cdd:TIGR00957 1505 NLLQQRG 1511
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
358-582 |
5.14e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 158.53 E-value: 5.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTA---GRILLDGEDIAGLDLRTYRRFL 434
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 435 SVVPQE--SILFEGSIRENVSYGMD-GEVPDEKIREALAAANALEfvdrmpqGVETVVGARGARLSGGQKQRLAIARALV 511
Cdd:COG1123 86 GMVFQDpmTQLNPVTVGDQIAEALEnLGLSRAEARARVLELLEAV-------GLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2764013554 512 RDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
371-581 |
7.57e-42 |
|
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: 150.95 E-value: 7.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 371 EHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAglDLRTYRRFLSVVPQESILFEG-SIR 449
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHmTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVSYGM-----DGEVPDEKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDPRVLVLDEATS 524
Cdd:cd03299 90 KNIAYGLkkrkvDKKEIERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 525 ALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELL 581
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
357-580 |
1.30e-41 |
|
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: 150.02 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 357 FTFDEVGFRYPDaaEHSVRDFSLSVRAGETVALVGGSGAGKST---VLNLVIGFI--RPTAGRILLDGEDIAGLDLR--T 429
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIpgAPDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 430 YRRFLSVVPQESILFEGSIRENVSYG--MDGEVPDEKIRealaaanalefvDRMPQGVETV-----VGAR--GARLSGGQ 500
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrLHGIKLKEELD------------ERVEEALRKAalwdeVKDRlhALGLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 501 KQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEE 579
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 2764013554 580 L 580
Cdd:cd03260 227 I 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
358-570 |
2.04e-41 |
|
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: 147.01 E-value: 2.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDAaeHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVV 437
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 PQesilfegsirenvsygmdgevpdekirealaaanalefvdrmpqgvetvvgargarLSGGQKQRLAIARALVRDPRVL 517
Cdd:cd00267 79 PQ--------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 518 VLDEATSALDNQSEALVQEALERLM-RGRTVFVVAHRLSTIQDA-DRIVVMERGR 570
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
357-581 |
2.43e-41 |
|
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: 150.19 E-value: 2.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 357 FTFDEVGFRYPDAAehSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSV 436
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 437 VPQESIL-FEGSIRENVSYG---------MDGEVPDEKIREALAAANALEFVDRMpqgVETvvgargarLSGGQKQRLAI 506
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGryphlglfgRPSAEDREAVEEALERTGLEHLADRP---VDE--------LSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 507 ARALVRDPRVLVLDEATSALD--NQSEALvqEALERL--MRGRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDlaHQLEVL--ELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
358-586 |
5.73e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 148.36 E-value: 5.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDAAEHsvrdFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIagLDLRTYRRFLSVV 437
Cdd:COG3840 3 RLDDLTYRYGDFPLR----FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL--TALPPAERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 PQESILFEG-SIRENVSYGMDgevPD--------EKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIAR 508
Cdd:COG3840 77 FQENNLFPHlTVAQNIGLGLR---PGlkltaeqrAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 509 ALVRDPRVLVLDEATSALDnqsEALVQEALE-----RLMRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:COG3840 143 CLVRKRPILLLDEPFSALD---PALRQEMLDlvdelCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
....
gi 2764013554 583 GTGP 586
Cdd:COG3840 220 GEPP 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
340-582 |
5.80e-41 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 159.81 E-value: 5.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 340 DLEVNEGKR--DAGEVTGTFTFDEVGFRY---PDAAEHsvRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGF------- 407
Cdd:PTZ00265 1147 DVRDNGGIRikNKNDIKGKIEIMDVNFRYisrPNVPIY--KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndh 1224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 408 -----------------------------------------------IRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQE 440
Cdd:PTZ00265 1225 hivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQE 1304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 441 SILFEGSIRENVSYGMDgEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLD 520
Cdd:PTZ00265 1305 PMLFNMSIYENIKFGKE-DATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLD 1383
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 521 EATSALDNQSEALVQEALERL--MRGRTVFVVAHRLSTIQDADRIVVMER----GRLVEV-GTHEELLA 582
Cdd:PTZ00265 1384 EATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLS 1452
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
357-570 |
2.77e-40 |
|
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: 144.64 E-value: 2.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 357 FTFDEVGFRYPDAaeHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD--LRTYRRFL 434
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 435 SVVPQESILFEG-SIRENVSYGmdgevpdekirealaaanalefvdrmpqgvetvvgargarLSGGQKQRLAIARALVRD 513
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG----------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 514 PRVLVLDEATSALDNQSEALVQEALERL--MRGRTVFVVAHRLSTIQD-ADRIVVMERGR 570
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
374-524 |
4.72e-40 |
|
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: 143.17 E-value: 4.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILF-EGSIRENV 452
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 453 SYGMDGEVPDEKIREALAAANALEFvdRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATS 524
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKL--GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
372-580 |
7.65e-40 |
|
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: 145.46 E-value: 7.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDlrTYRRFLSVVPQESILFEG-SIRE 450
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP--PHKRPVNTVFQNYALFPHlTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 451 NVSYG-----MDGEVPDEKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDPRVLVLDEATSA 525
Cdd:cd03300 92 NIAFGlrlkkLPKAEIKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 526 LDNQSEALVQEALERLMR--GRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEEL 580
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
364-582 |
1.26e-39 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 147.92 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 364 FRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD---LRTYRRFLSVVPQE 440
Cdd:COG1135 11 FPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereLRAARRKIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 441 SILFEG-SIRENVSY-----GMDGEVPDEKirealaaanalefVDRMpqgVETV-----VGARGARLSGGQKQRLAIARA 509
Cdd:COG1135 91 FNLLSSrTVAENVALpleiaGVPKAEIRKR-------------VAEL---LELVglsdkADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 510 LVRDPRVLVLDEATSALDNQSE----ALVQEALERLmrGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTrsilDLLKDINREL--GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDVFA 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
372-582 |
1.79e-39 |
|
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: 144.11 E-value: 1.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGldLRTYRRF---LSVVPQESILFEG-S 447
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG--LPPHERAragIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 448 IRENVSYGMDGEVPDEkirealaaanalefVDRMPQGV-------ETVVGARGARLSGGQKQRLAIARALVRDPRVLVLD 520
Cdd:cd03224 92 VEENLLLGAYARRRAK--------------RKARLERVyelfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 521 EATSALdnqSEALVQEALERLMR----GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:cd03224 158 EPSEGL---APKIVEEIFEAIRElrdeGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
299-579 |
3.56e-39 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 154.42 E-value: 3.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 299 VMISTFFtgLTASLTALLNLMpivsRGLESVRSVGEVL-QAPDLEVNEGKRDAGEVTgTFTFDEVGFRYPDAAEHSV-RD 376
Cdd:PTZ00265 331 VLISMFM--LTIILPNITEYM----KSLEATNSLYEIInRKPLVENNDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIyKD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 377 FSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILL-DGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYG 455
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYS 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 456 M---------------DGE-----------------------------------------VPDEKIREALAAANALEFVD 479
Cdd:PTZ00265 484 LyslkdlealsnyyneDGNdsqenknkrnscrakcagdlndmsnttdsneliemrknyqtIKDSEVVDVSKKVLIHDFVS 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 480 RMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLM--RGRTVFVVAHRLSTI 557
Cdd:PTZ00265 564 ALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTI 643
|
330 340
....*....|....*....|....*
gi 2764013554 558 QDADRIVVM---ERGRLVEVGTHEE 579
Cdd:PTZ00265 644 RYANTIFVLsnrERGSTVDVDIIGE 668
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
358-582 |
5.69e-39 |
|
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: 143.21 E-value: 5.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDAAEhSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVV 437
Cdd:cd03295 2 EFENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 PQESILF-EGSIRENVsygmdGEVP------DEKIREALAAANA------LEFVDRMPqgvetvvgargARLSGGQKQRL 504
Cdd:cd03295 81 IQQIGLFpHMTVEENI-----ALVPkllkwpKEKIRERADELLAlvgldpAEFADRYP-----------HELSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 505 AIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRL-STIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
.
gi 2764013554 582 A 582
Cdd:cd03295 225 R 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
355-570 |
6.74e-39 |
|
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: 141.84 E-value: 6.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 355 GTFTFDEVGFRYPDAaehsVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEdiagldlrtyrrfL 434
Cdd:cd03250 6 ASFTWDSGEQETSFT----LKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------I 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 435 SVVPQESILFEGSIRENVSYG--MDGE-----------VPDEKIrealaaanalefvdrMPQGVETVVGARGARLSGGQK 501
Cdd:cd03250 69 AYVSQEPWIQNGTIRENILFGkpFDEEryekvikacalEPDLEI---------------LPDGDLTEIGEKGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 502 QRLAIARALVRDPRVLVLDEATSALDNQ-SEALVQEAL-ERLMRGRTVFVVAHRLSTIQDADRIVVMERGR 570
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
359-582 |
8.86e-39 |
|
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: 143.34 E-value: 8.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 359 FDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD-LRTYRRFLSVV 437
Cdd:TIGR04520 3 VENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 ---P--QesilFEGSI-RENVSYGMdgE---VPDEKIREALAAANAL----EFVDRMPQgvetvvgargaRLSGGQKQRL 504
Cdd:TIGR04520 83 fqnPdnQ----FVGATvEDDVAFGL--EnlgVPREEMRKRVDEALKLvgmeDFRDREPH-----------LLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 505 AIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLA 582
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
362-571 |
1.69e-38 |
|
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: 141.09 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 362 VGFRYPDAAE--HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRT----YRRFLS 435
Cdd:cd03255 6 LSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafRRRHIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 436 VVPQESILFEG-SIRENVSYGMDGevpdEKIREALAAANALEFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDP 514
Cdd:cd03255 86 FVFQSFNLLPDlTALENVELPLLL----AGVPKKERRERAEELLERV--GLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEALERL--MRGRTVFVVAHRLSTIQDADRIVVMERGRL 571
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
374-581 |
6.05e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 143.36 E-value: 6.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDiAGLDLRTYRRFLSVVPQESILFEG-SIRENV 452
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD-LFTNLPPRERRVGFVFQHYALFPHmTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 SYGMDGEVPD-----EKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:COG1118 97 AFGLRVRPPSkaeirARVEELLELVQLEGLADRYP-----------SQLSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 528 NQsealVQEALERLMR-------GRTVFVV-----AHRLstiqdADRIVVMERGRLVEVGTHEELL 581
Cdd:COG1118 166 AK----VRKELRRWLRrlhdelgGTTVFVThdqeeALEL-----ADRVVVMNQGRIEQVGTPDEVY 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
374-582 |
9.45e-38 |
|
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: 140.86 E-value: 9.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGL---DLRTYRR-FLSVVPQESILF-EGSI 448
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRkKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 449 RENVSYGMDGEVPDEKIREALAAANALE-----FVDRMPQgvetvvgargaRLSGGQKQRLAIARALVRDPRVLVLDEAT 523
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELvglegWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 524 SALDNQSEALVQEALERL--MRGRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEELLA 582
Cdd:cd03294 189 SALDPLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
375-582 |
1.43e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 139.36 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIA--GLDLRTYRRFLSVVPQESILFEG-SIREN 451
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLRRKVGMVFQQFNLFPHlTVLEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 452 VSY------GMDGEVPDEKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDPRVLVLDEATSA 525
Cdd:COG1126 98 VTLapikvkKMSKAEAEERAMELLERVGLADKADAYP-----------AQLSGGQQQRVAIARALAMEPKVMLFDEPTSA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 526 LDNQseaLVQEALErLMR-----GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:COG1126 167 LDPE---LVGEVLD-VMRdlakeGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
358-580 |
8.11e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 140.59 E-value: 8.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYpdAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAglDLRTYRRFLSVV 437
Cdd:COG3839 5 ELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT--DLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 PQESILFEG-SIRENVSYG-----MDGEVPDEKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALV 511
Cdd:COG3839 81 FQSYALYPHmTVYENIAFPlklrkVPKAEIDRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 512 RDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHrlstiqD-------ADRIVVMERGRLVEVGTHEEL 580
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRrlGTTTIYVTH------DqveamtlADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
362-575 |
1.19e-36 |
|
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: 134.87 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 362 VGFRYPDAaeHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQES 441
Cdd:cd03214 5 LSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 442 ILFegsirenvsyGMDGevpdekirealaaanaleFVDRmpqGVETvvgargarLSGGQKQRLAIARALVRDPRVLVLDE 521
Cdd:cd03214 83 ELL----------GLAH------------------LADR---PFNE--------LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 522 ATSALD--NQSEALvqEALERLMR--GRTVFVVAHRLS-TIQDADRIVVMERGRLVEVG 575
Cdd:cd03214 124 PTSHLDiaHQIELL--ELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
372-582 |
1.37e-36 |
|
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: 136.27 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGldLRTYRRF---LSVVPQESILFEG-S 447
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG--LPPHRIArlgIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 448 IRENVSYGMDGEVPDEKIREAlaaanalefVDRM----PQgVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEAT 523
Cdd:COG0410 95 VEENLLLGAYARRDRAEVRAD---------LERVyelfPR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 524 SALdnqSEALVQE---ALERLMR-GRTVFVV---AHRLSTIqdADRIVVMERGRLVEVGTHEELLA 582
Cdd:COG0410 165 LGL---APLIVEEifeIIRRLNReGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
362-582 |
9.64e-36 |
|
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: 136.72 E-value: 9.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 362 VGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRP---TAGRILLDGEDIAGLD---LRTYR-RFL 434
Cdd:COG0444 9 VYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekeLRKIRgREI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 435 SVVPQES------------ILFEGsIRenVSYGMDGEVPDEKIREALAA---ANALEFVDRMP-QgvetvvgargarLSG 498
Cdd:COG0444 89 QMIFQDPmtslnpvmtvgdQIAEP-LR--IHGGLSKAEARERAIELLERvglPDPERRLDRYPhE------------LSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 499 GQKQRLAIARALVRDPRVLVLDEATSALDnqseALVQ----EALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRL 571
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALD----VTIQaqilNLLKDLQRelGLAILFITHDLGVVAEiADRVAVMYAGRI 229
|
250
....*....|.
gi 2764013554 572 VEVGTHEELLA 582
Cdd:COG0444 230 VEEGPVEELFE 240
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
373-580 |
1.20e-35 |
|
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: 134.00 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 373 SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRtyRRFLSVVPQESILFEG-SIREN 451
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 452 VSYGMD----GEVPDE-----KIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDPRVLVLDEA 522
Cdd:cd03296 95 VAFGLRvkprSERPPEaeiraKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 523 TSALDnqseALVQEALERLMRG-------RTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEEL 580
Cdd:cd03296 164 FGALD----AKVRKELRRWLRRlhdelhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
364-580 |
1.50e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 136.40 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 364 FRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGL---DLRTYRRFLSVV--- 437
Cdd:COG4608 24 FGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVfqd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 PQESILFEGSIRENVSYGMD--GEVPDEKIREALAAANAL-----EFVDRMPQgvetvvgargaRLSGGQKQRLAIARAL 510
Cdd:COG4608 104 PYASLNPRMTVGDIIAEPLRihGLASKAERRERVAELLELvglrpEHADRYPH-----------EFSGGQRQRIGIARAL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 511 VRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEEL 580
Cdd:COG4608 173 ALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
360-582 |
1.68e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 134.76 E-value: 1.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 360 DEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQ 439
Cdd:PRK13635 9 EHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 440 E-SILFEGS-IRENVSYGMDGE-VPD----EKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVR 512
Cdd:PRK13635 89 NpDNQFVGAtVQDDVAFGLENIgVPReemvERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 513 DPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
374-579 |
1.76e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 137.39 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRtyRRFLSVVPQESILF-EGSIRENV 452
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 SYGMDGE-VPDEKIREALAAANalefvdRMPQgVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSE 531
Cdd:PRK09452 108 AFGLRMQkTPAAEITPRVMEAL------RMVQ-LEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 532 ALVQEALERLMR--GRT-VFVVAHRLSTIQDADRIVVMERGRLVEVGTHEE 579
Cdd:PRK09452 181 KQMQNELKALQRklGITfVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
355-589 |
2.68e-35 |
|
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: 133.50 E-value: 2.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 355 GTFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTvlnLVIGFIRPT---AGRILLDGEDIAGLDLRTYR 431
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSS---LSLAFFRMVdifDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 432 RFLSVVPQESILFEGSIRENvsygMDGE--VPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARA 509
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFN----LDPEckCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 510 LVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAG-TGPYA 588
Cdd:cd03288 171 FVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQeDGVFA 250
|
.
gi 2764013554 589 T 589
Cdd:cd03288 251 S 251
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
372-582 |
2.83e-35 |
|
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: 132.95 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDL-RTYRRFLSVVPQESILFEG-SIR 449
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPhEIARLGIGRTFQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVSYGMdgevpdekIREALAAANALEFVDRMPQGVETV------VG------ARGARLSGGQKQRLAIARALVRDPRVL 517
Cdd:cd03219 94 ENVMVAA--------QARTGSGLLLARARREEREARERAeellerVGladladRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 518 VLDEATSALdnqSEALVQEALERLM----RGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:cd03219 166 LLDEPAAGL---NPEETEELAELIRelreRGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
365-580 |
2.99e-35 |
|
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: 132.24 E-value: 2.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 365 RYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGlDLRTYRRFLSVVPQESILF 444
Cdd:cd03263 9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 445 EG-SIRENVSY--GMDGeVPDEKIREAlaaanalefVDRMPQGVE-TVVGARGAR-LSGGQKQRLAIARALVRDPRVLVL 519
Cdd:cd03263 88 DElTVREHLRFyaRLKG-LPKSEIKEE---------VELLLRVLGlTDKANKRARtLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 520 DEATSALDNQSEALVQEALERLMRGRTVFVVAHrlsTIQDA----DRIVVMERGRLVEVGTHEEL 580
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGRSIILTTH---SMDEAealcDRIAIMSDGKLRCIGSPQEL 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
376-582 |
3.66e-35 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 136.01 E-value: 3.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDI----AGLDLRTYRRFLSVVPQESILFEG-SIRE 450
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 451 NVSYGM-DGEVPDEKIREalaaanalefvDRMPQ--GVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:TIGR02142 95 NLRYGMkRARPSERRISF-----------ERVIEllGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 528 NQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:TIGR02142 164 DPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
359-579 |
5.13e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.71 E-value: 5.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 359 FDEVGFRYPDAAEHsVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGL---DLRTYRRFLS 435
Cdd:COG2884 4 FENVSKRYPGGREA-LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 436 VVPQE-SILFEGSIRENVSYGMD-GEVPDEKIRealaaanalefvDRMPQ-----GVETVVGARGARLSGGQKQRLAIAR 508
Cdd:COG2884 83 VVFQDfRLLPDRTVYENVALPLRvTGKSRKEIR------------RRVREvldlvGLSDKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 509 ALVRDPRVLVLDEATSALDNQSEALVQEALERL-MRGRTVFVVAHRLSTIQDAD-RIVVMERGRLVEVGTHEE 579
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPkRVLELEDGRLVRDEARGV 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
358-581 |
5.66e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.14 E-value: 5.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDaaEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIagldlRTYRRFLSVV 437
Cdd:COG1121 8 ELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 PQESILFEG---SIRENVSYGMDGEVPDEKIREALAAANALEFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDP 514
Cdd:COG1121 81 PQRAEVDWDfpiTVRDVVLMGRYGRRGLFRRPSRADREAVDEALERV--GLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEALERL-MRGRTVFVVAHRLSTIQD-ADRIVVMERgRLVEVGTHEELL 581
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNR-GLVAHGPPEEVL 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
376-575 |
6.16e-35 |
|
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: 131.26 E-value: 6.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVR---AGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDG----EDIAGLDLRTYRRFLSVVPQESILFEG-S 447
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfDSRKKINLPPQQRKIGLVFQQYALFPHlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 448 IRENVSYGMDGEVPDEKirealaaanaLEFVDRMPQ--GVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSA 525
Cdd:cd03297 92 VRENLAFGLKRKRNRED----------RISVDELLDllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 526 LDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVG 575
Cdd:cd03297 162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
359-569 |
8.86e-35 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 130.73 E-value: 8.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 359 FDEVGFRYPDaaEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRtyrrfLSVVP 438
Cdd:cd03235 2 VEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 439 Q-ESIL--FEGSIRENVSYGMDGEVP---------DEKIREALAAANALEFVDRmpqgvetvvgaRGARLSGGQKQRLAI 506
Cdd:cd03235 75 QrRSIDrdFPISVRDVVLMGLYGHKGlfrrlskadKAKVDEALERVGLSELADR-----------QIGELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 507 ARALVRDPRVLVLDEATSALDNQSEALVQEALERL-MRGRTVFVVAHRLSTIQD-ADRIVVMERG 569
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
374-582 |
2.37e-34 |
|
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: 130.93 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGldLRTYRR--------FlsvvpQESILFE 445
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG--LPPHRIarlgiartF-----QNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 446 G-SIRENV----SYGMDGEVPDEKIREALAAANALEFVDRMPQ-----GVETVVGARGARLSGGQKQRLAIARALVRDPR 515
Cdd:COG0411 93 ElTVLENVlvaaHARLGRGLLAALLRLPRARREEREARERAEEllervGLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 516 VLVLDEATSALdnqSEALVQEALERLMR-----GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:COG0411 173 LLLLDEPAAGL---NPEETEELAELIRRlrderGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
374-575 |
2.51e-34 |
|
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: 129.30 E-value: 2.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAglDLRTYRRFLSVVPQESILF-EGSIRENV 452
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAMVFQNYALYpHMTVYDNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 SYG-----MDGEVPDEKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:cd03301 94 AFGlklrkVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 528 NQSEALVQEALERLMR--GRTVFVVAH-RLSTIQDADRIVVMERGRLVEVG 575
Cdd:cd03301 163 AKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
357-572 |
4.82e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 129.79 E-value: 4.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 357 FTFDEVGFRYPDAAeHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGL---DLRTYRRF 433
Cdd:COG3638 3 LELRNLSKRYPGGT-PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgrALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 434 LSVVPQESILFEG-SIRENVSYGMDGEVP-----------DEKIREALaaanaleFVDRMpqGVETVVGARGARLSGGQK 501
Cdd:COG3638 82 IGMIFQQFNLVPRlSVLTNVLAGRLGRTStwrsllglfppEDRERALE-------ALERV--GLADKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2764013554 502 QRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLV 572
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
364-572 |
7.96e-34 |
|
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: 127.76 E-value: 7.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 364 FRYPDAAEhSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAgldLRTYRRFLSVVPQES-- 441
Cdd:cd03226 7 FSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQDVdy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 442 ILFEGSIRENVSYGMDgEVPD--EKIREALAAANALEFVDRMPQGvetvvgargarLSGGQKQRLAIARALVRDPRVLVL 519
Cdd:cd03226 83 QLFTDSVREELLLGLK-ELDAgnEQAETVLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 520 DEATSALDNQSEALVQEALERLM-RGRTVFVVAHRLSTIQD-ADRIVVMERGRLV 572
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
373-580 |
1.13e-33 |
|
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: 127.87 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 373 SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGlDLRTYRRFLSVVPQESILFEG-SIREN 451
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 452 VS-----YGMDGEVPDEKIREALAAANALEFVDRMpqgVETvvgargarLSGGQKQRLAIARALVRDPRVLVLDEATSAL 526
Cdd:cd03265 94 LYiharlYGVPGAERRERIDELLDFVGLLEAADRL---VKT--------YSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 527 DNQSEALVQEALERLMR--GRTVFVVAHRLSTI-QDADRIVVMERGRLVEVGTHEEL 580
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-582 |
2.00e-33 |
|
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: 134.54 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 28 LGYLLRPDRRRLTLAVLVFAVKHIP-VWLLPLVTARIIDIVVDhkPVSALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIR 106
Cdd:COG4615 4 LRLLLRESRWLLLLALLLGLLSGLAnAGLIALINQALNATGAA--LARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 107 RtgteLRGALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALeTMLQQTAQNGLGAVMTLLGGLAVIGFQAPVALPLFIVV 186
Cdd:COG4615 82 R----LRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 187 VPLAALLVRSLRGRIRADNEAFRVEVEQLSARVGEMTTLIPITRAHALERTALRRVDssLQRVLTAGFRLDMLGGRFGSL 266
Cdd:COG4615 157 LGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKLNRRRRRAFFDED--LQPTAERYRDLRIRADTIFAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 267 SWILLNVMAVAFLsGSALVAYYGLFGISPGDVVMISTFFTGLTASLTALLNLMPIVSRG---LESVRSVGEVLQAPDLEV 343
Cdd:COG4615 235 ANNWGNLLFFALI-GLILFLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRAnvaLRKIEELELALAAAEPAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 344 NEGKRDAGEVT-GTFTFDEVGFRYPDAAEHS---VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDG 419
Cdd:COG4615 314 ADAAAPPAPADfQTLELRGVTYRYPGEDGDEgftLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 420 EDIAGLDLRTYRRFLSVVPQESILFEGsirenvSYGMDGEVPDEKIRealaaanalEFVDRMpqGVETVVGARGAR---- 495
Cdd:COG4615 394 QPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDGEADPARAR---------ELLERL--ELDHKVSVEDGRfstt 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 496 -LSGGQKQRLAIARALVRDPRVLVLDEATSALDNQ-----SEALVQEaLERlmRGRTVFVVAHrlstiqD------ADRI 563
Cdd:COG4615 457 dLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfYTELLPE-LKA--RGKTVIAISH------DdryfdlADRV 527
|
570
....*....|....*....
gi 2764013554 564 VVMERGRLVEVGTHEELLA 582
Cdd:COG4615 528 LKMDYGKLVELTGPAALAA 546
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
377-591 |
5.88e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 126.24 E-value: 5.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 377 FSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAgldlRT--YRRFLSVVPQESILFEG-SIRENVS 453
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT----TTppSRRPVSMLFQENNLFSHlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 454 YGMD-----GEVPDEKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDPRVLVLDEATSALDn 528
Cdd:PRK10771 94 LGLNpglklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 529 qsEALVQEALERL-----MRGRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEELLAGTGPYATTL 591
Cdd:PRK10771 162 --PALRQEMLTLVsqvcqERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
374-582 |
8.83e-33 |
|
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: 125.73 E-value: 8.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDL-RTYRRFLSVVPQESILFEG-SIREN 451
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 452 VSYGMDGEVPDEKIREALAAANALEFvdrmpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSE 531
Cdd:cd03218 96 ILAVLEIRGLSKKEREEKLEELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 532 ALVQEALERLM-RGRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEELLA 582
Cdd:cd03218 170 QDIQKIIKILKdRGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
365-572 |
1.31e-32 |
|
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: 122.92 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 365 RYPdaAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDlrtyrrflsvvpqesilf 444
Cdd:cd03216 9 RFG--GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 445 egsirenvsygmdgevPDEKIRealaaanalefvdrmpQGVETVvgargARLSGGQKQRLAIARALVRDPRVLVLDEATS 524
Cdd:cd03216 69 ----------------PRDARR----------------AGIAMV-----YQLSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2764013554 525 ALDNQSEALVQEALERLM-RGRTVFVVAHRLSTIQD-ADRIVVMERGRLV 572
Cdd:cd03216 112 ALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
372-582 |
1.74e-32 |
|
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: 128.29 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVR----AGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDI----AGLDLRTYRRFLSVVPQESIL 443
Cdd:COG4148 9 LRRGGFTLDVDftlpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsaRGIFLPPHRRRIGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 444 FEG-SIRENVSYGMdgevpdekiREALAAANALEF---VDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVL 519
Cdd:COG4148 89 FPHlSVRGNLLYGR---------KRAPRAERRISFdevVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 520 DEATSALDNQSEALVQEALERLmRGRT---VFVVAH------RLstiqdADRIVVMERGRLVEVGTHEELLA 582
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERL-RDELdipILYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
357-580 |
1.94e-32 |
|
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: 124.99 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 357 FTFDEVGFRYPDAaEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGL---DLRTYRRF 433
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 434 LSVVPQESILFEG-SIRENVSYGMDGEVP-----------DEKIREALAaanalefVDRMpqGVETVVGARGARLSGGQK 501
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGRLGRRStwrslfglfpkEEKQRALAA-------LERV--GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 502 QRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHE 578
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPA 230
|
..
gi 2764013554 579 EL 580
Cdd:cd03256 231 EL 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
372-580 |
2.57e-32 |
|
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: 124.17 E-value: 2.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLdlRTYRRF---LSVVPQESILFEG-S 447
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL--PPHERAragIAYVPQGREIFPRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 448 IRENVSYGMDG------EVPDEkirealaaanaleFVDRMPQgVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDE 521
Cdd:TIGR03410 92 VEENLLTGLAAlprrsrKIPDE-------------IYELFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 522 ATSALDNQSEALVQEALERL--MRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEEL 580
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
360-575 |
2.92e-32 |
|
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: 123.76 E-value: 2.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 360 DEVGFRYPDAAEHsvrdFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDlrTYRRFLSVVPQ 439
Cdd:cd03298 4 DKIRFSYGEQPMH----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP--PADRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 440 ESILFEG-SIRENVSYGMD-----GEVPDEKIREALAAANALEFVDRMPQgvetvvgargaRLSGGQKQRLAIARALVRD 513
Cdd:cd03298 78 ENNLFAHlTVEQNVGLGLSpglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 514 PRVLVLDEATSALD----NQSEALVQEAleRLMRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVG 575
Cdd:cd03298 147 KPVLLLDEPFAALDpalrAEMLDLVLDL--HAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
372-571 |
4.32e-32 |
|
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: 123.02 E-value: 4.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDI--AGLDLRTYRRFLSVVPQESILFEG-SI 448
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPHlTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 449 RENVSY------GMDGEVPDEKIREalaaanaleFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEA 522
Cdd:cd03262 94 LENITLapikvkGMSKAEAEERALE---------LLEKV--GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 523 TSALDNQseaLVQEALErLMR-----GRTVFVVAHRLSTIQD-ADRIVVMERGRL 571
Cdd:cd03262 163 TSALDPE---LVGEVLD-VMKdlaeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
83-580 |
8.36e-32 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 131.82 E-value: 8.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 83 VLVVLL--LNYPLHMYFSklsSLAIRRTGTELRGALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQNGLG 160
Cdd:PTZ00243 1005 LGIVLLgtFSVPLRFFLS---YEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQ 1081
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 161 AVMTLLGGLAVIGFQAPVALplfIVVVPLAALLVRsLRGRIRADNEAFR----VEVEQLSARVGEMT----TLIPITRAH 232
Cdd:PTZ00243 1082 CLFSICSSILVTSASQPFVL---VALVPCGYLYYR-LMQFYNSANREIRriksVAKSPVFTLLEEALqgsaTITAYGKAH 1157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 233 ALERTALRRVDSslqrVLTAGFRLDM----LGGRFGSLSWILLNVMAVAFLSGSALVAyyglfgiSPGDVVMIS---TFF 305
Cdd:PTZ00243 1158 LVMQEALRRLDV----VYSCSYLENVanrwLGVRVEFLSNIVVTVIALIGVIGTMLRA-------TSQEIGLVSlslTMA 1226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 306 TGLTASLTALLNLMPIVSRGLESVRSV--------GEVLQAPDLEVNEGKRDAG---EVTGTFT---------------- 358
Cdd:PTZ00243 1227 MQTTATLNWLVRQVATVEADMNSVERLlyytdevpHEDMPELDEEVDALERRTGmaaDVTGTVViepasptsaaphpvqa 1306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 359 ----FDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFL 434
Cdd:PTZ00243 1307 gslvFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 435 SVVPQESILFEGSIRENVSYGMdgEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALV-RD 513
Cdd:PTZ00243 1387 SMIPQDPVLFDGTVRQNVDPFL--EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKG 1464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 514 PRVLVLDEATS----ALDNQSEALVQEALErlmrGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEEL 580
Cdd:PTZ00243 1465 SGFILMDEATAnidpALDRQIQATVMSAFS----AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
372-580 |
1.01e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.61 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVL---N----LVIGFiRpTAGRILLDGEDI--AGLDLRTYRRFLSVVPQESI 442
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLrclNrmndLIPGA-R-VEGEILLDGEDIydPDVDVVELRRRVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 443 LFEGSIRENVSYGM------DGEVPDEKirealaaanalefvdrmpqgVETV---------VGAR----GARLSGGQKQR 503
Cdd:COG1117 103 PFPKSIYDNVAYGLrlhgikSKSELDEI--------------------VEESlrkaalwdeVKDRlkksALGLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 504 LAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAH------RLStiqdaDRIVVMERGRLVEVGTH 577
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELVEFGPT 237
|
...
gi 2764013554 578 EEL 580
Cdd:COG1117 238 EQI 240
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
359-581 |
5.02e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.02 E-value: 5.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 359 FDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVP 438
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 439 QE-SILFEGS-IRENVSYGM-----DGEVPDEKIREALAAANALEFVDRMPQgvetvvgargaRLSGGQKQRLAIARALV 511
Cdd:PRK13632 90 QNpDNQFIGAtVEDDIAFGLenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 512 RDPRVLVLDEATSALDNQSEALVQEALERL--MRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
371-580 |
6.88e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 124.18 E-value: 6.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 371 EHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAglDLRTYRRFLSVVPQESILF-EGSIR 449
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFpHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVSYGMD------GEVPDeKIREALAAANALEFVDRMPQgvetvvgargaRLSGGQKQRLAIARALVRDPRVLVLDEAT 523
Cdd:PRK11607 110 QNIAFGLKqdklpkAEIAS-RVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 524 SALDNQSEALVQ----EALERLmrGRTVFVVAH-RLSTIQDADRIVVMERGRLVEVGTHEEL 580
Cdd:PRK11607 178 GALDKKLRDRMQlevvDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
375-565 |
8.93e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 119.12 E-value: 8.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAgLDLRTYRRFLSVVPQESILFEG-SIRENVS 453
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR-DAREDYRRRLAYLGHADGLKPElTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 454 Y--GMDGEVPDEkirealaaANALEFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSE 531
Cdd:COG4133 98 FwaALYGLRADR--------EAIDEALEAV--GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180 190
....*....|....*....|....*....|....*
gi 2764013554 532 ALVQEALER-LMRGRTVFVVAHRLSTIQDADRIVV 565
Cdd:COG4133 168 ALLAELIAAhLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
273-569 |
9.97e-31 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 126.85 E-value: 9.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 273 VMAVAFLSGSalvayyglfgISPGDVVMISTFFTGLTASLTALLNLMPIVSR---GLESVRSVGEVLQAPDLEVNEGKRD 349
Cdd:COG4178 286 VAAPRYFAGE----------ITLGGLMQAASAFGQVQGALSWFVDNYQSLAEwraTVDRLAGFEEALEAADALPEAASRI 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 350 AGEVTGTFTFDEVGFRYPDAaEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILL-DGEDIAgldlr 428
Cdd:COG4178 356 ETSEDGALALEDLTLRTPDG-RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL----- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 429 tyrrFLsvvPQESILFEGSIRENVSY-GMDGEVPDEKIREALAAANALEFVDRMpqgveTVVGARGARLSGGQKQRLAIA 507
Cdd:COG4178 430 ----FL---PQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFA 497
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 508 RALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERG 569
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
364-575 |
2.10e-30 |
|
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: 118.62 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 364 FRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGlDLRTYRRFLSVVPQESIL 443
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 444 FEG-SIRENVSY-----GMDGEVPDEKIREALAAANALEFVDRmpqgvetvvgaRGARLSGGQKQRLAIARALVRDPRVL 517
Cdd:cd03266 90 YDRlTARENLEYfaglyGLKGDELTARLEELADRLGMEELLDR-----------RVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 518 VLDEATSALDNQSEALVQEALERLMR-GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVG 575
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
359-582 |
2.91e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 120.09 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 359 FDEVGFRYPDAAEhSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD-LRTYRRFLSVV 437
Cdd:PRK13644 4 LENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 PQ--ESILFEGSIRENVSYGMDGE-VPDEKIREAlaaanalefVDRM--PQGVETVVGARGARLSGGQKQRLAIARALVR 512
Cdd:PRK13644 83 FQnpETQFVGRTVEEDLAFGPENLcLPPIEIRKR---------VDRAlaEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 513 DPRVLVLDEATSALDNQSEALVQEALERLMR-GRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
360-575 |
4.78e-30 |
|
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: 117.29 E-value: 4.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 360 DEVGFRYPDaaEHSVRDFSLSVRAGETvALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIaGLDLRTYRRFLSVVPQ 439
Cdd:cd03264 4 ENLTKRYGK--KRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 440 ESILFEG-SIRENVSY-GMDGEVPDEKIREAlaaanalefVDRMPQ--GVETVVGARGARLSGGQKQRLAIARALVRDPR 515
Cdd:cd03264 80 EFGVYPNfTVREFLDYiAWLKGIPSKEVKAR---------VDEVLElvNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 516 VLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVG 575
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
364-582 |
7.81e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.29 E-value: 7.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 364 FRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD---LRTYRRFLSVVPQE 440
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKARRQIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 441 -SILFEGSIRENVSY-----GMDGEVPDEKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDP 514
Cdd:PRK11153 91 fNLLSSRTVFDNVALplelaGTPKAEIKARVTELLELVGLSDKADRYP-----------AQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTI-QDADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGTVSEVFS 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
360-566 |
8.57e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 117.12 E-value: 8.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 360 DEVGFRYPDAAehSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQ 439
Cdd:PRK10247 11 QNVGYLAGDAK--ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 440 ESILFEGSIRENV--SYGMDGEVPDEKIrealaaanaleFVDRMPQ-GV-ETVVGARGARLSGGQKQRLAIARALVRDPR 515
Cdd:PRK10247 89 TPTLFGDTVYDNLifPWQIRNQQPDPAI-----------FLDDLERfALpDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 516 VLVLDEATSALDNQSEALVQEALERLMRGRTVFV--VAHRLSTIQDADRIVVM 566
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHADKVITL 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
374-582 |
1.04e-29 |
|
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: 123.26 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKST----VLNLVigfirPTAGRILLDGEDIAGLD---LRTYRRFLSVVPQE--SILf 444
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDpfGSL- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 445 egSIRENVsygmdGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGAR------LSGGQKQRLAIARALVRDPRVLV 518
Cdd:COG4172 376 --SPRMTV-----GQIIAEGLRVHGPGLSAAERRARVAEALEEVGLDPAARhrypheFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 519 LDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:COG4172 449 LDEPTSALDVSVQAQILDLLRDLQRehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
375-580 |
1.49e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.43 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRF-LSVVPQESILFEG-SIRENV 452
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNlSVAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 -------SYGMdgevpdekIREALAAANALEFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSA 525
Cdd:COG1129 101 flgreprRGGL--------IDWRAMRRRARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 526 LdNQSEAlvqEALERLMR-----GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEEL 580
Cdd:COG1129 171 L-TEREV---ERLFRIIRrlkaqGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
358-580 |
2.52e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.16 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVV 437
Cdd:PRK13648 9 VFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 PQE-SILFEGSI-RENVSYGMDGE-VPDEKIrealaaanalefVDRMPQGVETVVGARGA-----RLSGGQKQRLAIARA 509
Cdd:PRK13648 89 FQNpDNQFVGSIvKYDVAFGLENHaVPYDEM------------HRRVSEALKQVDMLERAdyepnALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 510 LVRDPRVLVLDEATSALDNQSEALVQEALERLMRGR--TVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEEL 580
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
374-581 |
3.65e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.41 E-value: 3.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESIL-FEGSIRENV 452
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 SYGMD--GEVPDEkirealaaanalefVDRMPQGVETVVGARG------ARLSGGQKQRLAIARALVR------DPRVLV 518
Cdd:PRK13548 98 AMGRAphGLSRAE--------------DDALVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARVLAQlwepdgPPRWLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 519 LDEATSALDNQSealvQEALERLMR------GRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:PRK13548 164 LDEPTSALDLAH----QHHVLRLARqlaherGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
359-571 |
3.70e-29 |
|
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: 114.81 E-value: 3.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 359 FDEVGFRYPdAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRT---YRRFLS 435
Cdd:cd03292 3 FINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 436 VVPQES-ILFEGSIRENVSYGMdgEVPDEKIREALaaanalefvDRMPQGVEtVVGARG------ARLSGGQKQRLAIAR 508
Cdd:cd03292 82 VVFQDFrLLPDRNVYENVAFAL--EVTGVPPREIR---------KRVPAALE-LVGLSHkhralpAELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 509 ALVRDPRVLVLDEATSALDNQSEALVQEALERL-MRGRTVFVVAHRLSTIQD-ADRIVVMERGRL 571
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
374-581 |
5.63e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 115.88 E-value: 5.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEG-SIRENV 452
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 SYG----------MDGEvpDEKIrealaaanalefVDR-MPQ-GVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLD 520
Cdd:PRK11231 98 AYGrspwlslwgrLSAE--DNAR------------VNQaMEQtRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 521 EATSALD--NQSEalvqeaLERLMR-----GRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:PRK11231 164 EPTTYLDinHQVE------LMRLMRelntqGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
374-581 |
6.66e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 115.60 E-value: 6.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESIL-FEGSIRENV 452
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLaFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 S-----YGMDGEVPDEKIREALAAANALEFVDRMPQgvetvvgargaRLSGGQKQRLAIARALV-------RDPRVLVLD 520
Cdd:COG4559 97 AlgrapHGSSAAQDRQIVREALALVGLAHLAGRSYQ-----------TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 521 EATSALD--NQSEALvqEALERLMR-GRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:COG4559 166 EPTSALDlaHQHAVL--RLARQLARrGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
361-582 |
9.79e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 115.72 E-value: 9.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 361 EVGFRYPDAAeHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGE--DIAGLDLRTYRRFLSVVP 438
Cdd:PRK13636 10 ELNYNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 439 Q--ESILFEGSIRENVSYG-MDGEVPDEKIREAlaaanalefVDRMPQ--GVETVVGARGARLSGGQKQRLAIARALVRD 513
Cdd:PRK13636 89 QdpDNQLFSASVYQDVSFGaVNLKLPEDEVRKR---------VDNALKrtGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2764013554 514 PRVLVLDEATSALDNQ--SE--ALVQEALERLmrGRTVFVVAHRLSTIQ-DADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMgvSEimKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
360-573 |
1.90e-28 |
|
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: 113.68 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 360 DEVGFRYPDAAE--HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD------LRtyR 431
Cdd:COG4181 12 RGLTKTVGTGAGelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedararLR--A 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 432 RFLSVVPQESILFEG-SIRENVSygmdgeVPDEKIREALAAANALEFVDRMpqGVETVVGARGARLSGGQKQRLAIARAL 510
Cdd:COG4181 90 RHVGFVFQSFQLLPTlTALENVM------LPLELAGRRDARARARALLERV--GLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 511 VRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQDADRIVVMERGRLVE 573
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
376-592 |
4.37e-28 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 113.36 E-value: 4.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD---LRTYRRFLSVVPQESI-------LFE 445
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDSPsavnprmTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 446 GSIRENVSYGMDGEVPDEKIREALAAANA---LEFVDRMPQgvetvvgargaRLSGGQKQRLAIARALVRDPRVLVLDEA 522
Cdd:TIGR02769 109 QIIGEPLRHLTSLDESEQKARIAELLDMVglrSEDADKLPR-----------QLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 523 TSALDNQSEALVQEALERL-MRGRTVFV-VAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLAGTGPYATTLQ 592
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLqQAFGTAYLfITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNLQ 250
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
376-580 |
5.17e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 115.20 E-value: 5.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAglDLRTYRRFLSVVPQESILF-EGSIRENVSY 454
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRDICMVFQSYALFpHMSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 455 G--MDGeVPDEKIRealaaanalefvDRMPQGVETV-VGARGAR----LSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:PRK11432 102 GlkMLG-VPKEERK------------QRVKEALELVdLAGFEDRyvdqISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2764013554 528 NQsealvqeaLERLMR----------GRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEEL 580
Cdd:PRK11432 169 AN--------LRRSMRekirelqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
358-582 |
5.20e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.96 E-value: 5.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRY----PdAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAG----LDLRT 429
Cdd:PRK13634 4 TFQKVEHRYqyktP-FERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 430 YRRFLSVVPQ--ESILFEGSIRENVSYG-MDGEVPDEKIREAlaaanalefVDRMPQGV---ETVVGARGARLSGGQKQR 503
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGpMNFGVSEEDAKQK---------AREMIELVglpEELLARSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 504 LAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEEL 580
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
..
gi 2764013554 581 LA 582
Cdd:PRK13634 234 FA 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
376-580 |
8.59e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 114.80 E-value: 8.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTyrRFLSVVPQESILFEG-SIRENVSY 454
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 455 GM---------DGEVPDEKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDPRVLVLDEATSA 525
Cdd:PRK10851 98 GLtvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 526 LDNQsealVQEALERLMRG-------RTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEEL 580
Cdd:PRK10851 167 LDAQ----VRKELRRWLRQlheelkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
39-332 |
1.30e-27 |
|
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: 112.64 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 39 LTLAVLVFAVKHIPVWLLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRTGTELRGALCH 118
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 119 RMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVALPLFIVVVPLAALLVRSLR 198
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 199 GRIRADNEAFRVEVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILLNVmavaf 278
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL----- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 279 lsGSALVAYYGLFGI-----SPGDVVMISTFFTGLTASLTALLNLMPIVSRGLESVRSV 332
Cdd:cd07346 236 --GTALVLLYGGYLVlqgslTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
362-592 |
3.83e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 110.93 E-value: 3.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 362 VGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD---LRTYRRFLSVVP 438
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 439 QESIlfeGSI--RENVsygmdGEVPDEKIR--EALAAANALEFVDRMPQGVE---TVVGARGARLSGGQKQRLAIARALV 511
Cdd:PRK10419 96 QDSI---SAVnpRKTV-----REIIREPLRhlLSLDKAERLARASEMLRAVDlddSVLDKRPPQLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 512 RDPRVLVLDEATSALDNQSEALVQEALERLM-RGRTVFV-VAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLAGTGPYA 588
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQqQFGTACLfITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLTFSSPAG 247
|
....
gi 2764013554 589 TTLQ 592
Cdd:PRK10419 248 RVLQ 251
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
356-574 |
4.28e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 110.34 E-value: 4.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 356 TFTFDEVGFRYP--DAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTyrrf 433
Cdd:COG4525 3 MLTVRHVSVRYPggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 434 lSVVPQESILFEG-SIRENVSYG--MDGEVPDEKIREalaaanalefVDRMPQ--GVETVVGARGARLSGGQKQRLAIAR 508
Cdd:COG4525 79 -GVVFQKDALLPWlNVLDNVAFGlrLRGVPKAERRAR----------AEELLAlvGLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2764013554 509 ALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHrlsTIQDA----DRIVVMER--GRLVEV 574
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITH---SVEEAlflaTRLVVMSPgpGRIVER 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
374-575 |
4.60e-27 |
|
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: 108.41 E-value: 4.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTA--GRILLDGEDiagLDLRTYRRFLSVVPQESILFEG-SIRE 450
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRP---LDKRSFRKIIGYVPQDDILHPTlTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 451 NVSYgmdgevpdekirealaaanalefvdrmpqgvetVVGARGarLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQS 530
Cdd:cd03213 102 TLMF---------------------------------AAKLRG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2764013554 531 EALVQEALERLMR-GRTVFVVAHRLST--IQDADRIVVMERGRLVEVG 575
Cdd:cd03213 147 ALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
376-579 |
2.33e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.98 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIA--GLDLRTYRRFLSVVPQ--ESILFEGSIREN 451
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQypEYQLFEETIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 452 VSYGM------DGEVPDEKIREALAA-ANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDPRVLVLDEATS 524
Cdd:PRK13637 105 IAFGPinlglsEEEIENRVKRAMNIVgLDYEDYKDKSP-----------FELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 525 ALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEE 579
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
374-521 |
4.68e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 107.04 E-value: 4.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLrtYRRF---LSVVPQESILFEG-SIR 449
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPM--HKRArlgIGYLPQEASIFRKlTVE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 450 ENVSYGMDGEVPDEKIREALAAANALEFvdrmpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDE 521
Cdd:COG1137 97 DNILAVLELRKLSKKEREERLEELLEEF------GITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
354-582 |
6.03e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 108.35 E-value: 6.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 354 TGTFTFDEVGFRYPDAAehSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGlDLRTYRRF 433
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 434 LSVVPQ-ESILFEGSIRENVS-YGMDGEVPDEKIREALAAANALEfvdRMPQGVETVVGArgarLSGGQKQRLAIARALV 511
Cdd:PRK13537 82 VGVVPQfDNLDPDFTVRENLLvFGRYFGLSAAAARALVPPLLEFA---KLENKADAKVGE----LSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 512 RDPRVLVLDEATSALDNQSEALVQEALERLM-RGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
374-580 |
7.02e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 107.89 E-value: 7.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDiagLDLRTYRRF--LsvvPQESILFEG-SIRE 450
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---LDPEDRRRIgyL---PEERGLYPKmKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 451 NVSY-----GMDGEVPDEKIRealaaanalEFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSA 525
Cdd:COG4152 91 QLVYlarlkGLSKAEAKRRAD---------EWLERL--GLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 526 LD--NQsEALVQEALERLMRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEEL 580
Cdd:COG4152 160 LDpvNV-ELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
358-584 |
8.38e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.19 E-value: 8.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTA---GRILLDGEDIAGLDLRTYRRFL 434
Cdd:PRK13640 7 EFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 435 SVVPQ--ESILFEGSIRENVSYGMDG-EVPDEK----IREALAAANALEFVDRMPQgvetvvgargaRLSGGQKQRLAIA 507
Cdd:PRK13640 87 GIVFQnpDNQFVGATVGDDVAFGLENrAVPRPEmikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 508 RALVRDPRVLVLDEATSALDNQSEALVQEALERLM--RGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGT 584
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
372-575 |
8.68e-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: 105.38 E-value: 8.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIaGLDLRTYRRFLSVVPQESILFEGSIREN 451
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIEAPGFYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 452 VSYGMDG-EVPDEKIrealaaanalefvdrmpQGVETVVGARGAR------LSGGQKQRLAIARALVRDPRVLVLDEATS 524
Cdd:cd03268 93 LRLLARLlGIRKKRI-----------------DEVLDVVGLKDSAkkkvkgFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 525 ALDNQSEALVQEALERLMR-GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVG 575
Cdd:cd03268 156 GLDPDGIKELRELILSLRDqGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
107-580 |
9.14e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 113.15 E-value: 9.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 107 RTGTELRGALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQ--NGL-GAVMTLLGGLAVIGFQAPVA---- 179
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEqlHGLwSAPFRIIVSMVLLYQQLGVAslfg 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 180 -LPLFIVVvPLAALLVRSLRgriRADNEAfrveVEQLSARVG---EMTTLIPITRAHALERTALRRVDSSLQRVLTAgFR 255
Cdd:PLN03232 447 sLILFLLI-PLQTLIVRKMR---KLTKEG----LQWTDKRVGiinEILASMDTVKCYAWEKSFESRIQGIRNEELSW-FR 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 256 LDMLGGRFGSLswiLLNVMAVAflsgsALVAYYGLFGISPGDVVMISTF-----FTGLTASLTALLNLMPIVSRGLESVR 330
Cdd:PLN03232 518 KAQLLSAFNSF---ILNSIPVV-----VTLVSFGVFVLLGGDLTPARAFtslslFAVLRSPLNMLPNLLSQVVNANVSLQ 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 331 SVGEVLQ------APDLEVNEGKRDAGEVTGTFTFDEvgfrypDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLV 404
Cdd:PLN03232 590 RIEELLLseerilAQNPPLQPGAPAISIKNGYFSWDS------KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 405 IGFIRPTagrilldgeDIAGLDLRTYrrfLSVVPQESILFEGSIRENVSYGMDGEvpDEKIREALAAANALEFVDRMPQG 484
Cdd:PLN03232 664 LGELSHA---------ETSSVVIRGS---VAYVPQVSWIFNATVRENILFGSDFE--SERYWRAIDVTALQHDLDLLPGR 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 485 VETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQ-SEALVQEALERLMRGRTVFVVAHRLSTIQDADRI 563
Cdd:PLN03232 730 DLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRI 809
|
490
....*....|....*..
gi 2764013554 564 VVMERGRLVEVGTHEEL 580
Cdd:PLN03232 810 ILVSEGMIKEEGTFAEL 826
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
362-582 |
1.73e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 106.35 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 362 VGFRY-PDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQ- 439
Cdd:PRK13650 10 LTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 440 -ESILFEGSIRENVSYGMDGE-VP----DEKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRD 513
Cdd:PRK13650 90 pDNQFVGATVEDDVAFGLENKgIPheemKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 514 PRVLVLDEATSALDNQSE-ALVQEALE-RLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRlELIKTIKGiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
375-572 |
2.63e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 105.55 E-value: 2.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGldLRTYRR--FLSVVPQESILfeG-----S 447
Cdd:COG1101 23 DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK--LPEYKRakYIGRVFQDPMM--GtapsmT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 448 IRENVS--------YGmdgevpdekIREALAAANALEFVDR---MPQGVE----TVVGArgarLSGGQKQRLAIARALVR 512
Cdd:COG1101 99 IEENLAlayrrgkrRG---------LRRGLTKKRRELFRELlatLGLGLEnrldTKVGL----LSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 513 DPRVLVLDEATSALDNQSEALVQEALERLMRGR--TVFVVAHRLstiQDA----DRIVVMERGRLV 572
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNM---EQAldygNRLIMMHEGRII 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
374-581 |
3.88e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 106.84 E-value: 3.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGlDLRTYRRFLSVVPQ-ESILFEGSIRENV 452
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQfDNLDLEFTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 -----SYGMdgevpdeKIREALAAANALEFVDRMpqgvETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:PRK13536 136 lvfgrYFGM-------STREIEAVIPSLLEFARL----ESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 528 NQSEALVQEALERLM-RGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELL 581
Cdd:PRK13536 205 PHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
373-571 |
8.26e-25 |
|
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: 101.74 E-value: 8.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 373 SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRF-LSVVP----QESILFEGS 447
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPedrkREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 448 IRENVSYGmdgevpdekirealaaanalefvdrmpqgvetvvgargARLSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:cd03215 95 VAENIALS--------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2764013554 528 NQSEALVQEALERL-MRGRTVFVVAHRLSTIQD-ADRIVVMERGRL 571
Cdd:cd03215 137 VGAKAEIYRLIRELaDAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
374-581 |
9.34e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 106.66 E-value: 9.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGL---DLRTYRR--FLSVVPQESILFEGSI 448
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaELREVRRkkIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 449 RENVSYGMD-GEVPDEKIREALaaanalefVDRMPQ-GVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSAL 526
Cdd:PRK10070 124 LDNTAFGMElAGINAEERREKA--------LDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 527 DNQSEALVQEALERLM--RGRTVFVVAHRL-STIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:PRK10070 196 DPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
375-578 |
1.32e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.42 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIagldlrtyrRFLSvvPQESI------------ 442
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV---------RIRS--PRDAIalgigmvhqhfm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 443 LFEG-SIRENVSYGMDGeVPDEKIREALAAANALEFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDE 521
Cdd:COG3845 91 LVPNlTVAENIVLGLEP-TKGGRLDRKAARARIRELSERY--GLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 522 ATSALDNQsEAlvqEALERLMR-----GRTVFVVAHRLSTIQD-ADRIVVMERGRLveVGTHE 578
Cdd:COG3845 168 PTAVLTPQ-EA---DELFEILRrlaaeGKSIIFITHKLREVMAiADRVTVLRRGKV--VGTVD 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
374-581 |
1.42e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.08 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQE-SILFEGSIRENV 452
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDtSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 SYG---------MDGEVPDEKIREALAAANALEFVDRmpqGVETvvgargarLSGGQKQRLAIARALVRDPRVLVLDEAT 523
Cdd:PRK09536 99 EMGrtphrsrfdTWTETDRAAVERAMERTGVAQFADR---PVTS--------LSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 524 SALDNQSEALVQEALERLMR-GRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:PRK09536 168 ASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
374-575 |
1.87e-24 |
|
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: 102.16 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIA--GLDLrtyrrfLSVVPQESILFEGSIREN 451
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepGPDR------MVVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 452 VSYGMDGEVPDekireaLAAANALEFVDRMPQ--GVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDnq 529
Cdd:TIGR01184 75 IALAVDRVLPD------LSKSERRAIVEEHIAlvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD-- 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 530 seALVQEAL-ERLMR-----GRTVFVVAHRL-STIQDADRIVVMERGRLVEVG 575
Cdd:TIGR01184 147 --ALTRGNLqEELMQiweehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
376-581 |
1.91e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.48 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAG--LDLRTYRRFLSVVPQESILF-EGSIRENV 452
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAGMVFQQFYLFpHLTALENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 SYGmdgevPdEKIREALAAANALEFVDRMPQ-GVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQse 531
Cdd:PRK09493 99 MFG-----P-LRVRGASKEEAEKQARELLAKvGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE-- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 532 aLVQEALeRLMR-----GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELL 581
Cdd:PRK09493 171 -LRHEVL-KVMQdlaeeGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
362-582 |
2.07e-24 |
|
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: 107.08 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 362 VGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKS----TVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRF---- 433
Cdd:COG4172 14 VAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgnr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 434 LSVVPQE---------SIlfEGSIRENVS--YGMDGE--------------VPDEKIRealaaanalefVDRMPQgvetv 488
Cdd:COG4172 94 IAMIFQEpmtslnplhTI--GKQIAEVLRlhRGLSGAaararalellervgIPDPERR-----------LDAYPH----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 489 vgargaRLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVV 565
Cdd:COG4172 156 ------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRelGMALLLITHDLGVVRRfADRVAV 229
|
250
....*....|....*..
gi 2764013554 566 MERGRLVEVGTHEELLA 582
Cdd:COG4172 230 MRQGEIVEQGPTAELFA 246
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
372-575 |
4.71e-24 |
|
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: 100.68 E-value: 4.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLrtyrrflsvvpqeSILFEGSI--R 449
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL-------------GGGFNPELtgR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVS-----YGMDGEVPDEKIREALAAANALEFVDrMPqgVETvvgargarLSGGQKQRLAIARALVRDPRVLVLDEATS 524
Cdd:cd03220 103 ENIYlngrlLGLSRKEIDEKIDEIIEFSELGDFID-LP--VKT--------YSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 525 ALDNQSEALVQEAL-ERLMRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVG 575
Cdd:cd03220 172 VGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
373-591 |
4.96e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 103.25 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 373 SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD---LRTYRRFLSVVPQESIlfeGSI- 448
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDPL---ASLn 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 449 -RENVsygmdGEVPDEKIREalaaanaleFVDRMP-QGVETVVGARGARL--------------SGGQKQRLAIARALVR 512
Cdd:PRK15079 113 pRMTI-----GEIIAEPLRT---------YHPKLSrQEVKDRVKAMMLKVgllpnlinryphefSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 513 DPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLAGTG-PYA 588
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLhPYT 258
|
...
gi 2764013554 589 TTL 591
Cdd:PRK15079 259 KAL 261
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
372-582 |
8.92e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 100.54 E-value: 8.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTyrrflSVVPQ----ESILFEGS 447
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLELGA-----GFHPEltgrENIYLNGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 448 IrenvsYGMDGEVPDEKIREALAAANALEFVDrMPqgvetvVGargaRLSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:COG1134 115 L-----LGLSRKEIDEKFDEIVEFAELGDFID-QP------VK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 528 nqsEALVQEALERLM----RGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:COG1134 179 ---AAFQKKCLARIRelreSGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
374-570 |
1.02e-23 |
|
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: 99.82 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGE----DIAGLDLRT---YRR--------FLSVVP 438
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPREilaLRRrtigyvsqFLRVIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 439 QESIL--FEGSIRENvsyGMDGEVPDEKIREAlaaanalefVDRM--PQgvetvvgargaRL--------SGGQKQRLAI 506
Cdd:COG4778 107 RVSALdvVAEPLLER---GVDREEARARAREL---------LARLnlPE-----------RLwdlppatfSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 507 ARALVRDPRVLVLDEATSALDNQSEALVQEALERLM-RGRTVFVVAHRLSTI-QDADRIVVMERGR 570
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKaRGTAIIGIFHDEEVReAVADRVVDVTPFS 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
332-580 |
1.03e-23 |
|
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: 101.47 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 332 VGEVLQAPDLEVNEGKRDAGEVTGTFTfdevgfRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPT 411
Cdd:cd03291 17 FGELLEKAKQENNDRKHSSDDNNLFFS------NLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 412 AGRILLDGEdiagldlrtyrrfLSVVPQESILFEGSIRENVSYGMDgevPDE-KIREALAAANALEFVDRMPQGVETVVG 490
Cdd:cd03291 91 EGKIKHSGR-------------ISFSSQFSWIMPGTIKENIIFGVS---YDEyRYKSVVKACQLEEDITKFPEKDNTVLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 491 ARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEA-LERLMRGRTVFVVAHRLSTIQDADRIVVMERG 569
Cdd:cd03291 155 EGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
250
....*....|.
gi 2764013554 570 RLVEVGTHEEL 580
Cdd:cd03291 235 SSYFYGTFSEL 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
374-575 |
1.06e-23 |
|
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: 99.28 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEdiaGLDLRTYRRFlSVVPQESILFEG-SIRENV 452
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK---PLDIAARNRI-GYLPEERGLYPKmKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 SY--GMDGEVPDEKIREALAAANALEFVDRMPQGVETvvgargarLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQS 530
Cdd:cd03269 92 VYlaQLKGLKKEEARRRIDEWLERLELSEYANKRVEE--------LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2764013554 531 EALVQEALERLMR-GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVG 575
Cdd:cd03269 164 VELLKDVIRELARaGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
373-569 |
1.14e-23 |
|
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: 99.33 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 373 SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRI-----LLDGEDIAGLDLRTyRRFLSVVPQESILFEGS 447
Cdd:cd03290 16 TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRN-RYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 448 IRENVSYGmdGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:cd03290 95 VEENITFG--SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2764013554 528 -NQSEALVQEALERLMRG--RTVFVVAHRLSTIQDADRIVVMERG 569
Cdd:cd03290 173 iHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
374-568 |
1.22e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.09 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRP---TAGRILLDGEDIAGLDlrTYRRFLSVVPQESILFEG-SIR 449
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALP--AEQRRIGILFQDDLLFPHlSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVSYGMDGEVP----DEKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDPRVLVLDEATSA 525
Cdd:COG4136 95 ENLAFALPPTIGraqrRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2764013554 526 LD----NQSEALVQEALERlmRGRTVFVVAHRLSTIQDADRIVVMER 568
Cdd:COG4136 164 LDaalrAQFREFVFEQIRQ--RGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
356-582 |
1.24e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.01 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 356 TFTFDEVGFRYPDAA--EH-SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD----LR 428
Cdd:PRK13646 2 TIRFDNVSYTYQKGTpyEHqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 429 TYRRFLSVVPQ--ESILFEGSIRENVSYG-----MD-GEVPDEKIREAlaaanalefvdrMPQGVE-TVVGARGARLSGG 499
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpknfkMNlDEVKNYAHRLL------------MDLGFSrDVMSQSPFQMSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 500 QKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLM--RGRTVFVVAHRLSTI-QDADRIVVMERGRLVEVGT 576
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTS 229
|
....*.
gi 2764013554 577 HEELLA 582
Cdd:PRK13646 230 PKELFK 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
364-582 |
2.46e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.15 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 364 FRYPDAAEhSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIA--GLDLRTYRRFLSVVPQ-- 439
Cdd:PRK13639 9 YSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVGIVFQnp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 440 ESILFEGSIRENVSYG-----MDGEVPDEKIREALAAANALEFVDRMPQgvetvvgargaRLSGGQKQRLAIARALVRDP 514
Cdd:PRK13639 88 DDQLFAPTVEEDVAFGplnlgLSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEALERLMR-GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
355-581 |
2.82e-23 |
|
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: 99.93 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 355 GTFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRpTAGRILLDGEDIAGLDLRTYRRFL 434
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 435 SVVPQESILFEGSIRENVSygMDGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDP 514
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLD--PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
374-580 |
2.84e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.29 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD---------LRTY---RRFLSVVPQES 441
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghqiarmgvVRTFqhvRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 442 ILF--EGSIRENVSYGMdGEVPDEKIREALAAANALEFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVL 519
Cdd:PRK11300 101 LLVaqHQQLKTGLFSGL-LKTPAFRRAESEALDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2764013554 520 DEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEEL 580
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
387-580 |
4.28e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.49 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 387 VALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQES--ILFEGSIRENVSY-----GMDGE 459
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQDIAFgpinlGLDEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 460 VPDEKIREALAAANALEFVDRMPQgvetvvgargaRLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALE 539
Cdd:PRK13652 113 TVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2764013554 540 RLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEEL 580
Cdd:PRK13652 182 DLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
374-581 |
4.73e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 98.62 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAG---RIL---LDGEDIAglDLRTYRRFLSVVPQESILFEGS 447
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVW--ELRKRIGLVSPALQLRFPRDET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 448 IRENV------SYGMDGEVPDEKIREALAAanalefVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDE 521
Cdd:COG1119 97 VLDVVlsgffdSIGLYREPTDEQRERAREL------LELL--GLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 522 ATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQDA-DRIVVMERGRLVEVGTHEELL 581
Cdd:COG1119 169 PTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
376-578 |
5.03e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.16 E-value: 5.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAGETVALVGGSGAGKST---VLNLVIGfirPTAGRIlldgeDIAGL-----------DLRTYRRFLSVVPQES 441
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSllrVLNLLEM---PRSGTL-----NIAGNhfdfsktpsdkAIRELRRNVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 442 ILFEG-SIRENVS------YGMDGEVPDEKIREALAAANALEFVDRMPQgvetvvgargaRLSGGQKQRLAIARALVRDP 514
Cdd:PRK11124 92 NLWPHlTVQQNLIeapcrvLGLSKDQALARAEKLLERLRLKPYADRFPL-----------HLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEALERLMR-GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHE 578
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
57-595 |
5.28e-23 |
|
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: 104.26 E-value: 5.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 57 PLVTARIIDIVVDhkPVSALWWN--------TAAVLVVLLLNYPLHMYFskLSSLAIRrtgTELRGALCHRMqhLSIGYH 128
Cdd:TIGR00957 337 PQILSLLIRFVND--PMAPDWQGyfytgllfVCACLQTLILHQYFHICF--VSGMRIK---TAVMGAVYRKA--LVITNS 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 129 SRVSAEVLQTKVVRDVDA-----LETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVALPLFIVVVPLAALLVRSLRgrira 203
Cdd:TIGR00957 408 ARKSSTVGEIVNLMSVDAqrfmdLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTK----- 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 204 dneAFRV-EVEQLSARVGEMTTL---IPITRAHALERTALRRVDSSLQRVLTAgFRLDMLGGRFGSLSWillnvMAVAFL 279
Cdd:TIGR00957 483 ---TYQVaHMKSKDNRIKLMNEIlngIKVLKLYAWELAFLDKVEGIRQEELKV-LKKSAYLHAVGTFTW-----VCTPFL 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 280 SgsALVAYYGLFGISPGDVVMISTFFTGLTAS--LTALLNLMPIVSRGLE----SVRSVGEVLQAPDLEVNEGKRDAGEV 353
Cdd:TIGR00957 554 V--ALITFAVYVTVDENNILDAEKAFVSLALFniLRFPLNILPMVISSIVqasvSLKRLRIFLSHEELEPDSIERRTIKP 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 354 TG--TFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEdiagldlrtyr 431
Cdd:TIGR00957 632 GEgnSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------- 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 432 rfLSVVPQESILFEGSIRENVSYGMDGEVPdeKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALV 511
Cdd:TIGR00957 701 --VAYVPQQAWIQNDSLRENILFGKALNEK--YYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVY 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 512 RDPRVLVLDEATSALDNQSEALVQEAL---ERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGPYA 588
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFA 856
|
....*..
gi 2764013554 589 TTLQPRA 595
Cdd:TIGR00957 857 EFLRTYA 863
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
355-582 |
2.53e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 102.12 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 355 GTFTFDevgfryPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILldgediagldlrTYRRFL 434
Cdd:PLN03130 620 GYFSWD------SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASV------------VIRGTV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 435 SVVPQESILFEGSIRENVSYGMDGEvpDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDP 514
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSPFD--PERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 515 RVLVLDEATSALDNQ-SEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLA 582
Cdd:PLN03130 760 DVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
139-581 |
2.91e-22 |
|
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: 101.91 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 139 KVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPValpLFIVVVPLAALLVRSLRGRIRADNEAFRVEVEqlsAR 218
Cdd:TIGR01271 987 RFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPY---IFIAAIPVAVIFIMLRAYFLRTSQQLKQLESE---AR 1060
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 219 VGEMTTLIPITRAHALERTALRR--VDSSLQRVL---TAGFRLDMlggrfGSLSWILL--NVMAVAFLSGSALVAYyGLF 291
Cdd:TIGR01271 1061 SPIFSHLITSLKGLWTIRAFGRQsyFETLFHKALnlhTANWFLYL-----STLRWFQMriDIIFVFFFIAVTFIAI-GTN 1134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 292 GISPGDVVMISTFFTGLTASLTALLNlMPIVSRGLesVRSVGEVLQAPDLEVNEGK---------------------RDA 350
Cdd:TIGR01271 1135 QDGEGEVGIILTLAMNILSTLQWAVN-SSIDVDGL--MRSVSRVFKFIDLPQEEPRpsggggkyqlstvlvienphaQKC 1211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 351 GEVTGTFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRpTAGRILLDGEDIAGLDLRTY 430
Cdd:TIGR01271 1212 WPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTW 1290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 431 RRFLSVVPQESILFEGSIRENVSygMDGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARAL 510
Cdd:TIGR01271 1291 RKAFGVIPQKVFIFSGTFRKNLD--PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSI 1368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 511 VRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
364-581 |
2.92e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 96.73 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 364 FRYPDAAeHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQE--S 441
Cdd:PRK13647 12 FRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpdD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 442 ILFEGSIRENVSYG-----MDGEVPDEKIREALAAANALEFVDRMPQgvetvvgargaRLSGGQKQRLAIARALVRDPRV 516
Cdd:PRK13647 91 QVFSSTVWDDVAFGpvnmgLDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 517 LVLDEATSALDNQSEALVQEALERL-MRGRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
364-582 |
5.05e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.32 E-value: 5.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 364 FRYPDAAE-HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQ--E 440
Cdd:PRK13642 12 FKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQnpD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 441 SILFEGSIRENVSYGMDGE-VPDE----KIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDPR 515
Cdd:PRK13642 92 NQFVGATVEDDVAFGMENQgIPREemikRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 516 VLVLDEATSALDNQSEALVQEALERLMRGR--TVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
376-575 |
5.59e-22 |
|
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: 94.65 E-value: 5.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRP---TAGRILLDGEDiagLDLRTYRRFLSVVPQESILFEG-SIREN 451
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQP---RKPDQFQKCVAYVRQDDILLPGlTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 452 VSYGMDGEVP---DEKIREALAAanalefVDRMPQGVETVVGARGAR-LSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:cd03234 102 LTYTAILRLPrksSDAIRKKRVE------DVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 528 NQSEALVQEALERLM-RGRTVFVVAH--RLSTIQDADRIVVMERGRLVEVG 575
Cdd:cd03234 176 SFTALNLVSTLSQLArRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
372-582 |
7.03e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 95.67 E-value: 7.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQES---------- 441
Cdd:COG4167 27 EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDPntslnprlni 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 442 --ILfEGSIRENVSygMDGEVPDEKIrealaaanalefvdrmpqgVETV--VGARGAR-------LSGGQKQRLAIARAL 510
Cdd:COG4167 107 gqIL-EEPLRLNTD--LTAEEREERI-------------------FATLrlVGLLPEHanfyphmLSSGQKQRVALARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 511 VRDPRVLVLDEATSALD----NQSEALVQEALERLmrGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:COG4167 165 ILQPKIIIADEALAALDmsvrSQIINLMLELQEKL--GISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
379-582 |
9.54e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 94.82 E-value: 9.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 379 LSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD--------LRTYRRFLSVVPQESILF-EGSIR 449
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkglIRQLRQHVGFVFQNFNLFpHRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVsygMDGEVPDEKIREALAAANALEFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQ 529
Cdd:PRK11264 104 ENI---IEGPVIVKGEPKEEATARARELLAKV--GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 530 seaLVQEALERLmRG-----RTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK11264 179 ---LVGEVLNTI-RQlaqekRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
374-581 |
1.04e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.76 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQE----SILfegSIR 449
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQEnhinSRL---TVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVSYGM-----------DGEVPDEKIREALAAANALEFVDrmpqgvetvvgargaRLSGGQKQRLAIARALVRDPRVLV 518
Cdd:COG4604 94 ELVAFGRfpyskgrltaeDREIIDEAIAYLDLEDLADRYLD---------------ELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 519 LDEATSALD-NQSEALVQeALERLMR--GRTVFVVAHrlstiqD-------ADRIVVMERGRLVEVGTHEELL 581
Cdd:COG4604 159 LDEPLNNLDmKHSVQMMK-LLRRLADelGKTVVIVLH------DinfascyADHIVAMKDGRVVAQGTPEEII 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
359-581 |
1.26e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.57 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 359 FDEVGFRY-PDA--AEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGL----DLRTYR 431
Cdd:PRK13643 4 FEKVNYTYqPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkEIKPVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 432 RFLSVVPQ--ESILFEGSIRENVSYGMD----GEVPDEKI--REALAAANALEFVDRMPqgvetvvgargARLSGGQKQR 503
Cdd:PRK13643 84 KKVGVVFQfpESQLFEETVLKDVAFGPQnfgiPKEKAEKIaaEKLEMVGLADEFWEKSP-----------FELSGGQMRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 504 LAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR-GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELL 581
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
360-580 |
1.61e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 94.77 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 360 DEVGFRYPDAAEH----SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGL-DLRTYRRFL 434
Cdd:PRK13633 8 KNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 435 SVVPQ--ESILFEGSIRENVSYGMDG-EVPDEKIREAlaaanalefVDRMPQGVETVVGARGA--RLSGGQKQRLAIARA 509
Cdd:PRK13633 88 GMVFQnpDNQIVATIVEEDVAFGPENlGIPPEEIRER---------VDESLKKVGMYEYRRHAphLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 510 LVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEEL 580
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
334-580 |
1.68e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.07 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 334 EVLQAPDLEVNEGKRDAgevtgtftfdevgfrypdaaehsVRDFSLSVRAGETVALVGGSGAGKSTVLNLV--IGFIRP- 410
Cdd:PRK14239 4 PILQVSDLSVYYNKKKA-----------------------LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPe 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 411 --TAGRILLDGEDIAG--LDLRTYRRFLSVVPQESILFEGSIRENVSYGM------DGEVPDEKIREALAAANALEFV-D 479
Cdd:PRK14239 61 vtITGSIVYNGHNIYSprTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLrlkgikDKQVLDEAVEKSLKGASIWDEVkD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 480 RMPqgvETVVGargarLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRL---ST 556
Cdd:PRK14239 141 RLH---DSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSR 212
|
250 260
....*....|....*....|....
gi 2764013554 557 IqdADRIVVMERGRLVEVGTHEEL 580
Cdd:PRK14239 213 I--SDRTGFFLDGDLIEYNDTKQM 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
374-566 |
1.74e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.30 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILldgediagldlRTYRRFLSVVPQESIL---FEGSIRE 450
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR-----------RAGGARVAYVPQRSEVpdsLPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 451 NVSYGMDGEVPDEKIREALAAANALEFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQS 530
Cdd:NF040873 77 LVAMGRWARRGLWRRLTRDDRAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 2764013554 531 EALVQEALERLM-RGRTVFVVAHRLSTIQDADRIVVM 566
Cdd:NF040873 155 RERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
356-584 |
2.07e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.08 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 356 TFTFDEVGFRYPDAAehSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLS 435
Cdd:PRK10575 11 TFALRNVSFRVPGRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 436 VVPQESILFEG-SIRENVSYGM-------------DGEVPDEKIREALAAANALEFVDRmpqgvetvvgargarLSGGQK 501
Cdd:PRK10575 89 YLPQQLPAAEGmTVRELVAIGRypwhgalgrfgaaDREKVEEAISLVGLKPLAHRLVDS---------------LSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 502 QRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERL--MRGRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHE 578
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsqERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPA 233
|
....*.
gi 2764013554 579 ELLAGT 584
Cdd:PRK10575 234 ELMRGE 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
339-582 |
2.09e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 339 PDLEVNEGKRDAGEVtgtFTFDEVGFRYPDaaEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRIlld 418
Cdd:COG0488 301 VEIRFPPPERLGKKV---LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 419 gedIAGLDLRtyrrfLSVVPQESILFEG--SIRENVSYGMDGEvPDEKIRealaaanalEFVDRM---PQGVETVVGArg 493
Cdd:COG0488 373 ---KLGETVK-----IGYFDQHQEELDPdkTVLDELRDGAPGG-TEQEVR---------GYLGRFlfsGDDAFKPVGV-- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 494 arLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLmRGrTVFVVAH-R--LSTIqdADRIVVMERGR 570
Cdd:COG0488 433 --LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHdRyfLDRV--ATRILEFEDGG 506
|
250
....*....|...
gi 2764013554 571 LVE-VGTHEELLA 582
Cdd:COG0488 507 VREyPGGYDDYLE 519
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
373-582 |
2.58e-21 |
|
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: 97.57 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 373 SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRI-LLDGEDIA-----GLDLR-TYRRFLSVVPQESILF- 444
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVdmtkpGPDGRgRAKRYIGILHQEYDLYp 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 445 EGSIRENVSYGMDGEVPDE-KIREALAAANALEFVDRMpqgVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEAT 523
Cdd:TIGR03269 379 HRTVLDNLTEAIGLELPDElARMKAVITLKMVGFDEEK---AEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 524 SALDNQSEALVQEAL--ERLMRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:TIGR03269 456 GTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
376-582 |
3.15e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.13 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDI----AGLDLRTYRRFLSVVPQ--ESILFEGSIR 449
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSLVFQfpEAQLFENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVSYG-MDGEVPDEKIREALAAANALEFVDrmpqgvETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDN 528
Cdd:PRK13641 105 KDVEFGpKNFGFSEDEAKEKALKWLKKVGLS------EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 529 QS-EALVQEALERLMRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK13641 179 EGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFS 234
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
375-580 |
3.25e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.48 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAglDLRTYRRFLSVVPQESILFEG-SIRENVS 453
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVGMVFQSYALYPHlSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 454 YGM-----DGEVPDEKIREALAAANALEFVDRMPQGvetvvgargarLSGGQKQRLAIARALVRDPRVLVLDEATSALDn 528
Cdd:PRK11000 98 FGLklagaKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 529 qsEAL-VQEALE--RLMR--GRTVFVVAH-RLSTIQDADRIVVMERGRLVEVGTHEEL 580
Cdd:PRK11000 166 --AALrVQMRIEisRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
363-582 |
3.84e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 94.65 E-value: 3.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 363 GFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD---LRTYRRFLSVVPQ 439
Cdd:PRK11308 20 GLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 440 ------------ESILFEgSIRENVSygMDGEVPDEKIREALAAA-NALEFVDRMPQgvetvvgargaRLSGGQKQRLAI 506
Cdd:PRK11308 100 npygslnprkkvGQILEE-PLLINTS--LSAAERREKALAMMAKVgLRPEHYDRYPH-----------MFSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 507 ARALVRDPRVLVLDEATSALDNQSEALVQEA---LERLMRGRTVFvVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQAQVLNLmmdLQQELGLSYVF-ISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
374-582 |
4.40e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 92.65 E-value: 4.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTY-RRFLSVVPQESILFEG-SIREN 451
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARaRRGIGYLPQEASIFRRlSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 452 VSYGMdgevpdeKIREALAAANALEFVDRMPQ--GVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQ 529
Cdd:PRK10895 99 LMAVL-------QIRDDLSAEQREDRANELMEefHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 530 SEALVQEALERLM-RGRTVFVVAHRL-STIQDADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK10895 172 SVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
376-578 |
4.96e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.38 E-value: 4.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAGETVALVGGSGAGKST---VLNLVIgfiRPTAGRILLDGE------DIAGLDLRTYRRFLSVVPQESILFEG 446
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSllrVLNLLE---TPDSGQLNIAGHqfdfsqKPSEKAIRLLRQKVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 447 -SIRENVS------YGMDGEVPDEKIREALAAANALEFVDRMPQgvetvvgargaRLSGGQKQRLAIARALVRDPRVLVL 519
Cdd:COG4161 97 lTVMENLIeapckvLGLSKEQAREKAMKLLARLRLTDKADRFPL-----------HLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 520 DEATSALDNQSEALVQEALERLMR-GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHE 578
Cdd:COG4161 166 DEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
366-572 |
4.99e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.49 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 366 YPdAAEHSV---RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD---LRTYRR--FLSVV 437
Cdd:PRK10535 14 YP-SGEEQVevlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLAQLRRehFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 PQESILFEGSIRENVsygmdgEVPD--EKIREALAAANALEFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDPR 515
Cdd:PRK10535 93 QRYHLLSHLTAAQNV------EVPAvyAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 516 VLVLDEATSALDNQSEALVQEALERLM-RGRTVFVVAHRLSTIQDADRIVVMERGRLV 572
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
375-571 |
5.19e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 92.82 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFlsvvpQESILFE-GSIRENVS 453
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMF-----QDARLLPwKKVIDNVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 454 YGMDGEVPDEKIREALAAanalefvdrmpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEAL 533
Cdd:PRK11247 104 LGLKGQWRDAALQALAAV------------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2764013554 534 VQEALERLMR--GRTVFVVAHRLS-TIQDADRIVVMERGRL 571
Cdd:PRK11247 172 MQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
376-590 |
7.96e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 93.76 E-value: 7.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRI----LLDGEDIAGLDLRTY------------RRFLSVVPQ 439
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNpyskkiknfkelRRRVSMVFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 440 --ESILFEGSIRENVSYG-MDGEVPDEKIREALAAANAL-----EFVDRMPQGvetvvgargarLSGGQKQRLAIARALV 511
Cdd:PRK13631 124 fpEYQLFKDTIEKDIMFGpVALGVKKSEAKKLAKFYLNKmglddSYLERSPFG-----------LSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 512 RDPRVLVLDEATSALDNQSEA-LVQEALERLMRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLAGTGPYAT 589
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQHIINS 272
|
.
gi 2764013554 590 T 590
Cdd:PRK13631 273 T 273
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
358-576 |
9.37e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.50 E-value: 9.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDAAEHSVR---DFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGL----DLRTY 430
Cdd:PRK13649 4 NLQNVSYTYQAGTPFEGRalfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 431 RRFLSVVPQ--ESILFEGSIRENVSYG-MDGEVPDEKIREALAAANALEFVDrmpqgvETVVGARGARLSGGQKQRLAIA 507
Cdd:PRK13649 84 RKKVGLVFQfpESQLFEETVLKDVAFGpQNFGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 508 RALVRDPRVLVLDEATSALDNQSEALVQEALERLMR-GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGT 576
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
367-580 |
1.14e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.48 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 367 PDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRF-LSVVPQE----- 440
Cdd:COG3845 267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDrlgrg 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 441 SILfEGSIRENV---SYGMDGEVPDEKIREALAAANALEFVDRM---PQGVETVVGArgarLSGGQKQRLAIARALVRDP 514
Cdd:COG3845 347 LVP-DMSVAENLilgRYRRPPFSRGGFLDRKAIRAFAEELIEEFdvrTPGPDTPARS----LSGGNQQKVILARELSRDP 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEAL-ERLMRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEEL 580
Cdd:COG3845 422 KLLIAAQPTRGLDVGAIEFIHQRLlELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIVGEVPAAEA 489
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
358-552 |
1.53e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 91.30 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPdaAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTyrrflSVV 437
Cdd:PRK11248 3 QISHLYADYG--GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 PQ-ESILFEGSIRENVSYGMD-GEVPDEKIREALAAANALefvdrmpqgvetvVGARGA------RLSGGQKQRLAIARA 509
Cdd:PRK11248 76 FQnEGLLPWRNVQDNVAFGLQlAGVEKMQRLEIAHQMLKK-------------VGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2764013554 510 LVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAH 552
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH 187
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-581 |
1.87e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.13 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIR--PTA---GRILLDGEDIAGLDLRTYRRFLSVVPQ-ESILFEGS 447
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 448 IRENVSYGMDGEVPDEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:PRK14247 99 IFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 528 NQSEALVQEALERLMRGRTVFVVAH------RLStiqdaDRIVVMERGRLVEVGTHEELL 581
Cdd:PRK14247 179 PENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREVF 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
371-592 |
2.51e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.80 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 371 EHSV-RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGL-------------DLRTYRRFLSV 436
Cdd:PRK10619 17 EHEVlKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 437 VPQESILFEG-SIRENVsygMDGEVPDEKIREALAAANALEFVDRMpqGV-ETVVGARGARLSGGQKQRLAIARALVRDP 514
Cdd:PRK10619 97 VFQHFNLWSHmTVLENV---MEAPIQVLGLSKQEARERAVKYLAKV--GIdERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 515 RVLVLDEATSALDNQseaLVQEALeRLMR-----GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLAgtGPYA 588
Cdd:PRK10619 172 EVLLFDEPTSALDPE---LVGEVL-RIMQqlaeeGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG--NPQS 245
|
....
gi 2764013554 589 TTLQ 592
Cdd:PRK10619 246 PRLQ 249
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
374-580 |
2.56e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 92.60 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTyrRFLSVVPQESILF-EGSIRENV 452
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVFQNYALYpHMSVRENM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 SYG-----MDGEVPDEKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:PRK11650 98 AYGlkirgMPKAEIEERVAEAARILELEPLLDRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 528 nqsEAL-VQEALE--RLMR--GRTVFVVAH-RLSTIQDADRIVVMERGRLVEVGTHEEL 580
Cdd:PRK11650 167 ---AKLrVQMRLEiqRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
356-582 |
2.63e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 94.65 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 356 TFTFDEVGFRYPDAAeHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLS 435
Cdd:PRK10522 322 TLELRNVTFAYQDNG-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 436 VVPQESILFEGSIrenvsyGMDGEVPDEKIrealaaanALEFVDR--MPQGVEtVVGARGA--RLSGGQKQRLAIARALV 511
Cdd:PRK10522 401 AVFTDFHLFDQLL------GPEGKPANPAL--------VEKWLERlkMAHKLE-LEDGRISnlKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 512 RDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAA 538
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
372-580 |
2.79e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.31 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIaglDLRTYR----RFLSVVP----QESIL 443
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV---RIRSPRdairAGIAYVPedrkGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 444 FEGSIRENVS------YGMDGEVPDEKIRealaaANALEFVDRM---PQGVETVVGArgarLSGGQKQRLAIARALVRDP 514
Cdd:COG1129 343 LDLSIRENITlasldrLSRGGLLDRRRER-----ALAEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEALERL-MRGRTVFVVahrlST-----IQDADRIVVMERGRLVEVGTHEEL 580
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIRELaAEGKAVIVI----SSelpelLGLSDRILVMREGRIVGELDREEA 481
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
375-578 |
3.16e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 90.13 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFI--RPTAGRILLDGEDIagLDLRTYRR-----FLS------------ 435
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDI--LELSPDERaragiFLAfqypveipgvsv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 436 ---------VVPQESI---LFEGSIRENVS-YGMDGEvpdekirealaaanaleFVDRmpqGVEtvVGargarLSGGQKQ 502
Cdd:COG0396 95 snflrtalnARRGEELsarEFLKLLKEKMKeLGLDED-----------------FLDR---YVN--EG-----FSGGEKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 503 RLAIARALVRDPRVLVLDEATSALDnqSEAL--VQEALERLMR-GRTVFVVAH--RLSTIQDADRIVVMERGRLVEVGTH 577
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLD--IDALriVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGK 225
|
.
gi 2764013554 578 E 578
Cdd:COG0396 226 E 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
357-582 |
3.21e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 89.94 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 357 FTFDEVGFRYPD-AAEHSVrdfSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDL-RTYRRFL 434
Cdd:PRK11614 6 LSFDKVSAHYGKiQALHEV---SLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 435 SVVPQESILFEG-SIRENVSYG---MDGEVPDEKIREAlaaanalefVDRMPQGVETVVgARGARLSGGQKQRLAIARAL 510
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMGgffAERDQFQERIKWV---------YELFPRLHERRI-QRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2764013554 511 VRDPRVLVLDEATSALDNQSEALVQEALERLM-RGRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLReQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
374-581 |
3.75e-20 |
|
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: 88.74 E-value: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGF--IRPTAGRILLDGEDIagLDLRTYRR-----FLSvvPQESILFEG 446
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDI--TDLPPEERarlgiFLA--FQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 447 -SIRE---NVSYGmdgevpdekirealaaanalefvdrmpqgvetvvgargarLSGGQKQRLAIARALVRDPRVLVLDEA 522
Cdd:cd03217 92 vKNADflrYVNEG----------------------------------------FSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 523 TSALDNQSEALVQEALERLMR-GRTVFVVAH--RLSTIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELAL 193
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
376-592 |
3.96e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.96 E-value: 3.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLsvRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD-LRTYRRFLSVVPQESILFEG-SIRENVS 453
Cdd:PRK15439 31 DFTL--HAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFPNlSVKENIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 454 YGMDGEVPDEKirealaaanalefvdRMPQ-----GVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALD- 527
Cdd:PRK15439 109 FGLPKRQASMQ---------------KMKQllaalGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTp 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 528 NQSEALVQEALERLMRGRTVFVVAHRLSTI-QDADRIVVMERGRLVEVG-----THEELLAGTGPYATTLQ 592
Cdd:PRK15439 174 AETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGktadlSTDDIIQAITPAAREKS 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
388-579 |
4.43e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 91.86 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 388 ALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGE---DIA-GLDLRTYRRFLSVVPQESILFEG-SIRENVSYGMDGEVPD 462
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEkGICLPPEKRRIGYVFQDARLFPHyKVRGNLRYGMAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 463 EkirealaaanaleFvDRMPQ--GVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALER 540
Cdd:PRK11144 108 Q-------------F-DKIVAllGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2764013554 541 LmrGRTVFV----VAHRLSTI-QDADRIVVMERGRLVEVGTHEE 579
Cdd:PRK11144 174 L--AREINIpilyVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
374-580 |
7.19e-20 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 94.59 E-value: 7.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEdiagldlrtyrrfLSVVPQESILFEGSIRENVS 453
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 454 YGMDgevPDE-KIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEA 532
Cdd:TIGR01271 509 FGLS---YDEyRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2764013554 533 LVQEA-LERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEEL 580
Cdd:TIGR01271 586 EIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
373-563 |
1.25e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.07 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 373 SVRDFSLSVRAGETVALVGGSGAGKSTVL-------NLVIGFirPTAGRILLDGEDI--AGLDLRTYRRFLSVVPQESIL 443
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGF--RVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 444 FEGSIRENVSYG-----MDGEVpDEKI-REALAAANALEFVDRMPQGvetvvgarGARLSGGQKQRLAIARALVRDPRVL 517
Cdd:PRK14243 103 FPKSIYDNIAYGaringYKGDM-DELVeRSLRQAALWDEVKDKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2764013554 518 VLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLstiQDADRI 563
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM---QQAARV 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
357-567 |
1.47e-19 |
|
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: 86.05 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 357 FTFDEVGFRYPDAaEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNlVIGFIRP-TAGRI-LLDGEDIAgldlrtyrrFL 434
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFR-ALAGLWPwGSGRIgMPEGEDLL---------FL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 435 svvPQESILFEGSIRENVSYgmdgevPDEKIrealaaanalefvdrmpqgvetvvgargarLSGGQKQRLAIARALVRDP 514
Cdd:cd03223 70 ---PQRPYLPLGTLREQLIY------PWDDV------------------------------LSGGEQQRLAFARLLLHKP 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEALERlmRGRTVFVVAHRLSTIQDADRIVVME 567
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRVLDLD 161
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
365-571 |
2.83e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.18 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 365 RYPDAAEHS--VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGL------DLRTYR----- 431
Cdd:PRK11629 14 RYQEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaELRNQKlgfiy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 432 RFLSVVPQESILfegsirENVSYGM--DGEVPDEKIREALAAANALefvdrmpqGVETVVGARGARLSGGQKQRLAIARA 509
Cdd:PRK11629 94 QFHHLLPDFTAL------ENVAMPLliGKKKPAEINSRALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2764013554 510 LVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQDADRIVVMERGRL 571
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRlqGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
324-592 |
3.40e-19 |
|
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: 92.38 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 324 RGLESVRSVGEVLQAPdlEVNEGKRDA-------GEVTGTFTFDEVGFRYPdAAEHSVRDFSLSVRAGETVALVGGSGAG 396
Cdd:TIGR01257 892 RALEKTEPLTEEMEDP--EHPEGINDSfferelpGLVPGVCVKNLVKIFEP-SGRPAVDRLNITFYENQITAFLGHNGAG 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 397 KSTVLNLVIGFIRPTAGRILLDGEDIAgLDLRTYRRFLSVVPQESILFEG-SIRENVSY--GMDGEVPDEkireaLAAAN 473
Cdd:TIGR01257 969 KTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHHlTVAEHILFyaQLKGRSWEE-----AQLEM 1042
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 474 ALEFVDrmpQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHR 553
Cdd:TIGR01257 1043 EAMLED---TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHH 1119
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2764013554 554 LSTIQD-ADRIVVMERGRLVEVGTHEEL--LAGTGPYATTLQ 592
Cdd:TIGR01257 1120 MDEADLlGDRIAIISQGRLYCSGTPLFLknCFGTGFYLTLVR 1161
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
369-575 |
3.48e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 87.67 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 369 AAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTY----RRFLS-----VVPQ 439
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLLrtewgFVHQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 440 ESilfEGSIRENVSYG-------MD------GEVPDEKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAI 506
Cdd:PRK11701 97 HP---RDGLRMQVSAGgnigerlMAvgarhyGDIRATAGDWLERVEIDAARIDDLP-----------TTFSGGMQQRLQI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 507 ARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVG 575
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
374-582 |
5.78e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 86.68 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKS----TVLNLVIGFIRPTAGRILLDGEDIAGLDLRTyrRFLSVVPQESILFEGSIR 449
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRG--RKIATIMQNPRSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVSYGMdgevpdEKIREALAAANALEFVDRMP----QGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSA 525
Cdd:PRK10418 97 TMHTHAR------ETCLALGKPADDATLTAALEavglENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 526 LDNQSEALVQEALERLMRGRT--VFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFN 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
382-581 |
9.94e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.11 E-value: 9.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 382 RAGETVALVGGSGAGKSTVLNlVIGFIRPT----AGRILLDGEDIaglDLRTYRRFLSVVPQESILFeGSI--RENVSYG 455
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMN-ALAFRSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLFI-PTLtvREHLMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 456 ----MDGEVPDEKIREAlaaanalefVDRMPQGV------ETVVGARGAR--LSGGQKQRLAIARALVRDPRVLVLDEAT 523
Cdd:TIGR00955 124 ahlrMPRRVTKKEKRER---------VDEVLQALglrkcaNTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 524 SALDNQSEALVQEALERL-MRGRTVFVVAHRLST--IQDADRIVVMERGRLVEVGTHEELL 581
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
361-584 |
2.11e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.44 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 361 EVGFRYPDaaEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGE--DIAGLDLRTYRRFLSVVP 438
Cdd:PRK13638 6 DLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 439 Q--ESILFEGSIRENVSYGMDG-EVPDEKIRealaaanalefvdRMPQGVETVVGARGAR------LSGGQKQRLAIARA 509
Cdd:PRK13638 84 QdpEQQIFYTDIDSDIAFSLRNlGVPEAEIT-------------RRVDEALTLVDAQHFRhqpiqcLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 510 LVRDPRVLVLDEATSALDNQSEALVQEALERLM-RGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLAGT 584
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACT 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
376-572 |
3.13e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.77 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLsvRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRT---YRRFLSVVPQE-SILFEGSIREN 451
Cdd:PRK10908 22 TFHM--RPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDhHLLMDRTVYDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 452 VSYGM--DGEVPDEKIREALAAANALEFVDRmpqgvetvvgARG--ARLSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:PRK10908 100 VAIPLiiAGASGDDIRRRVSAALDKVGLLDK----------AKNfpIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2764013554 528 NQSEALVQEALERLMR-GRTVFVVAHRLSTIQDAD-RIVVMERGRLV 572
Cdd:PRK10908 170 DALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
374-589 |
3.83e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 89.07 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDgediagldlrtyrRFLSVVPQESILFEGSIRENVS 453
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 454 YgMDGEVPdEKIREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQ-SEA 532
Cdd:PTZ00243 743 F-FDEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGER 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 533 LVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAgTGPYAT 589
Cdd:PTZ00243 821 VVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR-TSLYAT 876
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
362-591 |
4.10e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 362 VGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKStVLNLVIGFIRPT------AGRILLDGEDIAGLDLRTYRRF-- 433
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKS-VTALSILRLLPSppvvypSGDIRFHGESLLHASEQTLRGVrg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 434 --LSVVPQESIL-------FEGSIRENVSY--GMDGEVPDEKIrealaaanaLEFVDRmpqgvetvVGARGAR------- 495
Cdd:PRK15134 92 nkIAMIFQEPMVslnplhtLEKQLYEVLSLhrGMRREAARGEI---------LNCLDR--------VGIRQAAkrltdyp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 496 --LSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTI-QDADRIVVMERGR 570
Cdd:PRK15134 155 hqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGR 234
|
250 260
....*....|....*....|..
gi 2764013554 571 LVEVGTHEELL-AGTGPYATTL 591
Cdd:PRK15134 235 CVEQNRAATLFsAPTHPYTQKL 256
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
354-582 |
6.27e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.67 E-value: 6.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 354 TGTFTFDEVGFRYPDAAEHSVR---DFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDI-AGL---- 425
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTPFEFKalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLkkik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 426 DLRTYRRFLSVVPQ--ESILFEGSIRENVSYG-----MDGEVPDEKI-REALAAANALEFVDRMPqgvetvvgargARLS 497
Cdd:PRK13645 84 EVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGpvnlgENKQEAYKKVpELLKLVQLPEDYVKRSP-----------FELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 498 GGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTI-QDADRIVVMERGRLVEV 574
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISI 232
|
....*...
gi 2764013554 575 GTHEELLA 582
Cdd:PRK13645 233 GSPFEIFS 240
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
375-571 |
6.30e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.04 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGediaglDLRtyrrfLSVVPQESILFEG-SIRENVS 453
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYLPQEPPLDDDlTVLDTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 454 YGMD--GEVPDEKIREALAAANALEFVDRM---------------PQGVETVVGARG----------ARLSGGQKQRLAI 506
Cdd:COG0488 84 DGDAelRALEAELEELEAKLAEPDEDLERLaelqeefealggweaEARAEEILSGLGfpeedldrpvSELSGGWRRRVAL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 507 ARALVRDPRVLVLDEATSALDNQSealvQEALERLMRGR--TVFVVAH-R--LSTIqdADRIVVMERGRL 571
Cdd:COG0488 164 ARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYpgTVLVVSHdRyfLDRV--ATRILELDRGKL 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
374-572 |
6.65e-18 |
|
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: 83.15 E-value: 6.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEdIAGLDLRTYRRFLSVV------------PQES 441
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVfgqktqlwwdlpVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 442 ILFEGSIrenvsYGMDGEVPDEKIRealaaanalEFVDRMPQGVETVVGARgaRLSGGQKQRLAIARALVRDPRVLVLDE 521
Cdd:cd03267 116 FYLLAAI-----YDLPPARFKKRLD---------ELSELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2764013554 522 ATSALDNQSEALVQEALERLMRGR--TVFVVAHRLSTIQD-ADRIVVMERGRLV 572
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
372-587 |
1.01e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 84.37 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAgLDLRTYRRFLSVV------------PQ 439
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPF-KRRKEFARRIGVVfgqrsqlwwdlpAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 440 ESILFEGSIrenvsYgmdgEVPDEKIRealaaANALEFVDRMpqGVETVVG--ARgaRLSGGQKQRLAIARALVRDPRVL 517
Cdd:COG4586 115 DSFRLLKAI-----Y----RIPDAEYK-----KRLDELVELL--DLGELLDtpVR--QLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 518 VLDEATSALDNQSEALVQEALERL--MRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLAGTGPY 587
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-581 |
1.17e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.17 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIR------PTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEG- 446
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 447 SIRENVSYGMDGEVPDEKIREALAAANALEFVDrMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSAL 526
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKIVEECLRKVG-LWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 527 DNQSEALVQEALERLMRGRTVFVVAHRLSTI-QDADRIVVMERGRLVEVGTHEELL 581
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
359-580 |
1.76e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.73 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 359 FDEVGFRYPdaaehSVR---DFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDiagldlrtyRRFLS 435
Cdd:PRK11288 7 FDGIGKTFP-----GVKaldDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE---------MRFAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 436 ----------VVPQESILF-EGSIRENVsygMDGEVPDEK--IREALAAANALEFVDRMpqGVETVVGARGARLSGGQKQ 502
Cdd:PRK11288 73 ttaalaagvaIIYQELHLVpEMTVAENL---YLGQLPHKGgiVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 503 RLAIARALVRDPRVLVLDEATSALDNQSealvqeaLERLMR--------GRTVFVVAHRLSTIQD-ADRIVVMERGRLVE 573
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSARE-------IEQLFRvirelraeGRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
....*..
gi 2764013554 574 vgTHEEL 580
Cdd:PRK11288 221 --TFDDM 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
372-575 |
2.27e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLR-TYRRFLSVVPQE-SILFEGSIR 449
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQElSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVSYGmdgEVPDEK------IREALAAANALEFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEAT 523
Cdd:PRK09700 99 ENLYIG---RHLTKKvcgvniIDWREMRVRAAMMLLRV--GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2764013554 524 SALDNQSEALVQEALERLMR-GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVG 575
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
378-582 |
4.05e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 81.68 E-value: 4.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 378 SLSVRAGETVALVGGSGAGKSTVL-------NLVIGFirPTAGRILLDGEDIAGL-DLRTYRRFLSVVPQESILFEGSIR 449
Cdd:PRK14271 41 SMGFPARAVTSLMGPTGSGKTTFLrtlnrmnDKVSGY--RYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVSYGMDGE--VPDEKIREALAAANALEfvdRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:PRK14271 119 DNVLAGVRAHklVPRKEFRGVAQARLTEV---GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 528 NQSEALVQEALERLMRGRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
376-552 |
6.23e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 6.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSvrAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSvvPQESILFEGSIRENVS-- 453
Cdd:PRK13539 22 SFTLA--AGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVAENLEfw 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 454 ---YGMDGEVPDEKIrealaaanalEFVDRmpQGVETVvgaRGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQS 530
Cdd:PRK13539 98 aafLGGEELDIAAAL----------EAVGL--APLAHL---PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|...
gi 2764013554 531 EALVQEAL-ERLMRGRTVFVVAH 552
Cdd:PRK13539 163 VALFAELIrAHLAQGGIVIAATH 185
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
376-567 |
1.07e-16 |
|
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: 79.76 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAG-----ETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAgldlrtYRrflsvvPQE-SILFEGSIR 449
Cdd:cd03237 12 EFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------YK------PQYiKADYEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVSYGMDGEVPDEKIRealaaanalefVDRM-PQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDN 528
Cdd:cd03237 80 DLLSSITKDFYTHPYFK-----------TEIAkPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2764013554 529 QSEALVQEALERLM--RGRTVFVVAHRLSTIQD-ADRIVVME 567
Cdd:cd03237 149 EQRLMASKVIRRFAenNEKTAFVVEHDIIMIDYlADRLIVFE 190
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
377-581 |
2.79e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.73 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 377 FSLSVRAGETVALVGGSGAGKSTVLNLVIGFIrPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILfegsirenvSYGM 456
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSP---------PFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 457 -----------DGEVPDEKIREALAAANALEFVDRMPQGVETvvgargarLSGGQKQRLAIARALVR-------DPRVLV 518
Cdd:COG4138 85 pvfqylalhqpAGASSEAVEQLLAQLAEALGLEDKLSRPLTQ--------LSGGEWQRVRLAAVLLQvwptinpEGQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 519 LDEATSALDNQSEAlvqeALERLMR-----GRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:COG4138 157 LDEPMNSLDVAQQA----ALDRLLRelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
55-312 |
3.07e-16 |
|
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: 79.22 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 55 LLPLVTARIIDIVVDHKPVSA------LWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRtgteLRGALCHRMQHLSIGYH 128
Cdd:pfam00664 17 AFPLVLGRILDVLLPDGDPETqalnvySLALLLLGLAQFILSFLQSYLLNHTGERLSRR----LRRKLFKKILRQPMSFF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 129 SRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAP----VALPLFIVVVPLAALLVRSLRGRIRAD 204
Cdd:pfam00664 93 DTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWkltlVLLAVLPLYILVSAVFAKILRKLSRKE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 205 NEAfrveVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILLN-VMAVAFLSGSA 283
Cdd:pfam00664 173 QKA----VAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYlSYALALWFGAY 248
|
250 260
....*....|....*....|....*....
gi 2764013554 284 LVAYyglFGISPGDVVMISTFFTGLTASL 312
Cdd:pfam00664 249 LVIS---GELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
72-308 |
4.55e-16 |
|
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: 79.09 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 72 PVSALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRTGTELRGALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALETML 151
Cdd:cd18564 49 PLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 152 QQTAQNGLGAVMTLLGGLAVIgFQAPVALPLF-IVVVPLAALLVRSLRGRIRADNEAFRVEVEQLSARVGEMTTLIPITR 230
Cdd:cd18564 129 VSGVLPLLTNLLTLVGMLGVM-FWLDWQLALIaLAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 231 AHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILlnvMAVaflsGSALVAYYGLFGI-----SPGDVVMISTFF 305
Cdd:cd18564 208 AFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVL---VAV----GTALVLWFGAWLVlagrlTPGDLLVFLAYL 280
|
...
gi 2764013554 306 TGL 308
Cdd:cd18564 281 KNL 283
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
373-582 |
4.90e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 78.29 E-value: 4.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 373 SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRtYR----RFL------SVVPQESI 442
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS-YRsqriRMIfqdpstSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 443 --LFEGSIRENVsyGMDGEVPDEKI----REALAAANALEFVDRMpqgvetvvgargarLSGGQKQRLAIARALVRDPRV 516
Cdd:PRK15112 107 sqILDFPLRLNT--DLEPEQREKQIietlRQVGLLPDHASYYPHM--------------LAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 517 LVLDEATSALD----NQSEALVQEALERlmRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK15112 171 IIADEALASLDmsmrSQLINLMLELQEK--QGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
358-570 |
5.76e-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: 75.18 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 358 TFDEVGFRYPDaaEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGediagldlrtyrrflsvv 437
Cdd:cd03221 2 ELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 pqesilfegsiRENVSYgmdgevpdekirealaaanalefvdrMPQgvetvvgargarLSGGQKQRLAIARALVRDPRVL 517
Cdd:cd03221 62 -----------TVKIGY--------------------------FEQ------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 518 VLDEATSALDNQSealvQEALERLMRG--RTVFVVAH-R--LSTIqdADRIVVMERGR 570
Cdd:cd03221 93 LLDEPTNHLDLES----IEALEEALKEypGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
381-569 |
6.78e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 81.69 E-value: 6.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 381 VRAGETVALVGGSGAGKSTVLNLVIGfiRPTAGrILLDGEDIAG---LDlRTYRRFLSVVPQESI-LFEGSIRENVSYG- 455
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAE--RVTTG-VITGGDRLVNgrpLD-SSFQRSIGYVQQQDLhLPTSTVRESLRFSa 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 456 ---MDGEVPD-EKIRealaaanaleFVDR------MPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLV-LDEATS 524
Cdd:TIGR00956 862 ylrQPKSVSKsEKME----------YVEEviklleMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTS 931
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 525 ALDNQSEAlvqeALERLMR-----GRTVFVVAHRLSTI--QDADRIVVMERG 569
Cdd:TIGR00956 932 GLDSQTAW----SICKLMRkladhGQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
374-582 |
9.99e-16 |
|
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: 80.23 E-value: 9.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGF--IRPTAGRIL----------------LDGE--------------D 421
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEpcpvcggtlepeevD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 422 IAGLD---LRTYRRFLSVVPQESILFEGSIR--ENVSYGMD--GEVPDEKIREALAAANALEFVDRMpqgvetvvgARGA 494
Cdd:TIGR03269 96 FWNLSdklRRRIRKRIAIMLQRTFALYGDDTvlDNVLEALEeiGYEGKEAVGRAVDLIEMVQLSHRI---------THIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 495 R-LSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGR 570
Cdd:TIGR03269 167 RdLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDlSDKAIWLENGE 246
|
250
....*....|..
gi 2764013554 571 LVEVGTHEELLA 582
Cdd:TIGR03269 247 IKEEGTPDEVVA 258
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
376-586 |
1.11e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.50 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD---LRTYRRFLSVVPQESILF-EGSIREN 451
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRMSMLFQSGALFtDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 452 VSYGM--DGEVPDEKIREALAAANalefvdrmpqgveTVVGARGA------RLSGGQKQRLAIARALVRDPRVLVLDEAT 523
Cdd:PRK11831 105 VAYPLreHTQLPAPLLHSTVMMKL-------------EAVGLRGAaklmpsELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 524 SALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLAGTGP 586
Cdd:PRK11831 172 VGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQANPDP 237
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
370-580 |
1.42e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.98 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 370 AEHSVrdfSLSVRAGETVALVGGSGAGKSTVLNLVIGFI---RPTAGRILLDGEDIA-----GLDLRTYRRFLSVVPQE- 440
Cdd:PRK09984 19 ALHAV---DLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlARDIRKSRANTGYIFQQf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 441 SILFEGSIRENVSYGMDGEVPDEK--IREALAAANALEFVDRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLV 518
Cdd:PRK09984 96 NLVNRLSVLENVLIGALGSTPFWRtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 519 LDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEEL 580
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
55-332 |
1.68e-15 |
|
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: 77.46 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 55 LLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLL----NYpLHMYF-SKLSSLAIRRtgteLRGALCHRMQHLSIGYHS 129
Cdd:cd18552 17 ALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLrglaSY-LQTYLmAYVGQRVVRD----LRNDLFDKLLRLPLSFFD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 130 RVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPV-ALpLFIVVVPLAALLVRSLRGRIRADNEAF 208
Cdd:cd18552 92 RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKlTL-IALVVLPLAALPIRRIGKRLRKISRRS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 209 RVEVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVltagFRLDMLGGRFGSLSwillnVMAVAFLSGSALVA-- 286
Cdd:cd18552 171 QESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERL----RRLSMKIARARALS-----SPLMELLGAIAIALvl 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 287 YYGLF-----GISPGDVVMISTFFTGLTASLTALLNLMPIVSRGLESVRSV 332
Cdd:cd18552 242 WYGGYqvisgELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
378-552 |
2.45e-15 |
|
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: 74.84 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 378 SLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSYGMD 457
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 458 gEVPDEKIREALAAANALEFVDRMpqgvetvvgarGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEA 537
Cdd:cd03231 100 -DHSDEQVEEALARVGLNGFEDRP-----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*.
gi 2764013554 538 L-ERLMRGRTVFVVAH 552
Cdd:cd03231 168 MaGHCARGGMVVLTTH 183
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
367-581 |
2.88e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 77.25 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 367 PDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRP----TAGRILLDGEDIAGLDLRTYRRflsVVPQE-S 441
Cdd:COG4170 16 PQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRK---IIGREiA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 442 ILFEgsirENVSYgMDgevPDEKI---------REALAAANALEFVDRMPQGVETV--VGARGAR---------LSGGQK 501
Cdd:COG4170 93 MIFQ----EPSSC-LD---PSAKIgdqlieaipSWTFKGKWWQRFKWRKKRAIELLhrVGIKDHKdimnsypheLTEGEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 502 QRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERL--MRGRTVFVVAHRLSTI-QDADRIVVMERGRLVEVGTHE 578
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnqLQGTSILLISHDLESIsQWADTITVLYCGQTVESGPTE 244
|
...
gi 2764013554 579 ELL 581
Cdd:COG4170 245 QIL 247
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
362-591 |
3.17e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.07 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 362 VGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRP---TAGRILLDGEDIAGLDLRTYRRFLSvvP 438
Cdd:PRK09473 20 VTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKLRA--E 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 439 QESILFEGSIRENVSY---------------GMDG-EVPDEKIREALAAanalefvdRMPQgvetvvgARgARL------ 496
Cdd:PRK09473 98 QISMIFQDPMTSLNPYmrvgeqlmevlmlhkGMSKaEAFEESVRMLDAV--------KMPE-------AR-KRMkmyphe 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 497 -SGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLV 572
Cdd:PRK09473 162 fSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTM 241
|
250 260
....*....|....*....|
gi 2764013554 573 EVGTHEELL-AGTGPYATTL 591
Cdd:PRK09473 242 EYGNARDVFyQPSHPYSIGL 261
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
378-580 |
3.34e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 76.66 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 378 SLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGL------------------------DLRTYRRF 433
Cdd:PRK13651 27 SVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqktrfkkikKIKEIRRR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 434 LSVVPQ--ESILFEGSIREN-----VSYGMDGEVPDEKIREALAAA-NALEFVDRMPQGvetvvgargarLSGGQKQRLA 505
Cdd:PRK13651 107 VGVVFQfaEYQLFEQTIEKDiifgpVSMGVSKEEAKKRAAKYIELVgLDESYLQRSPFE-----------LSGGQKRRVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 506 IARALVRDPRVLVLDEATSALDNQSealVQEALERL----MRGRTVFVVAHRL-STIQDADRIVVMERGRLVEVG-THEE 579
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQG---VKEILEIFdnlnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGdTYDI 252
|
.
gi 2764013554 580 L 580
Cdd:PRK13651 253 L 253
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
372-582 |
3.41e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.59 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRpTAGRILLDGEDIAGLDLRT---YRRFLSVVPQE--SILfeg 446
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDpnSSL--- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 447 SIRENVSygmdgEVPDEKIREALAAANALEFVDRMPQGVETVVGARGAR------LSGGQKQRLAIARALVRDPRVLVLD 520
Cdd:PRK15134 376 NPRLNVL-----QIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRhrypaeFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 521 EATSALDNQSEALVQEALERLMRGRTV--FVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
378-552 |
7.22e-15 |
|
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: 73.55 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 378 SLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLdlrtyrrflSVVPQESILFEG---------SI 448
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ---------RDEPHENILYLGhlpglkpelSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 449 RENVSYgmdgevpdekirealaAANALEFVDRMPQGVETVVGARG------ARLSGGQKQRLAIARALVRDPRVLVLDEA 522
Cdd:TIGR01189 91 LENLHF----------------WAAIHGGAQRTIEDALAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 2764013554 523 TSALDNQSEALVQEALE-RLMRGRTVFVVAH 552
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRaHLARGGIVLLTTH 185
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-598 |
1.08e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.30 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVL------NLVIGFIRpTAGRILLDGEDI--AGLDLRTYRRFLSVVPQESILFE 445
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnrmNELESEVR-VEGRVEFFNQNIyeRRVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 446 GSIRENVSYGMD--GEVPDEKIREALAAANALEfvdRMPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEAT 523
Cdd:PRK14258 102 MSVYDNVAYGVKivGWRPKLEIDDIVESALKDA---DLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 524 SALDNQSEALVQEALE--RLMRGRTVFVVAHRLSTIQ-----------DADRIvvmerGRLVEVGTHEELLagTGPYATT 590
Cdd:PRK14258 179 FGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSrlsdftaffkgNENRI-----GQLVEFGLTKKIF--NSPHDSR 251
|
....*...
gi 2764013554 591 LQPRAYSR 598
Cdd:PRK14258 252 TREYVLSR 259
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
381-569 |
1.11e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 72.66 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 381 VRAGETVALVGGSGAGKSTVLNLVIGfiRPTA----GRILLDGEDIAgldlRTYRRFLSVVPQESILFEGS-IRENVSYG 455
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAG--RKTAgvitGEILINGRPLD----KNFQRSTGYVEQQDVHSPNLtVREALRFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 456 MDgevpdekirealaaanalefvdrmpqgvetvvgARGarLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQ 535
Cdd:cd03232 104 AL---------------------------------LRG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 2764013554 536 EALERL-MRGRTVFVVAHRLS--TIQDADRIVVMERG 569
Cdd:cd03232 149 RFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
360-591 |
1.17e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.47 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 360 DEVGFRYpdAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGldlRTYRRflSVVPQ 439
Cdd:NF033858 5 EGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRR--AVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 440 esILF--EG---------SIRENVS-----YGMDGEVPDEKIREALAAANALEFVDRmPQGvetvvgargaRLSGGQKQR 503
Cdd:NF033858 78 --IAYmpQGlgknlyptlSVFENLDffgrlFGQDAAERRRRIDELLRATGLAPFADR-PAG----------KLSGGMKQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 504 LAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGR---TVFVvahrlST--IQDADR---IVVMERGRLVEVG 575
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLV-----ATayMEEAERfdwLVAMDAGRVLATG 219
|
250
....*....|....*.
gi 2764013554 576 THEELLAGTGpyATTL 591
Cdd:NF033858 220 TPAELLARTG--ADTL 233
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
55-315 |
2.18e-14 |
|
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: 74.01 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 55 LLPLVTARIIDIVVDHKPVsalwWNTAAVLVVLLLnypLHMYFSKLSSLAIRRTG----TELRGALCHRMQHLSIGYHSR 130
Cdd:cd18551 17 AQPLLVKNLIDALSAGGSS----GGLLALLVALFL---LQAVLSALSSYLLGRTGervvLDLRRRLWRRLLRLPVSFFDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 131 VSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVALPLFIVVVPLAALLVRSLRGRIRADNEAFRV 210
Cdd:cd18551 90 RRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 211 EVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILLNVMAVA------------F 278
Cdd:cd18551 170 ALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVvlgvggarvasgA 249
|
250 260 270
....*....|....*....|....*....|....*....
gi 2764013554 279 LSGSALVAY--YGLFGISPgdVVMISTFFTGLTASLTAL 315
Cdd:cd18551 250 LTVGTLVAFllYLFQLITP--LSQLSSFFTQLQKALGAL 286
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
55-332 |
3.51e-14 |
|
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: 73.36 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 55 LLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRTGTELRGALCHRMQHLSIGYHSRVSAE 134
Cdd:cd18557 14 LLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 135 VLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVALPLFIVVVPLAALLVRSLRGRIRADNEAFRVEVEQ 214
Cdd:cd18557 94 ELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 215 LSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILLNVMAVAFLS-GSALVAYYGLfgi 293
Cdd:cd18557 174 AGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWyGGYLVLSGQL--- 250
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2764013554 294 SPGDVV--MISTFFtgLTASLTALLNLMPIVSRGLESVRSV 332
Cdd:cd18557 251 TVGELTsfILYTIM--VASSVGGLSSLLADIMKALGASERV 289
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
374-581 |
6.22e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.17 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIG-FIRPTA-------GRILLDGEDIAGLDLRTYRRFLSVVPQES-ILF 444
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAqPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 445 EGSIRENVSYGM-------------DGEVPDEKIREAlaaanalefvdrmpqGVETVVGARGARLSGGQKQRLAIARAL- 510
Cdd:PRK13547 97 AFSAREIVLLGRypharragalthrDGEIAWQALALA---------------GATALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 511 --------VRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVA--HRLS-TIQDADRIVVMERGRLVEVGTHEE 579
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNlAARHADRIAMLADGAIVAHGAPAD 241
|
..
gi 2764013554 580 LL 581
Cdd:PRK13547 242 VL 243
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
372-575 |
8.64e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.51 E-value: 8.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD---LRTYRR---------FLSVVPQ 439
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRdiqfifqdpYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 440 ESILFegSIRE--NVSYGMDGEVPDEKIR-EALAAANALEFVDRMPQgvetvvgargaRLSGGQKQRLAIARALVRDPRV 516
Cdd:PRK10261 418 QTVGD--SIMEplRVHGLLPGKAAAARVAwLLERVGLLPEHAWRYPH-----------EFSGGQRQRICIARALALNPKV 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 517 LVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVG 575
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
373-578 |
9.09e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 9.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 373 SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLdLRtyRRFLSVVPQES-------ILFE 445
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-LQ--KNLVAYVPQSEevdwsfpVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 446 GSIRENvSYGMDGEVPDEKIREALAAANALEFVDrMPQGVETVVGargaRLSGGQKQRLAIARALVRDPRVLVLDEATSA 525
Cdd:PRK15056 99 DVVMMG-RYGHMGWLRRAKKRDRQIVTAALARVD-MVEFRHRQIG----ELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2764013554 526 LDNQSEALVQEALERLM-RGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHE 578
Cdd:PRK15056 173 VDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
357-581 |
1.57e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.64 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 357 FTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLN-----LVIGFIRPTAGRILLDGEDIAGLDLRT-- 429
Cdd:PRK14267 3 FAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDVDPie 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 430 YRRFLSVVPQESILFEG-SIRENVSYGMD--------GEVpDEKIREALAAANALEFV-DRMPQgvetvvgaRGARLSGG 499
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHlTIYDNVAIGVKlnglvkskKEL-DERVEWALKKAALWDEVkDRLND--------YPSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 500 QKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHrlSTIQDA---DRIVVMERGRLVEVGT 576
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVGP 231
|
....*
gi 2764013554 577 HEELL 581
Cdd:PRK14267 232 TRKVF 236
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
375-552 |
1.62e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.45 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESILFEGSIRENVSY 454
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 455 --GMDGEVPDEKIRealaaanalefvdrmpQGVETvVGARG------ARLSGGQKQRLAIARALVRDPRVLVLDEATSAL 526
Cdd:PRK13538 98 yqRLHGPGDDEALW----------------EALAQ-VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*..
gi 2764013554 527 DNQSEALVQEALER-LMRGRTVFVVAH 552
Cdd:PRK13538 161 DKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
377-581 |
4.47e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 377 FSLSVRAGETVALVGGSGAGKSTVLNLVIGFIrPTAGRILLDGEDIAGLDLRT---YRRFLSvvPQESILFEGSIRENVS 453
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAElarHRAYLS--QQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 454 -YGMDGEVPDEKIREALAAANALEFVDRMPQGVETvvgargarLSGGQKQR-------LAIARALVRDPRVLVLDEATSA 525
Cdd:PRK03695 92 lHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQ--------LSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 526 LDNQSEAlvqeALERLMR-----GRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:PRK03695 164 LDVAQQA----ALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
377-579 |
5.37e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 377 FSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDI----------AGLDLRTYRRflsvvPQESILFEG 446
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirsprdairAGIMLCPEDR-----KAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 447 SIREN---------------VSYGMDGEVPDEKIREALAaanalefvdRMPQGvETVVGArgarLSGGQKQRLAIARALV 511
Cdd:PRK11288 347 SVADNinisarrhhlragclINNRWEAENADRFIRSLNI---------KTPSR-EQLIMN----LSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 512 RDPRVLVLDEATSALDNQSEALVQEALERLM-RGRTVFVVAHRL-STIQDADRIVVMERGRLVEVGTHEE 579
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELAaQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
39-241 |
6.26e-13 |
|
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: 69.44 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 39 LTLAVLVFAVKHIPVWLLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRTGTELRGALCH 118
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 119 RMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIG-FQAPVALPLFIVVVPLAALLVRSL 197
Cdd:cd18546 81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLvLDPRLALVALAALPPLALATRWFR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2764013554 198 RGRIRADNEAfRVEVEQLSARVGEMTTLIPITRAHALERTALRR 241
Cdd:cd18546 161 RRSSRAYRRA-RERIAAVNADLQETLAGIRVVQAFRRERRNAER 203
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
374-569 |
7.11e-13 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 71.80 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGfiRPTAGRIllDGE-DIAGLDLR--TYRRFLSVVPQESILF-EGSIR 449
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--EGDiRISGFPKKqeTFARISGYCEQNDIHSpQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVSYGMDGEVP-----DEKIRealaaanaleFVDRMPQGVE------TVVGARGAR-LSGGQKQRLAIARALVRDPRVL 517
Cdd:PLN03140 972 ESLIYSAFLRLPkevskEEKMM----------FVDEVMELVEldnlkdAIVGLPGVTgLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 518 VLDEATSALDNQSEALVQEALERLM-RGRTVFVVAHRLST-IQDA-DRIVVMERG 569
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVdTGRTVVCTIHQPSIdIFEAfDELLLMKRG 1096
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
373-591 |
8.29e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.04 E-value: 8.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 373 SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEdiagLDLRTYRRFLSVVPQE------------ 440
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKM----LLRRRSRQVIELSEQSaaqmrhvrgadm 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 441 SILFEGSIRENVSYGMDGEVPDEKIREALAAANALEFVD--------RMPQGvETVVGARGARLSGGQKQRLAIARALVR 512
Cdd:PRK10261 107 AMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEakrmldqvRIPEA-QTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 513 DPRVLVLDEATSALDNQSEALVQEALERLMRGRT--VFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELL-AGTGPYA 588
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFhAPQHPYT 265
|
...
gi 2764013554 589 TTL 591
Cdd:PRK10261 266 RAL 268
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
348-574 |
9.42e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 9.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 348 RDAGEVTGTFtfdevGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFI--RPTAGRIlldgediagl 425
Cdd:COG2401 25 ERVAIVLEAF-----GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 426 dlrtyrrflsVVPQESILFEGSIRENVsyGMDGEVPDEKirealaaanalefvdrmpqGVETVVG--------ARGARLS 497
Cdd:COG2401 90 ----------DVPDNQFGREASLIDAI--GRKGDFKDAV-------------------ELLNAVGlsdavlwlRRFKELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 498 GGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHR---LSTIQDaDRIVVMERGRLV 572
Cdd:COG2401 139 TGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARraGITLVVATHHydvIDDLQP-DLLIFVGYGGVP 217
|
..
gi 2764013554 573 EV 574
Cdd:COG2401 218 EE 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
334-552 |
1.29e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.75 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 334 EVLQAPDLEVNEGKRDAGEVtgtFTFDEVGFRYPDaaEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAG 413
Cdd:PRK11147 300 EVMGTAKMQVEEASRSGKIV---FEMENVNYQIDG--KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 414 RILLDGE-DIAGLDlrTYRRFL----SVV------PQEsILFEGSIRENVSYGMDGEVPdekirealaaanalefvdrmP 482
Cdd:PRK11147 375 RIHCGTKlEVAYFD--QHRAELdpekTVMdnlaegKQE-VMVNGRPRHVLGYLQDFLFH--------------------P 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 483 QGVETVVGArgarLSGGQKQRLAIARALVRDPRVLVLDEATSALDnqSEALvqEALERLMRGR--TVFVVAH 552
Cdd:PRK11147 432 KRAMTPVKA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLD--VETL--ELLEELLDSYqgTVLLVSH 495
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
378-576 |
1.45e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 378 SLSVRAGETVALVGGSGAGKSTVLNLVIGfIRPTA---GRILLDGEDIAGLDLR-TYRRFLSVVPQESILFEG-SIRENV 452
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFEGEELQASNIRdTERAGIAIIHQELALVKElSVLENI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 SYGMD----GEVPDEKI--REALAAANALEFVDrmpqgVETVVGargaRLSGGQKQRLAIARALVRDPRVLVLDEATSAL 526
Cdd:PRK13549 104 FLGNEitpgGIMDYDAMylRAQKLLAQLKLDIN-----PATPVG----NLGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 527 DNQSEALVQEALERLM-RGRTVFVVAHRLSTIQD-ADRIVVMERGRlvEVGT 576
Cdd:PRK13549 175 TESETAVLLDIIRDLKaHGIACIYISHKLNEVKAiSDTICVIRDGR--HIGT 224
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
55-305 |
1.94e-12 |
|
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: 68.18 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 55 LLPLVTARIID--IVVDHKPVSALWWNTAAVLVVLL----LNYPLHMYFSKLSSLAIRRtgteLRGALCHRMQHLSIGYH 128
Cdd:cd18544 17 LGPLLIKRAIDdyIVPGQGDLQGLLLLALLYLGLLLlsflLQYLQTYLLQKLGQRIIYD----LRRDLFSHIQRLPLSFF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 129 SRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGF-QAPVALpLFIVVVPLAALLVRSLRGRIRADNEA 207
Cdd:cd18544 93 DRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLlNWRLAL-ISLLVLPLLLLATYLFRKKSRKAYRE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 208 FRVEVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILLNVmAVAflsgsALVAY 287
Cdd:cd18544 172 VREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSL-ALA-----LVLWY 245
|
250 260
....*....|....*....|....*.
gi 2764013554 288 YGLF----GISPGDVVM----ISTFF 305
Cdd:cd18544 246 GGGQvlsgAVTLGVLYAfiqyIQRFF 271
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
374-591 |
2.38e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.15 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRR--FLSvvpQE-SILFEGSIRE 450
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRvgYMS---QAfSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 451 NVS-----YGMdgevPDEKIREAlaaanalefVDRMPQ--GVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEAT 523
Cdd:NF033858 359 NLElharlFHL----PAAEIAAR---------VAEMLErfDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2764013554 524 S-----ALDNQSEALVQeaLERlMRGRTVFVVAHRLSTIQDADRIVVMERGRLVEVGTHEELLAGTGpyATTL 591
Cdd:NF033858 426 SgvdpvARDMFWRLLIE--LSR-EDGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAARG--AATL 493
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
361-561 |
2.61e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.13 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 361 EVGFRYPDaaEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGlDLRTYRRFLSVVPQE 440
Cdd:PRK13540 6 ELDFDYHD--QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 441 S-ILFEGSIRENVSYGMDGEVPDEKIREALAAANALEFVDrMPQGVetvvgargarLSGGQKQRLAIARALVRDPRVLVL 519
Cdd:PRK13540 83 SgINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2764013554 520 DEATSALDNQS-EALVQEALERLMRGRTVFVVAHRLSTIQDAD 561
Cdd:PRK13540 152 DEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
364-591 |
3.08e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.91 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 364 FRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGF----IRPTAGRILLDGEDIAGLDLRTYRRF----LS 435
Cdd:PRK15093 13 FKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKLvghnVS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 436 VVPQE--SILfegSIRENVSYGMDGEVPDEKIREALAAAnaleFVDRMPQGVETV--VGARGAR---------LSGGQKQ 502
Cdd:PRK15093 93 MIFQEpqSCL---DPSERVGRQLMQNIPGWTYKGRWWQR----FGWRKRRAIELLhrVGIKDHKdamrsfpyeLTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 503 RLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR--GRTVFVVAHRLSTI-QDADRIVVMERGRLVEVGTHEE 579
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQTVETAPSKE 245
|
250
....*....|...
gi 2764013554 580 LL-AGTGPYATTL 591
Cdd:PRK15093 246 LVtTPHHPYTQAL 258
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
361-567 |
3.59e-12 |
|
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: 69.04 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 361 EVGFRYPDAaEHSVRDFSLSV-----RAGETVALVGGSGAGKSTvlnlvigFIRPTAGRILLDGEDIAGlDLRtyrrfLS 435
Cdd:COG1245 339 ETLVEYPDL-TKSYGGFSLEVeggeiREGEVLGIVGPNGIGKTT-------FAKILAGVLKPDEGEVDE-DLK-----IS 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 436 VVPQE-SILFEGSIRENVSYGMDGEVPDEKIREAlaaanaleFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDP 514
Cdd:COG1245 405 YKPQYiSPDYDGTVEEFLRSANTDDFGSSYYKTE--------IIKPL--GLEKLLDKNVKDLSGGELQRVAIAACLSRDA 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEALERLM--RGRTVFVVAHRLsTIQD--ADRIVVME 567
Cdd:COG1245 475 DLYLLDEPSAHLDVEQRLAVAKAIRRFAenRGKTAMVVDHDI-YLIDyiSDRLMVFE 530
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
378-576 |
4.52e-12 |
|
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: 68.70 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 378 SLSVRAGETVALVGGSGAGKSTVLNLVIGfIRPTA---GRILLDGEDIAGLDLR-TYRRFLSVVPQESILF-EGSIRENV 452
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVpELSVAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 SYGMD-----GEVPDEKIREALAAANALEFVDRMPqgVETVVGARGarlsGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:TIGR02633 100 FLGNEitlpgGRMAYNAMYLRAKNLLRELQLDADN--VTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSLT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 528 NQSEALVQEALERL-MRGRTVFVVAHRLSTIQD-ADRIVVMERGRlvEVGT 576
Cdd:TIGR02633 174 EKETEILLDIIRDLkAHGVACVYISHKLNEVKAvCDTICVIRDGQ--HVAT 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
376-567 |
5.58e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSV-----RAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDgediagldLRtyrrfLSVVPQE-SILFEGSIR 449
Cdd:PRK13409 352 DFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--------LK-----ISYKPQYiKPDYDGTVE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVSygmdgEVPD---------EKIRealaaanalefvdrmPQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLD 520
Cdd:PRK13409 419 DLLR-----SITDdlgssyyksEIIK---------------PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLD 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 521 EATSALDNQSEALVQEALERLMRGR--TVFVVAHRLsTIQD--ADRIVVME 567
Cdd:PRK13409 479 EPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDI-YMIDyiSDRLMVFE 528
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
375-571 |
6.27e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRT-YRRFLSVVP---QESILF-EGSIR 449
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYlDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVSYGMDGEVP-------DEKIREALAAANALEFVDrMPQGVETvvgargarLSGGQKQRLAIARALVRDPRVLVLDEA 522
Cdd:PRK15439 360 WNVCALTHNRRGfwikparENAVLERYRRALNIKFNH-AEQAART--------LSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 523 TSALDNQSEALVQEALERLM-RGRTVFVVAHRLSTI-QDADRIVVMERGRL 571
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAaQNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
375-581 |
1.06e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPQESIL-FEGSIRENVS 453
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 454 YGMDGEVP------DEKIREALAAANALEFVDRMPQGVETvvgargarLSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:PRK10253 104 RGRYPHQPlftrwrKEDEEAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 528 NQSEALVQEALERLMR--GRTVFVVAHRLS-TIQDADRIVVMERGRLVEVGTHEELL 581
Cdd:PRK10253 176 ISHQIDLLELLSELNRekGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
384-582 |
1.44e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.21 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 384 GETVALVGGSGAGKSTVLNLVIGFIRPT--AGRILLDGEDIAGldlRTYRRfLSVVPQESILFEG-SIRENVSYGMDGEV 460
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK---QILKR-TGFVTQDDILYPHlTVRETLVFCSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 461 P-----DEKIREALAAANALEfvdrMPQGVETVVGARGAR-LSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSE-AL 533
Cdd:PLN03211 170 PksltkQEKILVAESVISELG----LTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRL 245
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 534 VQEALERLMRGRTVFVVAHRLST--IQDADRIVVMERGRLVEVGTHEELLA 582
Cdd:PLN03211 246 VLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
350-595 |
1.48e-11 |
|
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: 67.73 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 350 AGEVTGTFTFDEVGFRYPDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAgLDLRT 429
Cdd:TIGR01257 1931 GGNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISD 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 430 YRRFLSVVPQ-ESI--LFEGsiRENVS-YGMDGEVPDEKIREAL----AAANALEFVDRMpqgvetvvgarGARLSGGQK 501
Cdd:TIGR01257 2010 VHQNMGYCPQfDAIddLLTG--REHLYlYARLRGVPAEEIEKVAnwsiQSLGLSLYADRL-----------AGTYSGGNK 2076
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 502 QRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR-GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEE 579
Cdd:TIGR01257 2077 RKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIReGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQH 2156
|
250
....*....|....*..
gi 2764013554 580 LLAGTGP-YATTLQPRA 595
Cdd:TIGR01257 2157 LKSKFGDgYIVTMKIKS 2173
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
376-573 |
1.48e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.74 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAGETVALVGGSGAGKSTVLNLVIGfIRPTA---GRILLDGEDIAGLDLRTYRRF--------LSVVPQESI-- 442
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHGsyeGEILFDGEVCRFKDIRDSEALgiviihqeLALIPYLSIae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 443 -LFEGSirENVSYG-MD-----------------GEVPDEKIREAlaaanalefvdrmpqGVetvvgargarlsgGQKQR 503
Cdd:NF040905 98 nIFLGN--ERAKRGvIDwnetnrrarellakvglDESPDTLVTDI---------------GV-------------GKQQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 504 LAIARALVRDPRVLVLDEATSAL-DNQSEALVQEALERLMRGRTVFVVAHRLSTI-QDADRIVVMERGRLVE 573
Cdd:NF040905 148 VEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
384-570 |
1.67e-11 |
|
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: 62.39 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 384 GETVALVGGSGAGKSTVLNLVIGFIRPTAGR-ILLDGEDIAGLDLRtyrrflsvvpqesilfegsirenvsygmdgevpd 462
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLD---------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 463 ekirealaaanalefvdrmpQGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLM 542
Cdd:smart00382 48 --------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2764013554 543 -------RGRTVFVVAHRLSTIQDA------DRIVVMERGR 570
Cdd:smart00382 108 llllkseKNLTVILTTNDEKDLGPAllrrrfDRRIVLLLIL 148
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
379-573 |
1.99e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.03 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 379 LSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLD------LRTyrRFLSVVPQESILFEG-SIREN 451
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearakLRA--KHVGFVFQSFMLIPTlNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 452 VSY-----GMDGEVPDEKIREALAAANALEFVDRMPqgvetvvgargARLSGGQKQRLAIARALVRDPRVLVLDEATSAL 526
Cdd:PRK10584 109 VELpallrGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2764013554 527 DNQSEALVQEALERLMR--GRTVFVVAHRLSTIQDADRIVVMERGRLVE 573
Cdd:PRK10584 178 DRQTGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
41-298 |
2.26e-11 |
|
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: 64.80 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 41 LAVLVFAVKHIpvwLLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLNyplhMYFSKLSSLAIRRTGT----ELRGAL 116
Cdd:cd18545 7 LLMLLSTAASL---AGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVN----WVASRLRIYLMAKVGQrilyDLRQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 117 CHRMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLgGLAVIGFQAPVALPLF-IVVVPLAALLVR 195
Cdd:cd18545 80 FSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLV-GIVIIMFSLNVRLALVtLAVLPLLVLVVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 196 SLRGRIRADNEAFRVEVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAgfrlDMLGGRFGSLSWILLNVMA 275
Cdd:cd18545 159 LLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKA----NMRAVRLNALFWPLVELIS 234
|
250 260
....*....|....*....|...
gi 2764013554 276 VAflsGSALVAYYGLFGISPGDV 298
Cdd:cd18545 235 AL---GTALVYWYGGKLVLGGAI 254
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
379-572 |
2.47e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 379 LSVRAGETVALVGGSGAGKSTVLNLVigfirptAGRILLD-GEDIAGLDLRTYRrfLSVVPQESIlfEGSIRENVSYGM- 456
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQDLIVAR--LQQDPPRNV--EGTVYDFVAEGIe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 457 -DGEV--------------PDEK-------IREALAAANALEFVDRMPQGVETV---VGARGARLSGGQKQRLAIARALV 511
Cdd:PRK11147 93 eQAEYlkryhdishlvetdPSEKnlnelakLQEQLDHHNLWQLENRINEVLAQLgldPDAALSSLSGGWLRKAALGRALV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 512 RDPRVLVLDEATSALDNQSealvQEALERLM---RGRTVFvVAHRLSTIQD-ADRIVVMERGRLV 572
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIET----IEWLEGFLktfQGSIIF-ISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
374-579 |
4.78e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIA----------GLDLRTYRRflsvvpQESIL 443
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavkkGMAYITESR------RDNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 444 FEG-SIRENVSYGmdgevpdEKIREALAAANALEFVDRMPQGVetvvgARGAR----------------LSGGQKQRLAI 506
Cdd:PRK09700 353 FPNfSIAQNMAIS-------RSLKDGGYKGAMGLFHEVDEQRT-----AENQRellalkchsvnqniteLSGGNQQKVLI 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 507 ARALVRDPRVLVLDEATSALDNQSEALVQEALERLM-RGRTVFVVAHRLSTIQDA-DRIVVMERGRLVEVGTHEE 579
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQILTNRD 495
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
378-572 |
7.81e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 378 SLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDI----------AGldlrtyrrfLSVVPQE-SILFEG 446
Cdd:PRK10762 24 ALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqeAG---------IGIIHQElNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 447 SIRENVSYGMDGEVPDEKIREALAAANALEFVDRM--PQGVETVVGargaRLSGGQKQRLAIARALVRDPRVLVLDEATS 524
Cdd:PRK10762 95 TIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLnlRFSSDKLVG----ELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2764013554 525 AL-DNQSEALVQEALERLMRGRTVFVVAHRLSTI-QDADRIVVMERGRLV 572
Cdd:PRK10762 171 ALtDTETESLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDGQFI 220
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
57-318 |
8.07e-11 |
|
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: 63.27 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 57 PLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRTGTELRGALCHRMQHLSIGYHSRVSAEVL 136
Cdd:cd18550 19 PLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 137 QTKVVRDVDALETM----LQQTAQNGLGAVMTLLG------GLAVIGFqapVALPLFIVVVPLAALLVRSLRGRIRADNe 206
Cdd:cd18550 99 QSRLNNDVGGAQSVvtgtLTSVVSNVVTLVATLVAmlaldwRLALLSL---VLLPLFVLPTRRVGRRRRKLTREQQEKL- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 207 afrvevEQLSARVGEmtTL----IPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSlswillnVMAVAFLSGS 282
Cdd:cd18550 175 ------AELNSIMQE--TLsvsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFA-------ALGLFTAIGP 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2764013554 283 ALVAYYG-----LFGISPGDVVMISTFFTGLTASLTALLNL 318
Cdd:cd18550 240 ALVYWVGgllviGGGLTIGTLVAFTALLGRLYGPLTQLLNI 280
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-289 |
9.87e-11 |
|
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: 62.91 E-value: 9.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 39 LTLAVLVFAVKHIPvwllPLVTARIIDIVVD----HKPVSALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRTGTELRG 114
Cdd:cd18563 5 FLLMLLGTALGLVP----PYLTKILIDDVLIqlgpGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 115 ALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLgGLAVIGFQAPVALPLFIVV-VPLAALL 193
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMII-GIGVVLFSLNWKLALLVLIpVPLVVWG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 194 VRSLRGRIRADNEAFRVEVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILLNV 273
Cdd:cd18563 160 SYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSL 239
|
250
....*....|....*.
gi 2764013554 274 mavaflsGSALVAYYG 289
Cdd:cd18563 240 -------GTLIVWYFG 248
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
377-566 |
1.19e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 377 FSL----SVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRilLDGED--------IAGLDLRTYRRFLS-----VV-- 437
Cdd:PRK13409 88 FKLyglpIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEPswdevlkrFRGTELQNYFKKLYngeikVVhk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 PQ--ESI--LFEGSIRENVS----YGMDGEVpdekirealaaanalefVDRMpqGVETVVGARGARLSGGQKQRLAIARA 509
Cdd:PRK13409 166 PQyvDLIpkVFKGKVRELLKkvdeRGKLDEV-----------------VERL--GLENILDRDISELSGGELQRVAIAAA 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 510 LVRDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLsTIQD--ADRIVVM 566
Cdd:PRK13409 227 LLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL-AVLDylADNVHIA 284
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
374-572 |
1.32e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.12 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVL----NLVIGFIRPTaGRILLDGEDIAGlDLRTYRRFLSVVPQESILF-EGSI 448
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLkalaNRTEGNVSVE-GDIHYNGIPYKE-FAEKYPGEIIYVSEEDVHFpTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 449 RENVSygmdgevpdekirealaaanaleFVDRMpQGVETVvgaRGarLSGGQKQRLAIARALVRDPRVLVLDEATSALDN 528
Cdd:cd03233 101 RETLD-----------------------FALRC-KGNEFV---RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 529 QSealvqeALERLMRGRTvfvVAH--RLSTI----QDA-------DRIVVMERGRLV 572
Cdd:cd03233 152 ST------ALEILKCIRT---MADvlKTTTFvslyQASdeiydlfDKVLVLYEGRQI 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
376-554 |
1.49e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.05 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 376 DFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEdiagldLRtyrrfLSVVPQEsILFEGSIRENVSYG 455
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------LR-----IGYVPQK-LYLDTTLPLTVNRF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 456 MdgevpdeKIREALAAANALEFVDRMPQGveTVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQ 535
Cdd:PRK09544 90 L-------RLRPGTKKEDILPALKRVQAG--HLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170 180
....*....|....*....|.
gi 2764013554 536 EALERLMR--GRTVFVVAHRL 554
Cdd:PRK09544 161 DLIDQLRRelDCAVLMVSHDL 181
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
373-591 |
3.74e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 61.68 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 373 SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFI----RPTAGRILLDGEDIAGLDLRTYRRFlsVVPQESILFEGSI 448
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERRNL--VGAEVAMIFQDPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 449 RE-NVSYGMDGEVPdEKIREALAAANALefvdRMPQGVE--TVVG--ARGAR-------LSGGQKQRLAIARALVRDPRV 516
Cdd:PRK11022 100 TSlNPCYTVGFQIM-EAIKVHQGGNKKT----RRQRAIDllNQVGipDPASRldvyphqLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 517 LVLDEATSALDNQSEALVQEALERLMRGR--TVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELL-AGTGPYATTL 591
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIFrAPRHPYTQAL 253
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
382-566 |
4.12e-10 |
|
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: 62.49 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 382 RAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRIL--LDGEDI----AGLDLRTYRRFLSvvpqesilfEGSIR------ 449
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeePSWDEVlkrfRGTELQDYFKKLA---------NGEIKvahkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 --ENVSYGMDGEVPD--EKI--REALAAanaleFVDRMpqGVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEAT 523
Cdd:COG1245 168 yvDLIPKVFKGTVREllEKVdeRGKLDE-----LAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2764013554 524 SALD-----NQSEaLVQEALErlmRGRTVFVVAHRLsTIQD--ADRIVVM 566
Cdd:COG1245 241 SYLDiyqrlNVAR-LIRELAE---EGKYVLVVEHDL-AILDylADYVHIL 285
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
303-555 |
4.57e-10 |
|
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: 62.46 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 303 TFFTGLTASLTALLNLMPIVSRGLESVRSVGEVLQAPDLEVN-EGKRDAGEVTGTFT---FDEVGFRYPdAAEHSVRDFS 378
Cdd:TIGR00954 394 TRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNsNLVPGRGIVEYQDNgikFENIPLVTP-NGDVLIESLS 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 379 LSVRAGETVALVGGSGAGKSTvLNLVIGFIRPTAGRILLDGEDIAgldlrtyrrfLSVVPQESILFEGSIRENVSYGMDg 458
Cdd:TIGR00954 473 FEVPSGNNLLICGPNGCGKSS-LFRILGELWPVYGGRLTKPAKGK----------LFYVPQRPYMTLGTLRDQIIYPDS- 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 459 evPDEKIREALAAANALEFVDRMPQG--VETVVGARGAR-----LSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSE 531
Cdd:TIGR00954 541 --SEDMKRRGLSDKDLEQILDNVQLThiLEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE 618
|
250 260
....*....|....*....|....
gi 2764013554 532 ALVQEALERLmrGRTVFVVAHRLS 555
Cdd:TIGR00954 619 GYMYRLCREF--GITLFSVSHRKS 640
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
55-330 |
4.68e-10 |
|
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: 60.88 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 55 LLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRTGTELRGALCHRMQHLSIGYHSRVSAE 134
Cdd:cd18548 17 LLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 135 VLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVALPLFIVVVPLAALLVRSLRGRIRADNEAFRVEVEQ 214
Cdd:cd18548 97 SLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 215 LSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILLNVMAVAFL-SGSALVAYYGLfgi 293
Cdd:cd18548 177 LNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILwFGGHLINAGSL--- 253
|
250 260 270
....*....|....*....|....*....|....*..
gi 2764013554 294 SPGDVVMISTFFTGLTASLTALLNLMPIVSRGLESVR 330
Cdd:cd18548 254 QVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAK 290
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
374-582 |
4.72e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAgldlrtyrrflSVVPQESI----------- 442
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV-----------TRSPQDGLangivyisedr 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 443 -----LFEGSIRENVSYGMDGEVPDE--KIREALAAANALEFVD----RMPqGVETVVGargaRLSGGQKQRLAIARALV 511
Cdd:PRK10762 337 krdglVLGMSVKENMSLTALRYFSRAggSLKHADEQQAVSDFIRlfniKTP-SMEQAIG----LLSGGNQQKVAIARGLM 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 512 RDPRVLVLDEATSALD-----------NQSEAlvqealerlmRGRTVFVVAHRLSTIQD-ADRIVVMERGRL-----VEV 574
Cdd:PRK10762 412 TRPKVLILDEPTRGVDvgakkeiyqliNQFKA----------EGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQ 481
|
....*...
gi 2764013554 575 GTHEELLA 582
Cdd:PRK10762 482 ATQEKLMA 489
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
360-555 |
8.96e-10 |
|
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: 59.69 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 360 DEVGFRYpdaAEHSVRDFSLSV-RAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRilLDGED--------IAGLDLRTY 430
Cdd:cd03236 4 DEPVHRY---GPNSFKLHRLPVpREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeildeFRGSELQNY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 431 RRFL-------SVVPQESIL----FEGSIRENVSYGMDGEVPDEkirealaaanaleFVDRMpqGVETVVGARGARLSGG 499
Cdd:cd03236 79 FTKLlegdvkvIVKPQYVDLipkaVKGKVGELLKKKDERGKLDE-------------LVDQL--ELRHVLDRNIDQLSGG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 500 QKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR-GRTVFVVAHRLS 555
Cdd:cd03236 144 ELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLA 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
374-571 |
1.21e-09 |
|
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: 60.99 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIG-FIRPTAGRILLDGEDIaglDLRT----YRRFLSVVPQE----SILF 444
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPV---DIRNpaqaIRAGIAMVPEDrkrhGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 445 EGSIRENV------SYGMDGEVPDEK----IREALAAANALEFVDRMPQGvetvvgargaRLSGGQKQRLAIARALVRDP 514
Cdd:TIGR02633 353 ILGVGKNItlsvlkSFCFKMRIDAAAelqiIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 515 RVLVLDEATSALDNQSEALVQEALERLMR-GRTVFVVAHRLSTIQD-ADRIVVMERGRL 571
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQLAQeGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
372-581 |
1.34e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.06 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 372 HSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEdiagldlrtyrrfLSVVPQESILfEGSIR-- 449
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------VSVIAISAGL-SGQLTgi 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 450 ENVSYGM--DGEVPDEKIREALAAANALEFVDRMPQGVEtvvgargaRLSGGQKQRLAIARALVRDPRVLVLDEATSALD 527
Cdd:PRK13546 104 ENIEFKMlcMGFKRKEIKAMTPKIIEFSELGEFIYQPVK--------KYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 528 nqsEALVQEALERLM----RGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELL 581
Cdd:PRK13546 176 ---QTFAQKCLDKIYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVL 231
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
381-544 |
2.22e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 381 VRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAGLDLRTYRRFLSVVPqeSILFEGSIRENVSY--GMDG 458
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLP--GLKADLSTLENLHFlcGLHG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 459 EVPdekirealaaanalefvDRMPQGVETVVGARG------ARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEA 532
Cdd:PRK13543 112 RRA-----------------KQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGIT 174
|
170
....*....|..
gi 2764013554 533 LVQEALERLMRG 544
Cdd:PRK13543 175 LVNRMISAHLRG 186
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
367-575 |
4.80e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 55.79 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 367 PDAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNlvigfirptagrilldgEDIAGLDLRTYRRFLSVVPQESILFEG 446
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------------EGLYASGKARLISFLPKFSRNKLIFID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 447 SIRENVSYGMdGEVPdekirealaaanalefvdrmpqgvetvVGARGARLSGGQKQRLAIARAL-VRDPRVL-VLDEATS 524
Cdd:cd03238 67 QLQFLIDVGL-GYLT---------------------------LGQKLSTLSGGELQRVKLASELfSEPPGTLfILDEPST 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 525 ALDNQSEALVQEALERLM-RGRTVFVVAHRLSTIQDADRIVVM------ERGRLVEVG 575
Cdd:cd03238 119 GLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
55-318 |
5.37e-09 |
|
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: 57.49 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 55 LLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRTGTELRGALCHRMQHLSIGYH------ 128
Cdd:cd18576 14 VFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFherrvg 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 129 ---SRVSAevlqtkvvrDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVALPLFIVVVPLAALLVRSLRGRIRADN 205
Cdd:cd18576 94 eltSRLSN---------DVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 206 EAFRVEVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSlswillnVMAVAFLSGSALV 285
Cdd:cd18576 165 KKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSS-------FIIFLLFGAIVAV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2764013554 286 AYYGLF-----GISPGDVV--MISTFFtgLTASLTALLNL 318
Cdd:cd18576 238 LWYGGRlvlagELTAGDLVafLLYTLF--IAGSIGSLADL 275
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
375-585 |
1.98e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 375 RDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRI-LLDGEDIAGLDLRTYRRFlsvvPQESILFEGsirenVS 453
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYAQDHAYDF----ENDLTLFDW-----MS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 454 YGMDGEVPDEKIREalaaanaleFVDRMPQGVETVvgARGAR-LSGGQKQRLAIARALVRDPRVLVLDEATSALDNQS-E 531
Cdd:PRK15064 407 QWRQEGDDEQAVRG---------TLGRLLFSQDDI--KKSVKvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESiE 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2764013554 532 ALvQEALErLMRGRTVFVVAHR--LSTIqdADRIVVMERGRLVEV-GTHEELLAGTG 585
Cdd:PRK15064 476 SL-NMALE-KYEGTLIFVSHDRefVSSL--ATRIIEITPDGVVDFsGTYEEYLRSQG 528
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
379-572 |
2.32e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 379 LSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIaglDLRTYRRFL----SVVPQE-SILFEGSIRENV- 452
Cdd:PRK10982 19 LKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI---DFKSSKEALengiSMVHQElNLVLQRSVMDNMw 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 453 --SYGMDGEVPDE-KIREALAAANALEFVDRMPQgvetvvgARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQ 529
Cdd:PRK10982 96 lgRYPTKGMFVDQdKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2764013554 530 SEALVQEALERLM-RGRTVFVVAHRLSTI-QDADRIVVMERGRLV 572
Cdd:PRK10982 169 EVNHLFTIIRKLKeRGCGIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
55-304 |
2.87e-08 |
|
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: 55.52 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 55 LLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRTGTELRGALCHRMQHLSIGYHSRVSAE 134
Cdd:cd18542 17 LIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 135 VLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQ-APVALpLFIVVVPLAALLVRSLRGRIRAdneAFrvevE 213
Cdd:cd18542 97 DLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSInWKLTL-ISLAIIPFIALFSYVFFKKVRP---AF----E 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 214 QLSARVGEMTTLIP--IT-----RAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILLNVMavaflsgSALVA 286
Cdd:cd18542 169 EIREQEGELNTVLQenLTgvrvvKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQ-------IVLVL 241
|
250 260
....*....|....*....|...
gi 2764013554 287 YYGLF-----GISPGDVVMISTF 304
Cdd:cd18542 242 WVGGYlvingEITLGELVAFISY 264
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
490-593 |
2.88e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 490 GARGARLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR-GRTVFVVAHRLSTI-QDADRIVVME 567
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAeQLAHELTVID 218
|
90 100
....*....|....*....|....*.
gi 2764013554 568 RGRLVEVGTHEELLAGTGPYATTLQP 593
Cdd:NF000106 219 RGRVIADGKVDELKTKVGGRTLQIRP 244
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
366-567 |
3.12e-08 |
|
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: 53.73 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 366 YPDAAeHSVRDFSLSVRA-----GETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIAgldlrtYRrflsvvpqe 440
Cdd:cd03222 3 YPDCV-KRYGVFFLLVELgvvkeGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------YK--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 441 silfegsirenvsygmdgevpdekirealaaanalefvdrmPQGVEtvvgargarLSGGQKQRLAIARALVRDPRVLVLD 520
Cdd:cd03222 67 -----------------------------------------PQYID---------LSGGELQRVAIAAALLRNATFYLFD 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2764013554 521 EATSALDNQSEALVQEALERL-MRG-RTVFVVAHRLSTIQD-ADRIVVME 567
Cdd:cd03222 97 EPSAYLDIEQRLNAARAIRRLsEEGkKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-332 |
4.00e-08 |
|
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: 55.24 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 39 LTLAVLVFavkhipvwllPLVTARIIDIV-VDHKPVSALWWnTAAVLVVL-----LLNYpLHMYFSKLSSLAIRRtgtEL 112
Cdd:cd18778 11 STLLGLVP----------PWLIRELVDLVtIGSKSLGLLLG-LALLLLGAyllraLLNF-LRIYLNHVAEQKVVA---DL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 113 RGALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLgGLAVIGFQAPVALPLF-IVVVPLAA 191
Cdd:cd18778 76 RSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLV-GVAIILFSINPKLALLtLIPIPFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 192 LLVRSLRGRIRadnEAFRveveQLSARVGEMTTL-------IPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFG 264
Cdd:cd18778 155 LGAWLYSKKVR---PRYR----KVREALGELNALlqdnlsgIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFH 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 265 SLswillnvmaVAFLS--GSALVAYYG----LFG-ISPGDVVMISTFFTGLTASLTALLNLMPIVSRGLESVRSV 332
Cdd:cd18778 228 PL---------MEFLTslGTVLVLGFGgrlvLAGeLTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
55-266 |
5.04e-08 |
|
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: 54.80 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 55 LLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRTGTELRGALCHRMQHLSIGYHSRVSAE 134
Cdd:cd18543 17 AIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 135 VLQTKVVRDVDALETMLQQTAQNgLGAVMTLLGGLAVIGFQAPVALPLFIVVVPLAALLVRSLRGRIRADNEAFRVEVEQ 214
Cdd:cd18543 97 QLLSRATSDLSLVQRFLAFGPFL-LGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2764013554 215 LSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSL 266
Cdd:cd18543 176 LATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPL 227
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
324-571 |
9.46e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 9.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 324 RGLESVRSVGEVLQAPDLEVNEGKRDAGEVTGTFTFDEVGFRYPdAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNL 403
Cdd:PLN03073 476 KALDRLGHVDAVVNDPDYKFEFPTPDDRPGPPIISFSDASFGYP-GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKL 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 404 VIGFIRPTAGRIL--------------LDGEDIAGLDLRTYRRFLSVVPqesilfEGSIRENV-SYGMDGEVPdekirea 468
Cdd:PLN03073 555 ISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSSNPLLYMMRCFPGVP------EQKLRAHLgSFGVTGNLA------- 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 469 laaanalefvdrmPQGVETvvgargarLSGGQKQRLAIARALVRDPRVLVLDEATSALD-NQSEALVQEALerLMRGrTV 547
Cdd:PLN03073 622 -------------LQPMYT--------LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIQGLV--LFQG-GV 677
|
250 260
....*....|....*....|....*
gi 2764013554 548 FVVAHRLSTIQDA-DRIVVMERGRL 571
Cdd:PLN03073 678 LMVSHDEHLISGSvDELWVVSEGKV 702
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
378-582 |
9.65e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 378 SLSVRAGETVALVGGSGAGKSTvlnlvigFIRPTAGR-ILLDGEDIAGLDlRTYRrfLSVVPQESILFEGSIREN---VS 453
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSA-------LARALAGElPLLSGERQSQFS-HITR--LSFEQLQKLVSDEWQRNNtdmLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 454 YGMD--GEVPDEKIREALAAAnalefvDRMPQ-----GVETVVGARGARLSGGQKQRLAIARALVRDPRVLVLDEATSAL 526
Cdd:PRK10938 93 PGEDdtGRTTAEIIQDEVKDP------ARCEQlaqqfGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2764013554 527 DNQSEALVQEALERLMR-GRTVFVVAHRLSTIQD-ADRIVVMERGRLVEVGTHEELLA 582
Cdd:PRK10938 167 DVASRQQLAELLASLHQsGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
373-581 |
1.52e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 373 SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDIA----------GLDLRTY-RRFLSVVPQES 441
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnaneainhGFALVTEeRRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 442 ILFEGSIRENVSY-GMDGEVPDEKIREALAAAnalefVDRM---PQGVETVVGArgarLSGGQKQRLAIARALVRDPRVL 517
Cdd:PRK10982 343 IGFNSLISNIRNYkNKVGLLDNSRMKSDTQWV-----IDSMrvkTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEIL 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2764013554 518 VLDEATSALDNQSE-ALVQEALERLMRGRTVFVVAHRLSTIQD-ADRIVVMERGRLVEV-----GTHEELL 581
Cdd:PRK10982 414 MLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLVAGIvdtktTTQNEIL 484
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
364-558 |
1.61e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 364 FRYPDAAEH-SVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPTAGRILLDGEDI-----AGLDLRtyrrfLSVV 437
Cdd:PRK13545 29 FRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAliaisSGLNGQ-----LTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 438 pqESILFEGsirenVSYGMDGEVPDEKIREALAAANALEFVDrmpQGVETvvgargarLSGGQKQRLAIARALVRDPRVL 517
Cdd:PRK13545 104 --ENIELKG-----LMMGLTKEKIKEIIPEIIEFADIGKFIY---QPVKT--------YSSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2764013554 518 VLDEATSALDnqsEALVQEALERL----MRGRTVFVVAHRLSTIQ 558
Cdd:PRK13545 166 VIDEALSVGD---QTFTKKCLDKMnefkEQGKTIFFISHSLSQVK 207
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
55-285 |
4.27e-07 |
|
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: 51.81 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 55 LLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRTGTELRGALCHRMQHLSIGYHSRVSAE 134
Cdd:cd18566 20 ATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 135 VLQTKvvrdVDALETMLQQTAQNGLGAVMTL------LGGLAVIG----FQAPVALPLFIVVvplAALLVRSLRGRIRAD 204
Cdd:cd18566 100 AHLER----LNSLEQIREFLTGQALLALLDLpfvlifLGLIWYLGgklvLVPLVLLGLFVLV---AILLGPILRRALKER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 205 NEA------FRVEVeqlsarVGEMTTLipitRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILLNVMAVAF 278
Cdd:cd18566 173 SRAderrqnFLIET------LTGIHTI----KAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAV 242
|
....*...
gi 2764013554 279 LS-GSALV 285
Cdd:cd18566 243 VAfGALLV 250
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
374-578 |
5.08e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGfiRP----TAGRILLDGEDIAGLD----------------------- 426
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDLEpeerahlgiflafqypieipgvs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 427 ----LR----TYRRFLSVVPQESILFEGSIRENVSY-GMDgevpdekirealaaanaLEFVDR-MPQGvetvvgargarL 496
Cdd:CHL00131 101 nadfLRlaynSKRKFQGLPELDPLEFLEIINEKLKLvGMD-----------------PSFLSRnVNEG-----------F 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 497 SGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR-GRTVFVVAH--RLSTIQDADRIVVMERGRLVE 573
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTsENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
....*
gi 2764013554 574 VGTHE 578
Cdd:CHL00131 233 TGDAE 237
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
494-571 |
7.20e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 494 ARLSGGQKQRLAIARALVRDPRVLVLDEATSALD--------NQSEALVQEalerlmrGRTVFVVAHRLSTIQD-ADRIV 564
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakyeiyKLINQLVQQ-------GVAIIVISSELPEVLGlSDRVL 476
|
....*..
gi 2764013554 565 VMERGRL 571
Cdd:PRK13549 477 VMHEGKL 483
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
357-572 |
1.89e-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: 50.70 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 357 FTFDEVGFRYPdAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGFIRPtagrilLDGEDIAGLDLRtyrrfLSV 436
Cdd:TIGR03719 5 YTMNRVSKVVP-PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------FNGEARPQPGIK-----VGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 437 VPQESILFEG-SIRENVSYGMdGEVPDEKIREALAAANALEFVDRMP-----QG-VETVVGARGA--------------- 494
Cdd:TIGR03719 73 LPQEPQLDPTkTVRENVEEGV-AEIKDALDRFNEISAKYAEPDADFDklaaeQAeLQEIIDAADAwdldsqleiamdalr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 495 ---------RLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLmRGrTVFVVAHrlstiqdaDR--- 562
Cdd:TIGR03719 152 cppwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH--------DRyfl 221
|
250
....*....|....*.
gi 2764013554 563 ------IVVMERGRLV 572
Cdd:TIGR03719 222 dnvagwILELDRGRGI 237
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
55-261 |
3.59e-06 |
|
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: 48.94 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 55 LLPLVTARIIDIVVDHKPV------SALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRTGTELRGALCHRMQHLSIGYH 128
Cdd:cd18547 17 LGPYLLGKAIDLIIEGLGGgggvdfSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 129 SRVSA-EVLqTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPV-ALpLFIVVVPLAALLVRSLRGRIRADNE 206
Cdd:cd18547 97 DTHSHgDIM-SRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLlTL-IVLVTVPLSLLVTKFIAKRSQKYFR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2764013554 207 AFRVEVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGG 261
Cdd:cd18547 175 KQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSG 229
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
496-561 |
6.34e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 496 LSGGQkQRLA-IARALVRDPRVLVLDEATSALDNQSEALVQEALERLMR-GRT--VFV----------VAHRLSTIQDAD 561
Cdd:PRK10938 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISeGETqlLFVshhaedapacITHRLEFVPDGD 480
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
496-593 |
8.62e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 496 LSGGQKQRLAIARAL---VRDPRVLVLDEATSALDNQS-EALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVM----- 566
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELgpegg 889
|
90 100
....*....|....*....|....*...
gi 2764013554 567 -ERGRLVEVGTHEELLAGTGPYATTLQP 593
Cdd:PRK00635 890 nLGGYLLASCSPEELIHLHTPTAKALRP 917
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
368-578 |
1.08e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 368 DAAEHSVRDFSLSVRAGETVALVGGSGAGKSTVLNLVIG--FIRPTAGRILLDGEDIaglDLRTYRRF----LSVVPQES 441
Cdd:NF040905 270 HPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEV---DVSTVSDAidagLAYVTEDR 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 442 -----ILFEgSIRENVSY-GMDGEVPDEKIREALAAANALEFVDRM----PqGVETVVGargaRLSGGQKQRLAIARALV 511
Cdd:NF040905 347 kgyglNLID-DIKRNITLaNLGKVSRRGVIDENEEIKVAEEYRKKMniktP-SVFQKVG----NLSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 512 RDPRVLVLDEATSALD-----------NQseaLVQEalerlmrGRTVFVVAHRL-STIQDADRIVVMERGRLV-EVGTHE 578
Cdd:NF040905 421 TDPDVLILDEPTRGIDvgakyeiytiiNE---LAAE-------GKGVIVISSELpELLGMCDRIYVMNEGRITgELPREE 490
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
374-577 |
1.19e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.09 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 374 VRDFSLSVRAGETVALVGGSGAGKSTVLNLVIGF--IRPTAGRILLDGEDIagLDLRTYRR-----FLSV-----VPQES 441
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDL--LELSPEDRagegiFMAFqypveIPGVS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 442 ILFEGSIRENVSYGMDGEVP----------DEKIREAlaaanalefvdRMPQGVETVVGARGarLSGGQKQRLAIARALV 511
Cdd:PRK09580 95 NQFFLQTALNAVRSYRGQEPldrfdfqdlmEEKIALL-----------KMPEDLLTRSVNVG--FSGGEKKRNDILQMAV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 512 RDPRVLVLDEATSALDNQSEALVQEALERLMRGRTVFVVAHRLSTIQD---ADRIVVMERGRLVEVGTH 577
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDyikPDYVHVLYQGRIVKSGDF 230
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
84-320 |
1.39e-05 |
|
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: 47.08 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 84 LVVLLLNYpLHMYFSKLSSLairRTGTELRGALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALetmlqqtaQNGLG--- 160
Cdd:cd18577 58 IGSFVLSY-IQTACWTITGE---RQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLI--------QDGIGekl 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 161 -----AVMTLLGGLaVIGF--QAPVALPLFIVVVPLA---ALLVRSLRGRIRADNEAFrvevEQLSARVGEMTTLIPITR 230
Cdd:cd18577 126 glliqSLSTFIAGF-IIAFiySWKLTLVLLATLPLIAivgGIMGKLLSKYTKKEQEAY----AKAGSIAEEALSSIRTVK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 231 AHALERTALRRVDSSLQRVLTAGFRLDML-GGRFGSLSWILLNVMAVAFLSGSALVAYYglfGISPGDVvmISTFFTGLT 309
Cdd:cd18577 201 AFGGEEKEIKRYSKALEKARKAGIKKGLVsGLGLGLLFFIIFAMYALAFWYGSRLVRDG---EISPGDV--LTVFFAVLI 275
|
250
....*....|.
gi 2764013554 310 ASlTALLNLMP 320
Cdd:cd18577 276 GA-FSLGQIAP 285
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
491-587 |
1.87e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.71 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 491 ARGAR-LSGGQKQR--LA--IARALVRdprVL-VLDEATSAL---DNqsEALVqEALERLmR--GRTVFVVAHRLSTIQD 559
Cdd:COG0178 480 DRSAGtLSGGEAQRirLAtqIGSGLVG---VLyVLDEPSIGLhqrDN--DRLI-ETLKRL-RdlGNTVIVVEHDEDTIRA 552
|
90 100 110
....*....|....*....|....*....|....*...
gi 2764013554 560 ADRIVVM-----ER-GRLVEVGTHEELLAG----TGPY 587
Cdd:COG0178 553 ADYIIDIgpgagEHgGEVVAQGTPEEILKNpdslTGQY 590
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
496-580 |
1.97e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.70 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 496 LSGGQKQRLAIARALVRD---PRVLVLDEATSALDNQSEALVQEALERLM-RGRTVFVVAHRLSTIQDADRIVVM----- 566
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVdKGNTVVVIEHNLDVIKTADYIIDLgpegg 909
|
90
....*....|....*
gi 2764013554 567 ER-GRLVEVGTHEEL 580
Cdd:TIGR00630 910 DGgGTVVASGTPEEV 924
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
361-575 |
3.11e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 361 EVGFRYPDAAEHSV-----RDFSLSVRAGETVALVGGSGAGKSTVLNLV----IGFIRPTAGRILLDGedIAGLDLRTYR 431
Cdd:TIGR00956 59 TRGFRKLKKFRDTKtfdilKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDG--ITPEEIKKHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 432 RFLSV--------VP----QESILFEGSIR--ENVSYGMDGEVPDEKIREALAAANAlefvdrMPQGVETVVG---ARGa 494
Cdd:TIGR00956 137 RGDVVynaetdvhFPhltvGETLDFAARCKtpQNRPDGVSREEYAKHIADVYMATYG------LSHTRNTKVGndfVRG- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 495 rLSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSealvqeALE--RLMRGRTVFVVAHRLSTI----QDA----DRIV 564
Cdd:TIGR00956 210 -VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT------ALEfiRALKTSANILDTTPLVAIyqcsQDAyelfDKVI 282
|
250
....*....|.
gi 2764013554 565 VMERGRLVEVG 575
Cdd:TIGR00956 283 VLYEGYQIYFG 293
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
491-587 |
8.54e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 491 ARGAR-LSGGQKQRLAIAR----ALVRdprVL-VLDEATSALDNQSEALVQEALERLMR-GRTVFVVAHRLSTIQDADRI 563
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATqigsGLTG---VLyVLDEPSIGLHQRDNRRLINTLKRLRDlGNTLIVVEHDEDTIRAADYV 559
|
90 100 110
....*....|....*....|....*....|....
gi 2764013554 564 VVM------ERGRLVEVGTHEELLAG----TGPY 587
Cdd:TIGR00630 560 IDIgpgageHGGEVVASGTPEEILANpdslTGQY 593
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
57-319 |
9.00e-05 |
|
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: 44.86 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 57 PLVTARIIDIVV-----DHKPVSALWWNTAA------VLVVLLLNYPLHMYFSKLSSLAIRRTGT----ELRGALCHRMQ 121
Cdd:cd18565 19 PLLIGVAIDAVFngeasFLPLVPASLGPADPrgqlwlLGGLTVAAFLLESLFQYLSGVLWRRFAQrvqhDLRTDTYDHVQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 122 HLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAP-VALPLFiVVVPLAALLVRSLRGR 200
Cdd:cd18565 99 RLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWqLALVAL-LPVPLIIAGTYWFQRR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 201 IRADNEAFRVEVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILLNVMAVA-FL 279
Cdd:cd18565 178 IEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVAtFV 257
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2764013554 280 SGsalvAYYGLFGISPgdvvmistFFTGLTA-SLTALLNLM 319
Cdd:cd18565 258 VG----GYWVLDGPPL--------FTGTLTVgTLVTFLFYT 286
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
496-576 |
9.59e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 496 LSGGQKQRLAIARALVRDPR---VLVLDEATSALDNQSEALVQEALERLM-RGRTVFVVAHRLSTIQDADRIVVM----- 566
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKCADWIIDLgpegg 249
|
90
....*....|.
gi 2764013554 567 ER-GRLVEVGT 576
Cdd:cd03271 250 DGgGQVVASGT 260
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
495-568 |
1.23e-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: 42.73 E-value: 1.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2764013554 495 RLSGGQKQRLAIARALV---RDPRVLV-LDEATSALDNQS-EALVQEALERLMRGRTVFVVAHRLSTIQDADRIVVMER 568
Cdd:cd03227 77 QLSGGEKELSALALILAlasLKPRPLYiLDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKK 155
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
60-305 |
1.66e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 43.81 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 60 TARIIDIVVDHKPVSALWWNTAAVLVVLLLNYPLhMYFSKLSSL-AIRRTGTELRGALCHRMQHLSIGYHSRVSAEVLQT 138
Cdd:cd18561 19 LARALARIFAGGPWEDIMPPLAGIAGVIVLRAAL-LWLRERVAHrAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 139 KVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVA---LPLFIVVVPLAALLVRSLRGRI-RADNEAFRVEVEQ 214
Cdd:cd18561 98 TVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLValiLLVFALLIPLSPALWDRLAKDTgRRHWAAYGRLSAQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 215 LSARVGEMTTLiPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGgrfgslswilLNVMAVAFLSGSALVAYYGLFGIS 294
Cdd:cd18561 178 FLDSLQGMTTL-KAFGASKRRGNELAARAEDLRQATMKVLAVSLLS----------SGIMGLATALGTALALGVGALRVL 246
|
250
....*....|.
gi 2764013554 295 PGDVVMISTFF 305
Cdd:cd18561 247 GGQLTLSSLLL 257
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
55-326 |
1.95e-04 |
|
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: 43.59 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 55 LLPLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLNYPLHMYFSKL-SSLAIRRTgTELRGALCHRMQHLSIGYHSRVSA 133
Cdd:cd18549 20 VFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWgHVMGARIE-TDMRRDLFEHLQKLSFSFFDNNKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 134 EVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAV-IGFQAPVALPLFIvVVPLAALLVRSLRGRIRADNEAFRVEV 212
Cdd:cd18549 99 GQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIIlLTINVPLTLIVFA-LLPLMIIFTIYFNKKMKKAFRRVREKI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 213 EQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAgfRLDM--LGGRFGSLSWILLNVMAVAFLSGSALVAYYGl 290
Cdd:cd18549 178 GEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLES--KKKAykAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKG- 254
|
250 260 270
....*....|....*....|....*....|....*.
gi 2764013554 291 fGISPGDVVMISTFFTGLTASLTALLNLMPIVSRGL 326
Cdd:cd18549 255 -EITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGM 289
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
483-564 |
2.14e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.58 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 483 QGVETVVGARGAR------LSGGQKQRLAIarALV-----RDPRVL-VLDEATSALDNQSEALVQEALERLMRGRTVFVV 550
Cdd:pfam02463 1059 GGIEISARPPGKGvknldlLSGGEKTLVAL--ALIfaiqkYKPAPFyLLDEIDAALDDQNVSRVANLLKELSKNAQFIVI 1136
|
90
....*....|....
gi 2764013554 551 AHRLSTIQDADRIV 564
Cdd:pfam02463 1137 SLREEMLEKADKLV 1150
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
57-285 |
5.07e-04 |
|
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: 42.19 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 57 PLVTARIIDIVVDHKPVSALWWNTAAVLVVLLLNYPLHMYFSKLSSLAIRRTGTELRGALCHRMQHLSIGY-HSRVSAEV 135
Cdd:cd18782 22 PLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFfDKRPVGEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 136 LQTkvVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVALPLFIVVVPLAALLV----RSLRGRIRADNEAFrve 211
Cdd:cd18782 102 STR--ISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTflfgPILRRQIRRRAEAS--- 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 212 vEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWIL--LNVMAVAFLsGSALV 285
Cdd:cd18782 177 -AKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLnkLSSLLVLWV-GAYLV 250
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
55-285 |
8.03e-04 |
|
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: 41.76 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 55 LLPLVTARIIDIVVDHKPVSALWwntAAVLVVLLLNYpLHMYFSKLS----SLAIRRTGTELRGALCHRMQHLSIGYH-- 128
Cdd:cd18572 14 AIPHYTGAVIDAVVADGSREAFY---RAVLLLLLLSV-LSGLFSGLRggcfSYAGTRLVRRLRRDLFRSLLRQDIAFFda 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 129 -------SRVSAEVlqTKVVRDVDA-LETMLQQTAQnGLGAVMTLLGG---LAVIGFqapVALPLFIVVVPLAALLVRSL 197
Cdd:cd18572 90 tktgeltSRLTSDC--QKVSDPLSTnLNVFLRNLVQ-LVGGLAFMFSLswrLTLLAF---ITVPVIALITKVYGRYYRKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 198 RGRIR-ADNEAFRVEVEQLSarvgemttLIPITRAHALERTALRRVDSSLQRVLTAGFRLDMLGGRFGSLSWILLNVMAV 276
Cdd:cd18572 164 SKEIQdALAEANQVAEEALS--------NIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQV 235
|
250
....*....|
gi 2764013554 277 AFL-SGSALV 285
Cdd:cd18572 236 LVLfYGGHLV 245
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
496-566 |
8.69e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.09 E-value: 8.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2764013554 496 LSGGQKQRLAIARALVRD-PRVL-VLDEATSALDNQSEALVQEALERLM-RGRTVFVVAHRLSTIQDADRIVVM 566
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
489-569 |
9.92e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 489 VGARGARLSGGQKQRLAIARALV---RDPRVLVLDEATSALDNQSEALVQEALERLM-RGRTVFVVAHRLSTIQDADRIV 564
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVsLGHSVIYIDHDPALLKQADYLI 1772
|
....*
gi 2764013554 565 VMERG 569
Cdd:PRK00635 1773 EMGPG 1777
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
480-540 |
1.41e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.98 E-value: 1.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2764013554 480 RMPQGVETVVGARGARLSGGQKQRLA-------------IARALVRDPRVLVLDEATSALDNQSEALVQEALER 540
Cdd:pfam13558 17 RDEDGSEVETYRRSGGLSGGEKQLLAylplaaalaaqygSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
496-572 |
1.57e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 496 LSGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALERLmRGrTVFVVAHrlstiqdaDR---------IVVM 566
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY-PG-TVVAVTH--------DRyfldnvagwILEL 233
|
....*.
gi 2764013554 567 ERGRLV 572
Cdd:PRK11819 234 DRGRGI 239
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
491-587 |
2.05e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 491 ARGAR-LSGGQKQR--LA--IARALVrdpRVL-VLDEATSAL---DNqsealvqealERL------MR--GRTVFVVAHR 553
Cdd:PRK00349 484 SRSAGtLSGGEAQRirLAtqIGSGLT---GVLyVLDEPSIGLhqrDN----------DRLietlkhLRdlGNTLIVVEHD 550
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2764013554 554 LSTIQDADRIVVM------ERGRLVEVGTHEELLAG----TGPY 587
Cdd:PRK00349 551 EDTIRAADYIVDIgpgagvHGGEVVASGTPEEIMKNpnslTGQY 594
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
107-289 |
2.14e-03 |
|
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: 40.55 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 107 RTGTELRGALCHRMQHLSIGYHSRVSAEVLQTKVVRDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAP-----VALP 181
Cdd:cd18575 66 RVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPkltllVLLV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 182 LFIVVVPLAaLLVRSLRGRIRADNEAfrveVEQLSARVGEMTTLIPITRAHALERTALRRVDSSLQRVLTAGFRldmlgg 261
Cdd:cd18575 146 IPLVVLPII-LFGRRVRRLSRASQDR----LADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALR------ 214
|
170 180
....*....|....*....|....*...
gi 2764013554 262 RFGSLSWILLNVMAVAFlSGSALVAYYG 289
Cdd:cd18575 215 RIRARALLTALVIFLVF-GAIVFVLWLG 241
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
496-587 |
2.84e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 496 LSGGQKQRLAIARALVR---DPRVLVLDEATSAL---DnqsealVQ---EALERLM-RGRTVFVVAHRLSTIQDADRIVV 565
Cdd:COG0178 827 LSGGEAQRVKLASELSKrstGKTLYILDEPTTGLhfhD------IRkllEVLHRLVdKGNTVVVIEHNLDVIKTADWIID 900
|
90 100 110
....*....|....*....|....*....|..
gi 2764013554 566 M-----ER-GRLVEVGTHEELLAG----TGPY 587
Cdd:COG0178 901 LgpeggDGgGEIVAEGTPEEVAKVkasyTGRY 932
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
497-552 |
3.23e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 3.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2764013554 497 SGGQKQRLAIARALVRDPRVLVLDEATSALDNQSEALVQEALerLMRGRTVFVVAH 552
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
495-568 |
3.85e-03 |
|
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: 39.13 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 495 RLSGGQKQ------RLAIARALVRDPRVLVLDEATSALDNQSealVQEALERLMR------GRTVFVVAHRLSTIQDADR 562
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---IEESLAEIIEerksqkNFQLIVITHDEELVDAADH 191
|
....*.
gi 2764013554 563 IVVMER 568
Cdd:cd03240 192 IYRVEK 197
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
381-406 |
6.45e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.15 E-value: 6.45e-03
10 20
....*....|....*....|....*.
gi 2764013554 381 VRAGETVALVGGSGAGKSTVLNLVIG 406
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLG 217
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
142-316 |
8.32e-03 |
|
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: 38.64 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 142 RDVDALETMLQQTAQNGLGAVMTLLGGLAVIGFQAPVALplfIVVVPLAALLVRSLRGRIRADNEAFRVEVEQLS---AR 218
Cdd:cd18580 104 KDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFL---IVLPPLLVVYYLLQRYYLRTSRQLRRLESESRSplySH 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 219 VGEMTTLIPITRA----HALERTALRRVDSS---------LQRVLtaGFRLDMLGgrfgslswillnvmaVAFLSGSALV 285
Cdd:cd18580 181 FSETLSGLSTIRAfgwqERFIEENLRLLDASqrafylllaVQRWL--GLRLDLLG---------------ALLALVVALL 243
|
170 180 190
....*....|....*....|....*....|.
gi 2764013554 286 AYYGLFGISPGDVVMISTFFTGLTASLTALL 316
Cdd:cd18580 244 AVLLRSSISAGLVGLALTYALSLTGSLQWLV 274
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
178-279 |
9.96e-03 |
|
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: 38.25 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2764013554 178 VALPLFIVvvpLAALLVRSLRGRIR------ADNEAFRVEveqlsaRVGEMTTLipitRAHALERTALRRVDSSLQRVLT 251
Cdd:cd18588 149 ASLPLYAL---LSLLVTPILRRRLEekfqrgAENQSFLVE------TVTGIETV----KSLAVEPQFQRRWEELLARYVK 215
|
90 100
....*....|....*....|....*...
gi 2764013554 252 AGFRLDMLGGRFGSLSWILLNVMAVAFL 279
Cdd:cd18588 216 ASFKTANLSNLASQIVQLIQKLTTLAIL 243
|
|
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