|
Name |
Accession |
Description |
Interval |
E-value |
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
36-577 |
1.46e-124 |
|
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: 383.42 E-value: 1.46e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 36 LLHRLWHQYIpisngAILAASLGINILALALPLLILQVYNRILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAG 115
Cdd:COG2274 150 LLRRYRRLLL-----QVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 116 AQYEHRAGCIAIKRLATGDLAHVESTPSGMHLDRLSSIELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIM 195
Cdd:COG2274 225 QRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 196 LGIAGFMAWKIGKSLQEQLEERREWDRRRYSFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTV 275
Cdd:COG2274 305 IPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 276 GTITSHLTVAAVVGFGSLMVINGTLSVGALAASTLLAGRTVQPALRALGLWSRFQSVSLAEDNLRDIDAIPAE-SRGRFK 354
Cdd:COG2274 385 SGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPErEEGRSK 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 355 MDRFT---SLDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDA 431
Cdd:COG2274 465 LSLPRlkgDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDP 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 432 ESVFNQISYIPQRPTLFHGTILDNLTMFRS--DQVEIMqRALELAAklhLDEVFARLPNGYDTEVGDSSADlLPAGVAQR 509
Cdd:COG2274 545 ASLRRQIGVVLQDVFLFSGTIRENITLGDPdaTDEEII-EAARLAG---LHDFIEALPMGYDTVVGEGGSN-LSGGQRQR 619
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1733551959 510 ITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
52-339 |
1.60e-98 |
|
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: 302.19 E-value: 1.60e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 52 ILAASLGINILALALPLLILQVYNRILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQYEHRAGCIAIKRLA 131
Cdd:cd18566 7 VLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 132 TGDLAHVESTPSGMHLDRLSSIELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIMLGIAGFMAWKIGKSLQ 211
Cdd:cd18566 87 SLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 212 EQLEERREWDRRRYSFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFG 291
Cdd:cd18566 167 RALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1733551959 292 SLMVINGTLSVGALAASTLLAGRTVQPALRALGLWSRFQSVSLAEDNL 339
Cdd:cd18566 247 ALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
75-577 |
9.47e-87 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 281.28 E-value: 9.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 75 NRILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQYEHRAGCIAIKRLATGDLAHVESTPSGMHLDRLSS-I 153
Cdd:COG1132 49 DALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNdV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 154 ELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIMLGIAGFMAWKIGKSLQEQLEERREWDRRRYSFLIEVLS 233
Cdd:COG1132 129 DAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 234 GIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGALAASTLLAG 313
Cdd:COG1132 209 GIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 314 RTVQPALRALGLWSRFQSVSLAEDNLRDI----DAIPAESRGRFKMDRFTSLDLKNLHFRYsPKDPEVLHNINLRLEQGQ 389
Cdd:COG1132 289 RLFGPLRQLANVLNQLQRALASAERIFELldepPEIPDPPGAVPLPPVRGEIEFENVSFSY-PGDRPVLKDISLTIPPGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 390 IIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIPQRPTLFHGTILDNLTMFRSD--QVEIM 467
Cdd:COG1132 368 TVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDatDEEVE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 468 qRALELAaklHLDEVFARLPNGYDTEVGDSSADlLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL 547
Cdd:COG1132 448 -EAAKAA---QAHEFIEALPDGYDTVVGERGVN-LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL 522
|
490 500 510
....*....|....*....|....*....|
gi 1733551959 548 KGTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:COG1132 523 MKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
72-578 |
2.64e-78 |
|
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: 258.52 E-value: 2.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 72 QVYNRILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQYEHRAGciaiKRLATGDLAHVESTPSGMHLDRLS 151
Cdd:COG4618 45 QVYDRVLTSRSVDTLLMLTLLALGLYAVMGLLDAVRSRILVRVGARLDRRLG----PRVFDAAFRAALRGGGGAAAQALR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 152 SIELIRDFYASQASLVLIDLPFILLFLGILALI---TGWLVLI-PIIMLGIAGFMAWKIGKSLQEqleeRREWDRRRYSF 227
Cdd:COG4618 121 DLDTLRQFLTGPGLFALFDLPWAPIFLAVLFLFhplLGLLALVgALVLVALALLNERLTRKPLKE----ANEAAIRANAF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 228 LIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGhaqTVGTITSHLTVA---AVVGFGSLMVINGTLSVGA 304
Cdd:COG4618 197 AEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAG---GFSALSKFLRLLlqsAVLGLGAYLVIQGEITPGA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 305 LAASTLLAGRTVQPALRALGLWSRFQSVSLAEDNLRDIDAIPAESRGRFKMDRFT-SLDLKNLHFRYSPKDPEVLHNINL 383
Cdd:COG4618 274 MIAASILMGRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMPLPRPKgRLSVENLTVVPPGSKRPILRGVSF 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 384 RLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIPQRPTLFHGTILDNLTMFRSDQ 463
Cdd:COG4618 354 SLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDAD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 464 VEIMQRALELAAkLHldEVFARLPNGYDTEVGDSSAdLLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDL 543
Cdd:COG4618 434 PEKVVAAAKLAG-VH--EMILRLPDGYDTRIGEGGA-RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAA 509
|
490 500 510
....*....|....*....|....*....|....*...
gi 1733551959 544 MRSLK---GTVsmILVSYRPSLLALADQRFSLEDGRLK 578
Cdd:COG4618 510 IRALKargATV--VVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
73-577 |
2.05e-73 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 248.89 E-value: 2.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 73 VYNRILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQYEHRAGCIAIKRLATGDLAHVESTPSGMHLDRLSS 152
Cdd:TIGR01846 165 VIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 153 IELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIMLGIAGFMAWKIGKSLQEQLEERREWDRRRYSFLIEVL 232
Cdd:TIGR01846 245 LEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESV 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 233 SGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGALAASTLLA 312
Cdd:TIGR01846 325 TGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLA 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 313 GRTVQPALRALGLWSRFQSVSLAEDNLRDIDAIPAESRGRFKM---DRFTSLDLKNLHFRYSPKDPEVLHNINLRLEQGQ 389
Cdd:TIGR01846 405 GRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGLAalpELRGAITFENIRFRYAPDSPEVLSNLNLDIKPGE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 390 IIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIPQRPTLFHGTILDNLTMFRSDQVEIMQR 469
Cdd:TIGR01846 485 FIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 470 AlelAAKLHLDEVF-ARLPNGYDTEVGDSSAdLLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLK 548
Cdd:TIGR01846 565 H---AAKLAGAHDFiSELPQGYNTEVGEKGA-NLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREIC 640
|
490 500
....*....|....*....|....*....
gi 1733551959 549 GTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:TIGR01846 641 RGRTVIIIAHRLSTVRACDRIIVLEKGQI 669
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
77-592 |
2.05e-67 |
|
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: 229.26 E-value: 2.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 77 ILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQ---------YEH--RAGCIAIKRLATGDLAHvestpsgM 145
Cdd:COG4988 48 IIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARvkrrlrrrlLEKllALGPAWLRGKSTGELAT-------L 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 146 HLDRlssIELIRDFYA---SQASLVLIDLPFILLFL-------GILALITgwLVLIPIIMLGIaGFMAWKIGKSLQEQLE 215
Cdd:COG4988 121 LTEG---VEALDGYFArylPQLFLAALVPLLILVAVfpldwlsGLILLVT--APLIPLFMILV-GKGAAKASRRQWRALA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 216 ERRewdrrrySFLIEVLSGIHTVKAMAMEAMMLRRYERLLESN----------AFASAQVSQIsghaqtvgtITShLTVA 285
Cdd:COG4988 195 RLS-------GHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFrkrtmkvlrvAFLSSAVLEF---------FAS-LSIA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 286 AVVGFGSLMVINGTLSVGALAASTLLAGRTVQPaLRALGlwSRF----QSVSLAEDnLRDIDAIPAESRGR----FKMDR 357
Cdd:COG4988 258 LVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLP-LRDLG--SFYharaNGIAAAEK-IFALLDAPEPAAPAgtapLPAAG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 358 FTSLDLKNLHFRYsPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQ 437
Cdd:COG4988 334 PPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYIPQRPTLFHGTILDNLTMFRSD-QVEIMQRALELAaklHLDEVFARLPNGYDTEVGDSSAdLLPAGVAQRITIVRAL 516
Cdd:COG4988 413 IAWVPQNPYLFAGTIRENLRLGRPDaSDEELEAALEAA---GLDEFVAALPDGLDTPLGEGGR-GLSGGQAQRLALARAL 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 517 INRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRLkpLDFADHKNLSRTN 592
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRI--VEQGTHEELLAKN 562
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
126-593 |
1.47e-60 |
|
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: 211.16 E-value: 1.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 126 AIKRLATGDLahvestpsgmhLDRLSS-IELIRDFY------ASQASLVLIdlpFILLFLGILALITGWLVLIPIIMLGI 198
Cdd:COG4987 105 GLARLRSGDL-----------LNRLVAdVDALDNLYlrvllpLLVALLVIL---AAVAFLAFFSPALALVLALGLLLAGL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 199 AG-FMAWKIGKSLQEQLEERREWDrrrYSFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGT 277
Cdd:COG4987 171 LLpLLAARLGRRAGRRLAAARAAL---RARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 278 ITSHLTVAAVVGFGSLMVINGTLSVGALAASTLL---AGRTVQPALRALGLWSRFQSvslAEDNLRDI-DAIPA--ESRG 351
Cdd:COG4987 248 LAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAalaLFEALAPLPAAAQHLGRVRA---AARRLNELlDAPPAvtEPAE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 352 RFKMDRFTSLDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDA 431
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 432 ESVFNQISYIPQRPTLFHGTILDNLTMFR---SDqvEIMQRALELAAklhLDEVFARLPNGYDTEVGDSSAdLLPAGVAQ 508
Cdd:COG4987 405 DDLRRRIAVVPQRPHLFDTTLRENLRLARpdaTD--EELWAALERVG---LGDWLAALPDGLDTWLGEGGR-RLSGGERR 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 509 RITIVRALINRPSLILFDESNTSLDGYSDRALC-DLMRSLKG-TVsmILVSYRPSLLALADQRFSLEDGRLKPLdfADHK 586
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLaDLLEALAGrTV--LLITHRLAGLERMDRILVLEDGRIVEQ--GTHE 554
|
....*..
gi 1733551959 587 NLSRTNE 593
Cdd:COG4987 555 ELLAQNG 561
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
52-339 |
3.65e-52 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 180.71 E-value: 3.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 52 ILAASLGINILALALPLLILQVYNRILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQ---------YEHra 122
Cdd:cd18587 7 VLLAALLINLFALASPLFVMNVYDRVVPNNAIETLWVLAIGVLIALLFDFILKLLRAYFIDVAGKRadvilssrlFER-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 123 gCIAIKRLA----TGDLAHvestpsgmhldRLSSIELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPI----I 194
Cdd:cd18587 85 -VLGLRLEArpasVGSFAN-----------NLREFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGPLALVPLvaipL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 195 MLGIAGFMAWKIGKSLQEQLEERREWdrrrYSFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQT 274
Cdd:cd18587 153 VLLYGLLLQKPLRRLVEESMRESAQK----NALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATN 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 275 VGTITSHLTVAAVVGFGSLMVINGTLSVGALAASTLLAGRTVQPALRALGLWSRFQSVSLAEDNL 339
Cdd:cd18587 229 FAQFVQQLVTVAIVIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLLTRYQQARTALKSL 293
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
361-576 |
9.27e-48 |
|
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: 164.86 E-value: 9.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISY 440
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTLFHGTILDNltmfrsdqveimqralelaaklhldevfarlpngydtevgdssadLLPAGVAQRITIVRALINRP 520
Cdd:cd03228 81 VPQDPFLFSGTIREN---------------------------------------------ILSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 521 SLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGR 576
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
81-568 |
9.41e-46 |
|
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: 169.77 E-value: 9.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 81 EGLSTLAMLTIGVAIALVLDVLLkiararlsGWAGAQYEHRAGCIAIKRLATGDLAHV--------ESTPSG----MHLD 148
Cdd:TIGR02857 38 EPLAELLPALGALALVLLLRALL--------GWLQERAAARAAAAVKSQLRERLLEAVaalgprwlQGRPSGelatLALE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 149 RLSSIELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIMlgIAGFMA---WKIGKSLQEQLEERREWDrrry 225
Cdd:TIGR02857 110 GVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPL--IPIFMIligWAAQAAARKQWAALSRLS---- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 226 SFLIEVLSGIHTVKAMAM---EAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGslmVINGTLSV 302
Cdd:TIGR02857 184 GHFLDRLRGLPTLKLFGRakaQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSVALVAVYIGFR---LLAGDLDL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 303 GALAASTLLAGRTVQPaLRALG-LW-SRFQSVSLAEDNLRDIDAIPAESRGRFKM--DRFTSLDLKNLHFRYSPKDPeVL 378
Cdd:TIGR02857 261 ATGLFVLLLAPEFYLP-LRQLGaQYhARADGVAAAEALFAVLDAAPRPLAGKAPVtaAPASSLEFSGVSVAYPGRRP-AL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 379 HNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIPQRPTLFHGTILDNLTM 458
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 459 FRSDQ-VEIMQRALELAAklhLDEVFARLPNGYDTEVGDSSADlLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSD 537
Cdd:TIGR02857 419 ARPDAsDAEIREALERAG---LDEFVAALPQGLDTPIGEGGAG-LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
490 500 510
....*....|....*....|....*....|.
gi 1733551959 538 RALCDLMRSLKGTVSMILVSYRPSLLALADQ 568
Cdd:TIGR02857 495 AEVLEALRALAQGRTVLLVTHRLALAALADR 525
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
360-577 |
2.24e-44 |
|
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: 157.37 E-value: 2.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQIS 439
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRPTLFHGTILDNLTMFR--SDQVEIMqRALELAAklhLDEVFARLPNGYDTEVGDsSADLLPAGVAQRITIVRALI 517
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAplADDERIL-RAAELAG---VTDFVNKHPNGLDLQIGE-RGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 518 NRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
73-339 |
5.03e-43 |
|
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: 156.12 E-value: 5.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 73 VYNRILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLsgwagaqYEHRAGCIAI-------KRLATGDLAHVESTPSGM 145
Cdd:cd18588 28 IIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYL-------FSHTTNRIDAelgarlfRHLLRLPLSYFESRQVGD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 146 HLDRLSSIELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIMLGIAGFMAWKIGKSLQEQLEERREWDRRRY 225
Cdd:cd18588 101 TVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 226 SFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGAL 305
Cdd:cd18588 181 SFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQL 260
|
250 260 270
....*....|....*....|....*....|....
gi 1733551959 306 AASTLLAGRTVQPALRALGLWSRFQSVSLAEDNL 339
Cdd:cd18588 261 IAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
364-577 |
3.10e-42 |
|
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: 151.99 E-value: 3.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 364 KNLHFRYSPKDPeVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIPQ 443
Cdd:cd03254 6 ENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 444 RPTLFHGTILDNLTMFRSD-QVEIMQRALELAaklHLDEVFARLPNGYDTEVGDsSADLLPAGVAQRITIVRALINRPSL 522
Cdd:cd03254 85 DTFLFSGTIMENIRLGRPNaTDEEVIEAAKEA---GAHDFIMKLPNGYDTVLGE-NGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 523 ILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKI 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
363-577 |
6.11e-41 |
|
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: 148.79 E-value: 6.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIP 442
Cdd:cd03252 3 FEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 443 QRPTLFHGTILDNLTMfrSDQVEIMQRALELAAKLHLDEVFARLPNGYDTEVGDSSADlLPAGVAQRITIVRALINRPSL 522
Cdd:cd03252 83 QENVLFNRSIRDNIAL--ADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAG-LSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 523 ILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRI 214
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
50-339 |
2.34e-38 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 143.13 E-value: 2.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 50 GAILAASLGINILALALPLLILQVYNRILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQYEHRAGciaiKR 129
Cdd:cd18586 5 VEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELG----RR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 130 LATGDLA-HVESTPSGMHLDRLSSIELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIMLGIAGFMAWKIGK 208
Cdd:cd18586 81 VFRAVLElPLESRPSGYWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 209 SLQEQLEERREWDRRRYSFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVV 288
Cdd:cd18586 161 ATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLIL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1733551959 289 GFGSLMVINGTLSVGALAASTLLAGRTVQPALRALGLWSRFQSVSLAEDNL 339
Cdd:cd18586 241 GVGAYLVIDGELTIGALIAASILSGRALAPIDQLVGAWKQLSAARQAYERL 291
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
78-577 |
6.23e-38 |
|
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: 149.50 E-value: 6.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 78 LPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQYEHRAGCIAIKRLATGDLAHVESTPSGMHLDRLSSIELIR 157
Cdd:TIGR01193 187 IPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSII 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 158 DFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIMLGIAGFMAWKIGKSLQEQLEERREWDRRRYSFLIEVLSGIHT 237
Cdd:TIGR01193 267 DALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIET 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 238 VKAMAMEAMMLR----RYERLLESNaFASAQVSQISghaQTVGTITSHLTVAAVVGFGSLMVINGTLSVGALAASTLLAG 313
Cdd:TIGR01193 347 IKSLTSEAERYSkidsEFGDYLNKS-FKYQKADQGQ---QAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 314 RTVQPALRALGLWSRFQSVSLAEDNLRDIDAIPAESRGRFKMDRFT----SLDLKNLHFRYSPKDPeVLHNINLRLEQGQ 389
Cdd:TIGR01193 423 YFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNnlngDIVINDVSYSYGYGSN-ILSDISLTIKMNS 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 390 IIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIPQRPTLFHGTILDNLTMFRSDQVEI--M 467
Cdd:TIGR01193 502 KTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQdeI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 468 QRALELAaklHLDEVFARLPNGYDTEVGDSSADlLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL 547
Cdd:TIGR01193 582 WAACEIA---EIKDDIENMPLGYQTELSEEGSS-ISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL 657
|
490 500 510
....*....|....*....|....*....|
gi 1733551959 548 KGTvSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:TIGR01193 658 QDK-TIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
361-576 |
2.11e-37 |
|
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: 138.90 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISY 440
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTLFHGTILDNLTMFRSD--QVEIMqRALELAaklHLDEVFARLPNGYDTEVGDSSAdLLPAGVAQRITIVRALIN 518
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGatREEVE-EAARAA---NAHEFIMELPEGYDTVIGERGV-KLSGGQRQRIAIARALLK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1733551959 519 RPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGR 576
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGK 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
361-577 |
1.32e-36 |
|
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: 134.65 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISY 440
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTLFHGTILDNltmfrsdqveimqralelaaklhldevfarlpngydtevgdssadLLPAGVAQRITIVRALINRP 520
Cdd:cd03246 81 LPQDDELFSGSIAEN---------------------------------------------ILSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1733551959 521 SLILFDESNTSLDGYSDRALCDLMRSLK-GTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
363-577 |
4.12e-36 |
|
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: 135.44 E-value: 4.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLHFRYSPKDPeVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIP 442
Cdd:cd03253 3 FENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 443 QRPTLFHGTILDNLTMFRSDQVEIMQRALELAAKLHldEVFARLPNGYDTEVGDSSAdLLPAGVAQRITIVRALINRPSL 522
Cdd:cd03253 82 QDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIH--DKIMRFPDGYDTIVGERGL-KLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 523 ILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
361-577 |
1.52e-35 |
|
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: 133.00 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEV--LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFD--AESVF- 435
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 436 -NQISYIPQRPTLF-HGTILDN----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQR 509
Cdd:cd03255 81 rRHIGFVFQSFNLLpDLTALENvelpLLLAGVPKKERRERAEELLERVGLGDRLNHYPSE------------LSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551959 510 ITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL---KGTvSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkeAGT-TIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
52-335 |
2.90e-35 |
|
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: 134.64 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 52 ILAASLGINILALALPLLILQVYNRILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQYEHRAGCIAIKRLA 131
Cdd:cd18782 7 VLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 132 TGDLAHVESTPSGMHLDRLSSIELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIMLGIAGFMAWKIGKSLQ 211
Cdd:cd18782 87 RLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 212 EQLEERREWDRRRYSFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFG 291
Cdd:cd18782 167 RQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1733551959 292 SLMVINGTLSVGALAASTLLAGRTVQPALRALGLWSRFQSVSLA 335
Cdd:cd18782 247 AYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVS 290
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
362-576 |
4.80e-35 |
|
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: 132.28 E-value: 4.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 362 DLKNLHFRYsPKDPE--VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQIS 439
Cdd:cd03249 2 EFKNVSFRY-PSRPDvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRPTLFHGTILDNLTMFRSD-QVEIMQRALELAAklhLDEVFARLPNGYDTEVGDSSAdLLPAGVAQRITIVRALIN 518
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDaTDEEVEEAAKKAN---IHDFIMSLPDGYDTLVGERGS-QLSGGQKQRIAIARALLR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551959 519 RPSLILFDESNTSLDGYSDRALCD-LMRSLKGTVSmILVSYRPSLLALADQRFSLEDGR 576
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEaLDRAMKGRTT-IVIAHRLSTIRNADLIAVLQNGQ 214
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
134-577 |
8.86e-35 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 140.24 E-value: 8.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 134 DLAHVESTPSGMHLDRLSS-IELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIMLGIAGFMAWKIGKSLQE 212
Cdd:TIGR00958 248 DLGFFDENKTGELTSRLSSdTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 213 QLEERREWDRRRYSFLIEVLSGIHTVKAMAMEAMMLRRYERLLES-------NAFASAQ---VSQISGHAQTVGtitshl 282
Cdd:TIGR00958 328 LSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEEtlqlnkrKALAYAGylwTTSVLGMLIQVL------ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 283 tvaaVVGFGSLMVINGTLSVGALAaSTLLAGRTVQPALRALG-LWSRF-QSVSLAEDNLRDIDAIPA-ESRGRFKMDRFT 359
Cdd:TIGR00958 402 ----VLYYGGQLVLTGKVSSGNLV-SFLLYQEQLGEAVRVLSyVYSGMmQAVGASEKVFEYLDRKPNiPLTGTLAPLNLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SL-DLKNLHFRYsPKDPE--VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFN 436
Cdd:TIGR00958 477 GLiEFQDVSFSY-PNRPDvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 437 QISYIPQRPTLFHGTILDNLT--MFRSDQVEIMQRALELAAklhlDEVFARLPNGYDTEVGDSSAdLLPAGVAQRITIVR 514
Cdd:TIGR00958 556 QVALVGQEPVLFSGSVRENIAygLTDTPDEEIMAAAKAANA----HDFIMEFPNGYDTEVGEKGS-QLSGGQKQRIAIAR 630
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733551959 515 ALINRPSLILFDESNTSLDGYSDRALCDLMRSlkGTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
361-594 |
3.77e-33 |
|
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: 127.28 E-value: 3.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYspKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAEsVFNQISY 440
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTLF-HGTILDNLTMF----RSDQVEIMQRALELAAKLHLDEVfarlpngYDTEVGDssadlLPAGVAQRITIVRA 515
Cdd:COG4555 79 LPDERGLYdRLTVRENIRYFaelyGLFDEELKKRIEELIELLGLEEF-------LDRRVGE-----LSTGMKKKVALARA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 516 LINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYR-PSLL-ALADQRFSLEDGRLKPLDFADHKNLSRTNE 593
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHiMQEVeALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
.
gi 1733551959 594 N 594
Cdd:COG4555 227 N 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
361-577 |
7.62e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.93 E-value: 7.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEV--LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAE--SVF- 435
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERelARLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 436 -NQISYIPQR----PTLfhgTILDN----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPNgydtevgdssadLLPAGV 506
Cdd:COG1136 85 rRHIGFVFQFfnllPEL---TALENvalpLLLAGVSRKERRERARELLERVGLGDRLDHRPS------------QLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 507 AQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL---KGTvSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnreLGT-TIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
370-577 |
3.71e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 131.12 E-value: 3.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 370 YSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGqIVPTKGSALLNGQPPHDFDAESVFNQISYIPQRPTLFH 449
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 450 GTILDNLTMFRSD--QVEIMQrALELAaklHLDEVFARLPNGYDTEVGDSSADlLPAGVAQRITIVRALINRPSLILFDE 527
Cdd:PRK11174 437 GTLRDNVLLGNPDasDEQLQQ-ALENA---WVSEFLPLLPQGLDTPIGDQAAG-LSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1733551959 528 SNTSLDGYSDRAlcdLMRSLK---GTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:PRK11174 512 PTASLDAHSEQL---VMQALNaasRRQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
363-576 |
4.00e-32 |
|
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: 123.35 E-value: 4.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIP 442
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 443 QRPT--LFHGTILD-------NLTMfrsDQVEIMQRALELAAKLHLDEVFARLPngydtevgdssaDLLPAGVAQRITIV 513
Cdd:cd03225 82 QNPDdqFFGPTVEEevafgleNLGL---PEEEIEERVEEALELVGLEGLRDRSP------------FTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 514 RALINRPSLILFDESNTSLDGYSDRALCDLMRSLK--GTvSMILVSYRPSLLA-LADQRFSLEDGR 576
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaeGK-TIIIVTHDLDLLLeLADRVIVLEDGK 211
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
361-577 |
1.49e-31 |
|
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: 122.19 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPK-DPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQIS 439
Cdd:cd03248 12 VKFQNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRPTLFHGTILDNLTmFRSDQVEiMQRALELAAKLHLDEVFARLPNGYDTEVGDSSAdLLPAGVAQRITIVRALINR 519
Cdd:cd03248 92 LVGQEPVLFARSLQDNIA-YGLQSCS-FECVKEAAQKAHAHSFISELASGYDTEVGEKGS-QLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1733551959 520 PSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
73-335 |
5.03e-31 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 122.63 E-value: 5.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 73 VYNRILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQYEHRAGCIAIKRLATGDLAHVESTPSGMHLDRLSS 152
Cdd:cd18783 28 VIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 153 IELIRDFYASQASLVLIDLPFILLFLGILALITG---WLVLI--PIIMLGIAGFMawkigKSLQEQLEERREWDRRRYSF 227
Cdd:cd18783 108 IERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPtlaLVVLAfsALIALIILAFL-----PPFRRRLQALYRAEGERQAF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 228 LIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGALAA 307
Cdd:cd18783 183 LVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIA 262
|
250 260
....*....|....*....|....*...
gi 1733551959 308 STLLAGRTVQPALRALGLWSRFQSVSLA 335
Cdd:cd18783 263 FNMLAGRVAGPLVQLAGLVQEYQEARLS 290
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
129-560 |
3.38e-30 |
|
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: 124.78 E-value: 3.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 129 RLATGDLAHVESTPSGMHLDRLSS-IELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIMLGIAGF-MAWKI 206
Cdd:TIGR02868 95 RLARQALAGRRRLRRGDLLGRLGAdVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFvAPLVS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 207 GKSLQEQLEERREWDRRRYSFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAA 286
Cdd:TIGR02868 175 LRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 287 VVGFGSLMVINGTLSVGALAASTLL---AGRTVQPALRALGLWSRFQSVSL----AEDNLRDIDAIPAESRGRFKMDRFT 359
Cdd:TIGR02868 255 ALWAGGPAVADGRLAPVTLAVLVLLplaAFEAFAALPAAAQQLTRVRAAAEriveVLDAAGPVAEGSAPAAGAVGLGKPT 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 sLDLKNLHFRYsPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQIS 439
Cdd:TIGR02868 335 -LELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVS 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRPTLFHGTILDNLTMFRSDQV-EIMQRALElAAKLHldEVFARLPNGYDTEVGDSSAdLLPAGVAQRITIVRALIN 518
Cdd:TIGR02868 413 VCAQDAHLFDTTVRENLRLARPDATdEELWAALE-RVGLA--DWLRALPDGLDTVLGEGGA-RLSGGERQRLALARALLA 488
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1733551959 519 RPSLILFDESNTSLD-GYSDRALCDLMRSLKGTVsMILVSYRP 560
Cdd:TIGR02868 489 DAPILLLDEPTEHLDaETADELLEDLLAALSGRT-VVLITHHL 530
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
230-577 |
3.14e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 122.13 E-value: 3.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 230 EVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGALAAST 309
Cdd:PRK10789 181 ESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIGGGSWMVVNGSLTLGQLTSFV 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 310 LLAGRTVQPAL----------RALGLWSRFQSVsLAEDNLRD--IDAIPAEsRGrfkmdrftSLDLKNLHFRYSPKDPEV 377
Cdd:PRK10789 261 MYLGLMIWPMLalawmfniveRGSAAYSRIRAM-LAEAPVVKdgSEPVPEG-RG--------ELDVNIRQFTYPQTDHPA 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIPQRPTLFHGTILDNLT 457
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 458 MFRSDQVeimQRALELAAKL---HLDevFARLPNGYDTEVGDSSAdLLPAGVAQRITIVRALINRPSLILFDESNTSLDG 534
Cdd:PRK10789 411 LGRPDAT---QQEIEHVARLasvHDD--ILRLPQGYDTEVGERGV-MLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1733551959 535 YSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:PRK10789 485 RTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
361-577 |
3.22e-29 |
|
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: 113.65 E-value: 3.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYspKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDfDAESVFNQISY 440
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTLFHG-TILDNLTmfrsdqveimqralelaaklhldevfarlpngydtevgdssadlLPAGVAQRITIVRALINR 519
Cdd:cd03230 78 LPEEPSLYENlTVRENLK--------------------------------------------LSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 520 PSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVS--YRPSLLALADQRFSLEDGRL 577
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSshILEEAERLCDRVAILNNGRI 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
361-527 |
4.65e-29 |
|
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: 114.88 E-value: 4.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDP--EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAesvfnQI 438
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 439 SYIPQRPTLF-HGTILDN----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPngydtevgdssaDLLPAGVAQRITIV 513
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNvalgLELQGVPKAEARERAEELLELVGLSGFENAYP------------HQLSGGMRQRVALA 143
|
170
....*....|....
gi 1733551959 514 RALINRPSLILFDE 527
Cdd:cd03293 144 RALAVDPDVLLLDE 157
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
363-576 |
9.39e-29 |
|
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: 111.95 E-value: 9.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLHFRYspKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIP 442
Cdd:cd00267 2 IENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 443 QrptlfhgtildnltmfrsdqveimqralelaaklhldevfarlpngydtevgdssadlLPAGVAQRITIVRALINRPSL 522
Cdd:cd00267 80 Q----------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 523 ILFDESNTSLDGYSDRALCDLMRSL-KGTVSMILVSYRPSLLA-LADQRFSLEDGR 576
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
361-577 |
1.06e-28 |
|
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: 113.77 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDpeVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ-----PPHDFDaesvf 435
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvPPERRN----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 436 nqISYIPQRPTLF-HGTILDN----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQRI 510
Cdd:cd03259 74 --IGMVFQDYALFpHLTVAENiafgLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHE------------LSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 511 TIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL--KGTVSMILVSYRPS-LLALADQRFSLEDGRL 577
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQEeALALADRIAVMNEGRI 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
361-577 |
1.81e-28 |
|
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: 113.43 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQI-----VPTKGSALLNGQPPH--DFDAES 433
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYdlDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 434 VFNQISYIPQRPTLFHGTILDNLTM------FRSDQV--EIMQRALELAAkLHlDEVFARLpngydtevgdsSADLLPAG 505
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYglrlhgIKLKEEldERVEEALRKAA-LW-DEVKDRL-----------HALGLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733551959 506 VAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLA-LADQRFSLEDGRL 577
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRL 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
361-527 |
2.77e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 114.03 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPE--VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAEsvfnqI 438
Cdd:COG1116 8 LELRGVSKRFPTGGGGvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 439 SYIPQRPTLF-HGTILDN----LTMFRSDQVEIMQRALELAAKLHLDEVfarlpngydtevgdssADLLPA----GVAQR 509
Cdd:COG1116 83 GVVFQEPALLpWLTVLDNvalgLELRGVPKAERRERARELLELVGLAGF----------------EDAYPHqlsgGMRQR 146
|
170
....*....|....*...
gi 1733551959 510 ITIVRALINRPSLILFDE 527
Cdd:COG1116 147 VAIARALANDPEVLLMDE 164
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
360-581 |
4.83e-28 |
|
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: 111.74 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQIS 439
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRPTLFHGTILDNLTMF-RSDQVEIMQrALELaaklhldevfarlpngydTEVGDSsadlLPAGVAQRITIVRALIN 518
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLDPFdEYSDEEIYG-ALRV------------------SEGGLN----LSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733551959 519 RPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRLKPLD 581
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
378-527 |
9.73e-28 |
|
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: 108.89 E-value: 9.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIPQRPTLF-HGTILDNL 456
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 457 ----TMFRSDQVEIMQRALELAAKLhldevfaRLPNGYDTEVGDSSADlLPAGVAQRITIVRALINRPSLILFDE 527
Cdd:pfam00005 81 rlglLLKGLSKREKDARAEEALEKL-------GLGDLADRPVGERPGT-LSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
360-581 |
1.08e-27 |
|
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: 111.05 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQIS 439
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRPTLFHGTILDNLTMF-RSDQVEIMQrALELAaklHLDEVFARLPNGYDTEVgDSSADLLPAGVAQRITIVRALIN 518
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDPFgEYSDEELWQ-ALERV---GLKEFVESLPGGLDTVV-EEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 519 RPSLILFDESNTSLDGYSDRALCDLMRS-LKGTvSMILVSYRPSLLALADQRFSLEDGRLKPLD 581
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREaFKDC-TVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
362-578 |
1.42e-27 |
|
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: 110.42 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 362 DLKNLHFRYsPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVfnqISYI 441
Cdd:cd03226 1 RIENISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS---IGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 442 PQRPT--LFHGTILDNLTMFRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQRITIVRALINR 519
Cdd:cd03226 77 MQDVDyqLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLS------------LSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551959 520 PSLILFDESNTSLDGYSDRALCDLMRSLKG-TVSMILVSYRPSLLAL-ADQRFSLEDGRLK 578
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
361-578 |
1.52e-27 |
|
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: 109.32 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDaESVFNQISY 440
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTLFHGTILDNLtmfrsdqveimqralelaaklhldevfarlpngydtevgdssADLLPAGVAQRITIVRALINRP 520
Cdd:cd03247 80 LNQRPYLFDTTLRNNL------------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1733551959 521 SLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRLK 578
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
282-578 |
2.29e-27 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 116.66 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 282 LTVAAVVGFGSLMVINGTLSVGALAA--STLLAgrTVQPaLRAL-GLWSRFQSVSLAEDNLRDI-DAIPAESRGRFKMDR 357
Cdd:PRK11176 261 LALAFVLYAASFPSVMDTLTAGTITVvfSSMIA--LMRP-LKSLtNVNAQFQRGMAACQTLFAIlDLEQEKDEGKRVIER 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 358 FT-SLDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFN 436
Cdd:PRK11176 338 AKgDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 437 QISYIPQRPTLFHGTILDNLTMFRSDQVEIMQraLELAAKL-HLDEVFARLPNGYDTEVGDSSAdLLPAGVAQRITIVRA 515
Cdd:PRK11176 418 QVALVSQNVHLFNDTIANNIAYARTEQYSREQ--IEEAARMaYAMDFINKMDNGLDTVIGENGV-LLSGGQRQRIAIARA 494
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 516 LI-NRPSLILfDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRLK 578
Cdd:PRK11176 495 LLrDSPILIL-DEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
363-555 |
2.35e-27 |
|
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: 109.93 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLHFRYSpkDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDaesvfNQISYIP 442
Cdd:cd03235 2 VEDLTVSYG--GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 443 QRPTL---FHGTILDNLTM--------FRSDQVEIMQRALELaaklhLDEVFArlpngydTEVGDSSADLLPAGVAQRIT 511
Cdd:cd03235 75 QRRSIdrdFPISVRDVVLMglyghkglFRRLSKADKAKVDEA-----LERVGL-------SELADRQIGELSGGQQQRVL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1733551959 512 IVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKG---TVSMIL 555
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVT 189
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
361-577 |
1.49e-26 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 108.53 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAE---SVFNQ 437
Cdd:COG1127 6 IEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYIPQRPTLFHG-TILDN----LTMFRS-DQVEIMQRALElaaKLHLdevfarlpngydteVG-DSSADLLPA----GV 506
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENvafpLREHTDlSEAEIRELVLE---KLEL--------------VGlPGAADKMPSelsgGM 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 507 AQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGT--VSMILVSYR-PSLLALADQRFSLEDGRL 577
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElgLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
361-577 |
3.50e-26 |
|
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: 107.20 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAE---SVFNQ 437
Cdd:cd03261 1 IELRGLTKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYIPQRPTLFHG-TILDNL-----TMFRSDQVEIMQRALElaaKLHLdevfarlpngydteVG-DSSADLLPA----GV 506
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVafplrEHTRLSEEEIREIVLE---KLEA--------------VGlRGAEDLYPAelsgGM 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 507 AQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGT--VSMILVSYR-PSLLALADQRFSLEDGRL 577
Cdd:cd03261 142 KKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgLTSIMVTHDlDTAFAIADRIAVLYDGKI 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
361-576 |
6.11e-26 |
|
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: 105.63 E-value: 6.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPE---VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGqpphdfdaesvfnQ 437
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYIPQRPTLFHGTILDNLTMFRSDQVEIMQRALELAAklhLDEVFARLPNGYDTEVGDSSADlLPAGVAQRITIVRALI 517
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACA---LEPDLEILPDGDLTEIGEKGIN-LSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551959 518 NRPSLILFDESNTSLDGYSDRALCD--LMRSLKGTVSMILVSYRPSLLALADQRFSLEDGR 576
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
177-577 |
6.53e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 110.45 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 177 FLGILALITGWLVLiPIIMLGIAGFMAWKigKSLQEQLEERREWDRRRYSFLIEVLSGIHTVKAMAMEAMMLRRYERLLE 256
Cdd:PLN03232 1044 LIGTVSTISLWAIM-PLLILFYAAYLYYQ--STSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMD 1120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 257 SNA-FASAQVSQ---ISGHAQTVGTITSHLTVAAVV----------GFGSLMvinGTLSVGALAASTLLAGrTVQPALRA 322
Cdd:PLN03232 1121 NNIrFTLANTSSnrwLTIRLETLGGVMIWLTATFAVlrngnaenqaGFASTM---GLLLSYTLNITTLLSG-VLRQASKA 1196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 323 LGLWSRFQSVSLAEDNLRDIDAIPAESRGRFKMDRFTSLDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKS 402
Cdd:PLN03232 1197 ENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKS 1276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 403 TLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIPQRPTLFHGTILDNLTMFRSDQVEIMQRALELAaklHLDEV 482
Cdd:PLN03232 1277 SMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERA---HIKDV 1353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 483 FARLPNGYDTEVGDSSADlLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSL 562
Cdd:PLN03232 1354 IDRNPFGLDAEVSEGGEN-FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNT 1432
|
410
....*....|....*
gi 1733551959 563 LALADQRFSLEDGRL 577
Cdd:PLN03232 1433 IIDCDKILVLSSGQV 1447
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
360-577 |
7.81e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 108.76 E-value: 7.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQIS 439
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRPTLFHGTILDNLTMfrsdqveimqrALELAAKLHLDEVFARL--------PNGYDTEVGDsSADLLPAGVAQRIT 511
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLLL-----------AAPNASDEALIEVLQQVgleklledDKGLNAWLGE-GGRQLSGGEQRRLG 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 512 IVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
361-576 |
1.01e-24 |
|
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: 102.17 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSpkDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDfDAESVFNQISY 440
Cdd:COG4133 3 LEAENLSCRRG--ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTLFHG-TILDNLTMFRS-DQVEI-MQRALELAAKLHLDEvFARLPngydtevgdssADLLPAGVAQRITIVRALI 517
Cdd:COG4133 80 LGHADGLKPElTVRENLRFWAAlYGLRAdREAIDEALEAVGLAG-LADLP-----------VRQLSAGQKRRVALARLLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 518 NRPSLILFDESNTSLDGYSDRALCDLMRSLK---GTVsmILVSYRPsLLALADQRFSLEDGR 576
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAV--LLTTHQP-LELAAARVLDLGDFK 206
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
237-576 |
1.13e-24 |
|
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: 108.75 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 237 TVKAMAMEAMMLRRYERLLEsnAFASAQV-SQIS----GHAQTVgtITShLTVAAVVGFGSLMVINGTLSVGALAASTLL 311
Cdd:COG5265 230 TVKYFGNEAREARRYDEALA--RYERAAVkSQTSlallNFGQAL--IIA-LGLTAMMLMAAQGVVAGTMTVGDFVLVNAY 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 312 AGRTVQPaLRALGLWSRFQSVSLAE-DNLRDIDAIPAESRgrfkmDRFTSLDLK---------NLHFRYSPkDPEVLHNI 381
Cdd:COG5265 305 LIQLYIP-LNFLGFVYREIRQALADmERMFDLLDQPPEVA-----DAPDAPPLVvgggevrfeNVSFGYDP-ERPILKGV 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 382 NLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIPQRPTLFHGTILDNLTMFRS 461
Cdd:COG5265 378 SFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 462 D--QVEIMQralelAAKL-HLDEVFARLPNGYDTEVGDSSadL-LPAGVAQRITIVRALINRPSLILFDESNTSLDGYSD 537
Cdd:COG5265 458 DasEEEVEA-----AARAaQIHDFIESLPDGYDTRVGERG--LkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTE 530
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1733551959 538 RALCDLMRSL-KGTVSMIlVSYRPSLLALADQRFSLEDGR 576
Cdd:COG5265 531 RAIQAALREVaRGRTTLV-IAHRLSTIVDADEILVLEAGR 569
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
361-577 |
1.98e-24 |
|
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: 107.30 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPT---KGSALLNGQPPHDFDAESVFNQ 437
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYIPQRPT--LFHGTILDN----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPngydtevgdssaDLLPAGVAQRIT 511
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQiaeaLENLGLSRAEARARVLELLEAVGLERRLDRYP------------HQLSGGQRQRVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551959 512 IVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGT--VSMILVSYRPSLLA-LADQRFSLEDGRL 577
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAeIADRVVVMDDGRI 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
361-577 |
2.41e-24 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 101.81 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKD--PEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESV---F 435
Cdd:cd03257 2 LEVKNLSVSFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 436 NQISYIPQ------RPTLfhgTILDNLT-MFR-----SDQVEIMQRALELAAKLHLDEVFA-RLPNGydtevgdssadlL 502
Cdd:cd03257 82 KEIQMVFQdpmsslNPRM---TIGEQIAePLRihgklSKKEARKEAVLLLLVGVGLPEEVLnRYPHE------------L 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551959 503 PAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLK---GTvSMILVSYRPSLLA-LADQRFSLEDGRL 577
Cdd:cd03257 147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQeelGL-TLLFITHDLGVVAkIADRVAVMYAGKI 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
362-577 |
4.24e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 99.43 E-value: 4.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 362 DLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYI 441
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 442 PQrptlfhgtildnltmfrsdqveimqrALELAAKLHLdevfarlpngydtevGDSSADLLPAGVAQRITIVRALINRPS 521
Cdd:cd03214 79 PQ--------------------------ALELLGLAHL---------------ADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551959 522 LILFDESNTSLDGYSDRALCDLMRSLKGTVSM--ILVSYRPSL-LALADQRFSLEDGRL 577
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERGKtvVMVLHDLNLaARYADRVILLKDGRI 176
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
361-557 |
1.10e-23 |
|
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: 104.99 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPE---VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFN- 436
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 437 --QISYIPQRPT--LFHG-TILDNLT-----MFRSDQVEIMQRALELAAKLHLDEVFA-RLPNGydtevgdssadlLPAG 505
Cdd:COG1123 341 rrRVQMVFQDPYssLNPRmTVGDIIAeplrlHGLLSRAERRERVAELLERVGLPPDLAdRYPHE------------LSGG 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 506 VAQRITIVRALINRPSLILFDESNTSLDgYSDRA-LCDLMRSLKGT--VSMILVS 557
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALD-VSVQAqILNLLRDLQRElgLTYLFIS 462
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
361-547 |
1.48e-23 |
|
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: 100.12 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISY 440
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTL-FHGTILD-----------NLTMFRSDQVEIMQRALELaakLHLDEvFArlpngydtevgDSSADLLPAGVAQ 508
Cdd:COG1120 80 VPQEPPApFGLTVRElvalgryphlgLFGRPSAEDREAVEEALER---TGLEH-LA-----------DRPVDELSGGERQ 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 1733551959 509 RITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL 547
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRL 183
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
359-556 |
3.10e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 99.34 E-value: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 359 TSLDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLL---N----LVAGQIVptKGSALLNGQPPHD--F 429
Cdd:COG1117 10 PKIEVRNLNVYYGDK--QALKDINLDIPENKVTALIGPSGCGKSTLLrclNrmndLIPGARV--EGEILLDGEDIYDpdV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 430 DAESVFNQISYIPQRPTLFHGTILDNLTM--------FRSDQVEIMQRALELAAklhL-DEVFARLpngydtevgDSSAD 500
Cdd:COG1117 86 DVVELRRRVGMVFQKPNPFPKSIYDNVAYglrlhgikSKSELDEIVEESLRKAA---LwDEVKDRL---------KKSAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 501 LLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILV 556
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIV 209
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
52-335 |
8.55e-23 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 98.79 E-value: 8.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 52 ILAASLGINILALALPLLILQVYNRILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQYEHRAGCIAIKRLA 131
Cdd:cd18568 7 ILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 132 TGDLAHVESTPSGMHLDRLSSIELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIMLGIAGFMAWKIGKSLQ 211
Cdd:cd18568 87 SLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 212 EQLEERREWDRRRYSFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFG 291
Cdd:cd18568 167 RNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1733551959 292 SLMVINGTLSVGALAASTLLAGRTVQPALRALGLWSRFQSVSLA 335
Cdd:cd18568 247 AYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRIS 290
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
361-576 |
1.02e-22 |
|
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: 95.33 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYspKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQP--PHDFDAESVFNQI 438
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 439 SYIPQRPTLF-HGTILDNLTMfrsdqveimqralelaaklhldevfarlpngydtevgdssadLLPAGVAQRITIVRALI 517
Cdd:cd03229 79 GMVFQDFALFpHLTVLENIAL------------------------------------------GLSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 518 NRPSLILFDESNTSLDGYSDRALCDLMRSLKGT--VSMILVSYRPS-LLALADQRFSLEDGR 576
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
359-533 |
4.32e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 97.86 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 359 TSLDLKNLHFRYspKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ-----PPHDFDaes 433
Cdd:COG3842 4 PALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglPPEKRN--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 434 vfnqISYIPQRPTLF-HGTILDN----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPngydtevgdssaDLLPAGVAQ 508
Cdd:COG3842 79 ----VGMVFQDYALFpHLTVAENvafgLRMRGVPKAEIRARVAELLELVGLEGLADRYP------------HQLSGGQQQ 142
|
170 180
....*....|....*....|....*..
gi 1733551959 509 RITIVRALINRPSLILFDE--SNtsLD 533
Cdd:COG3842 143 RVALARALAPEPRVLLLDEplSA--LD 167
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
75-331 |
6.00e-22 |
|
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: 96.47 E-value: 6.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 75 NRILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQ---------YEHragciaIKRLatgDLAHVESTPSGM 145
Cdd:cd07346 27 DDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRvvfdlrrdlFRH------LQRL---SLSFFDRNRTGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 146 HLDRLSS-IELIRDFYASQASLVLIDLpFILLFLGILALITGW-LVLIPIIMLGIAGFMAWKIGKSLQEQLEERREWDRR 223
Cdd:cd07346 98 LMSRLTSdVDAVQNLVSSGLLQLLSDV-LTLIGALVILFYLNWkLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 224 RYSFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVG 303
Cdd:cd07346 177 LSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIG 256
|
250 260
....*....|....*....|....*...
gi 1733551959 304 ALAASTLLAGRTVQPALRALGLWSRFQS 331
Cdd:cd07346 257 ELVAFLAYLGMLFGPIQRLANLYNQLQQ 284
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
363-577 |
1.09e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.96 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLHFRYsPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAesvfNQISYIP 442
Cdd:COG2884 4 FENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKR----REIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 443 QR--------PTLFHGTILDNLtMF-----RSDQVEIMQRALELAAKLHLDEVFARLPngydtevgdssaDLLPAGVAQR 509
Cdd:COG2884 79 RRigvvfqdfRLLPDRTVYENV-ALplrvtGKSRKEIRRRVREVLDLVGLSDKAKALP------------HELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 510 ITIVRALINRPSLILFDESNTSLD-GYSDRALcDLMRSL--KGTvSMILVSYRPSLLALADQR-FSLEDGRL 577
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDpETSWEIM-ELLEEInrRGT-TVLIATHDLELVDRMPKRvLELEDGRL 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
359-533 |
1.20e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 96.68 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 359 TSLDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ-----PPHDFDaes 433
Cdd:COG3839 2 ASLELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlPPKDRN--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 434 vfnqISYIPQRPTLF-HGTILDN----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQ 508
Cdd:COG3839 77 ----IAMVFQSYALYpHMTVYENiafpLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQ------------LSGGQRQ 140
|
170 180
....*....|....*....|....*..
gi 1733551959 509 RITIVRALINRPSLILFDE--SNtsLD 533
Cdd:COG3839 141 RVALGRALVREPKVFLLDEplSN--LD 165
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
361-527 |
2.03e-21 |
|
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: 92.88 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYspKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ-----PPHdfdaESVF 435
Cdd:cd03224 1 LEVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglPPH----ERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 436 NQISYIPQRPTLFHG-TILDNLTM-----FRSDQVEIMQRALELaaklhldevFARLPNGYDTEVGDssadlLPAGVAQR 509
Cdd:cd03224 75 AGIGYVPEGRRIFPElTVEENLLLgayarRRAKRKARLERVYEL---------FPRLKERRKQLAGT-----LSGGEQQM 140
|
170
....*....|....*...
gi 1733551959 510 ITIVRALINRPSLILFDE 527
Cdd:cd03224 141 LAIARALMSRPKLLLLDE 158
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
361-557 |
2.76e-21 |
|
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: 92.59 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ--PPHDFDAESVFNQI 438
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLklTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 439 SYIPQRPTLF-HGTILDNLTM-----FRSDQVEIMQRALELAAKLHLDevfarlpngydtEVGDSSADLLPAGVAQRITI 512
Cdd:cd03262 79 GMVFQQFNLFpHLTVLENITLapikvKGMSKAEAEERALELLEKVGLA------------DKADAYPAQLSGGQQQRVAI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1733551959 513 VRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGT-VSMILVS 557
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVT 192
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
377-533 |
3.05e-21 |
|
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: 92.78 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESvfNQISYIPQRPTLF-HGTILDN 455
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 456 ----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPngydtevgdssaDLLPAGVAQRITIVRALINRPSLILFDESNTS 531
Cdd:cd03299 92 iaygLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKP------------ETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
..
gi 1733551959 532 LD 533
Cdd:cd03299 160 LD 161
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
361-533 |
4.49e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.08 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSpkDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISY 440
Cdd:PRK10247 8 LQLQNVGYLAG--DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTLFHGTILDNLTM---FRSDQVEiMQRALELAAKLHLDEvfarlpngydtEVGDSSADLLPAGVAQRITIVRALI 517
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFpwqIRNQQPD-PAIFLDDLERFALPD-----------TILTKNIAELSGGEKQRISLIRNLQ 153
|
170
....*....|....*.
gi 1733551959 518 NRPSLILFDESNTSLD 533
Cdd:PRK10247 154 FMPKVLLLDEITSALD 169
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
377-577 |
5.42e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.63 E-value: 5.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQP-----PHdfDAESvfNQISYIPQRPTLF-HG 450
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPvrfrsPR--DAQA--AGIAIIHQELNLVpNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 451 TILDNLTM-------FRSDQVEIMQRALELAAKLHLDEvfarLPngyDTEVGDssadlLPAGVAQRITIVRALINRPSLI 523
Cdd:COG1129 95 SVAENIFLgreprrgGLIDWRAMRRRARELLARLGLDI----DP---DTPVGD-----LSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551959 524 LFDESNTSLDGYSDRALCDLMRSLKGT-VSMILVSYR-PSLLALADqRFS-LEDGRL 577
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRlDEVFEIAD-RVTvLRDGRL 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
361-577 |
8.08e-21 |
|
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: 91.16 E-value: 8.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ-----PPHDFDAESVF 435
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 436 NQISYIPqrptlfHGTILDN----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPngydtevgdssaDLLPAGVAQRIT 511
Cdd:cd03301 79 QNYALYP------HMTVYDNiafgLKLRKVPKDEIDERVREVAELLQIEHLLDRKP------------KQLSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551959 512 IVRALINRPSLILFDESNTSLDG---YSDRA-LCDLMRSLKGTvsMILVSY-RPSLLALADQRFSLEDGRL 577
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAklrVQMRAeLKRLQQRLGTT--TIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
278-577 |
3.34e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 94.64 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 278 ITSHLTVAAVVGFGSLMVINGTLSVGALAA----STLLAGRTVQpalralgLWSRFQSVSLAEDNLRD----IDAIPAES 349
Cdd:PRK13657 248 AASTITMLAILVLGAALVQKGQLRVGEVVAfvgfATLLIGRLDQ-------VVAFINQVFMAAPKLEEffevEDAVPDVR 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 350 rgrfkmDRFTSLDLKNLH---------FRYSPKDPEVlHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSAL 420
Cdd:PRK13657 321 ------DPPGAIDLGRVKgavefddvsFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 421 LNGQPPHDFDAESVFNQISYIPQRPTLFHGTILDNLTMFRSDQV-EIMQRALELAAKLhldEVFARLPNGYDTEVGDsSA 499
Cdd:PRK13657 394 IDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATdEEMRAAAERAQAH---DFIERKPDGYDTVVGE-RG 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 500 DLLPAGVAQRITIVRALI-NRPSLILfDESNTSLDGYSDR----ALCDLMrslKGTVSMIlVSYRPSLLALADQRFSLED 574
Cdd:PRK13657 470 RQLSGGERQRLAIARALLkDPPILIL-DEATSALDVETEAkvkaALDELM---KGRTTFI-IAHRLSTVRNADRILVFDN 544
|
...
gi 1733551959 575 GRL 577
Cdd:PRK13657 545 GRV 547
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
379-579 |
5.25e-20 |
|
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: 88.89 E-value: 5.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 379 HNINLRLE-QGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ-----------PPHDfdaesvfNQISYIPQRPT 446
Cdd:cd03297 13 FTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlPPQQ-------RKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 447 LF-HGTILDNLT--MFRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQRITIVRALINRPSLI 523
Cdd:cd03297 86 LFpHLNVRENLAfgLKRKRNREDRISVDELLDLLGLDHLLNRYPAQ------------LSGGEKQRVALARALAAQPELL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551959 524 LFDESNTSLDGYSDRALCDLMRSLKGT--VSMILVSYRPS-LLALADQRFSLEDGRLKP 579
Cdd:cd03297 154 LLDEPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSeAEYLADRIVVMEDGRLQY 212
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
377-527 |
1.21e-19 |
|
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: 88.26 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ-----PPHD---------Fdaesvfnqisyip 442
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglPPHEiarlgigrtF------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 443 QRPTLFHG-TILDNLTM--------------FRSDQVEIMQRALELAAKLHLDevfarlpngydtEVGDSSADLLPAGVA 507
Cdd:cd03219 82 QIPRLFPElTVLENVMVaaqartgsglllarARREEREARERAEELLERVGLA------------DLADRPAGELSYGQQ 149
|
170 180
....*....|....*....|
gi 1733551959 508 QRITIVRALINRPSLILFDE 527
Cdd:cd03219 150 RRLEIARALATDPKLLLLDE 169
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
361-533 |
2.53e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.01 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ-----PPHDFDAESVF 435
Cdd:PRK09452 15 VELRGISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 436 NqiSYipqrpTLF-HGTILDN----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQRI 510
Cdd:PRK09452 93 Q--SY-----ALFpHMTVFENvafgLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQ------------LSGGQQQRV 153
|
170 180
....*....|....*....|...
gi 1733551959 511 TIVRALINRPSLILFDESNTSLD 533
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALD 176
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
361-576 |
2.94e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 87.45 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSAL-LNGqppHDFDAESVF---N 436
Cdd:COG1119 4 LELRNVTVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFG---ERRGGEDVWelrK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 437 QI--------SYIPQRPTLFHgTIL----DNLTMFRSDQVEIMQRALELAAKLHLDEVFARLpngYDTevgdssadlLPA 504
Cdd:COG1119 79 RIglvspalqLRFPRDETVLD-VVLsgffDSIGLYREPTDEQRERARELLELLGLAHLADRP---FGT---------LSQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 505 GVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL--KGTVSMILVSYRPS-LLALADQRFSLEDGR 576
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVEeIPPGITHVLLLKDGR 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
377-533 |
3.59e-19 |
|
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: 86.91 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESvfNQISYIPQRPTLF-HGTILDN 455
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVFQNYALFpHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 456 ----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPngydtevgdssaDLLPAGVAQRITIVRALINRPSLILFDESNTS 531
Cdd:cd03300 93 iafgLRLKKLPKAEIKERVAEALDLVQLEGYANRKP------------SQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
..
gi 1733551959 532 LD 533
Cdd:cd03300 161 LD 162
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
361-527 |
5.39e-19 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 86.44 E-value: 5.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQpphDFDAESVFNQ--- 437
Cdd:cd03218 1 LRAENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ---DITKLPMHKRarl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 -ISYIPQRPTLFHG-TILDN----LTMFRSDQVEIMQRALELAAKLHLdevfarlpngydTEVGDSSADLLPAGVAQRIT 511
Cdd:cd03218 76 gIGYLPQEASIFRKlTVEENilavLEIRGLSKKEREEKLEELLEEFHI------------THLRKSKASSLSGGERRRVE 143
|
170
....*....|....*.
gi 1733551959 512 IVRALINRPSLILFDE 527
Cdd:cd03218 144 IARALATNPKFLLLDE 159
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
361-533 |
5.51e-19 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 85.71 E-value: 5.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDpeVLHNINLRLEQGqIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDfDAESVFNQISY 440
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTLF-HGTILDNL----TMFRSDQVEIMQRALELAAKLHLDEVfarlpngYDTEVGDSSadllpAGVAQRITIVRA 515
Cdd:cd03264 77 LPQEFGVYpNFTVREFLdyiaWLKGIPSKEVKARVDEVLELVNLGDR-------AKKKIGSLS-----GGMRRRVGIAQA 144
|
170
....*....|....*...
gi 1733551959 516 LINRPSLILFDESNTSLD 533
Cdd:cd03264 145 LVGDPSILIVDEPTAGLD 162
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
73-333 |
7.82e-19 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 87.22 E-value: 7.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 73 VYNRILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQYEhragciaiKRLATGDLAHVESTP--------SG 144
Cdd:cd18779 28 LVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLD--------TQLTLGFLEHLLRLPyrffqqrsTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 145 MHLDRLSSIELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIpiimlgIAGFMAWKIG------KSLQEQLEERR 218
Cdd:cd18779 100 DLLMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLV------VLGLAALQVAlllatrRRVRELMAREL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 219 EWDRRRYSFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVING 298
Cdd:cd18779 174 AAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDG 253
|
250 260 270
....*....|....*....|....*....|....*
gi 1733551959 299 TLSVGALAASTLLAGRTVQPALRALGLWSRFQSVS 333
Cdd:cd18779 254 QLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLG 288
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
361-577 |
8.69e-19 |
|
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: 85.56 E-value: 8.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEV--LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPH--DFDAESVF- 435
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFalDEDARARLr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 436 -NQISYIPQR----PTLfhgTILDNLTM---FRSDQvEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVA 507
Cdd:COG4181 89 aRHVGFVFQSfqllPTL---TALENVMLpleLAGRR-DARARARALLERVGLGHRLDHYPAQ------------LSGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733551959 508 QRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLK---GTvSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNrerGT-TLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
354-595 |
9.59e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 90.86 E-value: 9.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 354 KMDRFTSLDLKNLHFRY-SPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLN-GQPPHDFDA 431
Cdd:PTZ00265 376 KLKDIKKIQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 432 ESVFNQISYIPQRPTLFHGTILDNL--TMFRSDQVEIMQRALE------------------------------------- 472
Cdd:PTZ00265 456 KWWRSKIGVVSQDPLLFSNSIKNNIkySLYSLKDLEALSNYYNedgndsqenknkrnscrakcagdlndmsnttdsneli 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 473 ----------------LAAKLHLDEVFARLPNGYDTEVGdSSADLLPAGVAQRITIVRALINRPSLILFDESNTSLDGYS 536
Cdd:PTZ00265 536 emrknyqtikdsevvdVSKKVLIHDFVSALPDKYETLVG-SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 537 DRALCDLMRSLKGTVS--MILVSYRPSLLALADQRFSL---EDGRLKPLDFADHKNLSRTNENS 595
Cdd:PTZ00265 615 EYLVQKTINNLKGNENriTIIIAHRLSTIRYANTIFVLsnrERGSTVDVDIIGEDPTKDNKENN 678
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
376-578 |
1.14e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.25 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 376 EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFD----AESVFNQISYIPQrptlFHG- 450
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakAELRNQKLGFIYQ----FHHl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 451 ----TILDNLTM----FRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQRITIVRALINRPSL 522
Cdd:PRK11629 99 lpdfTALENVAMplliGKKKPAEINSRALEMLAAVGLEHRANHRPSE------------LSGGERQRVAIARALVNNPRL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551959 523 ILFDESNTSLDGYSDRALCDLMRSL---KGTvSMILVSYRPSLLALADQRFSLEDGRLK 578
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELnrlQGT-AFLVVTHDLQLAKRMSRQLEMRDGRLT 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
361-577 |
1.26e-18 |
|
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: 83.25 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQpPHDFD--AESVFNQI 438
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-EVSFAspRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 439 SYIPQrptlfhgtildnltmfrsdqveimqralelaaklhldevfarlpngydtevgdssadlLPAGVAQRITIVRALIN 518
Cdd:cd03216 78 AMVYQ----------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 519 RPSLILFDESNTSLDGYSDRALCDLMRSLKGT-VSMILVSYRPS-LLALADqRFS-LEDGRL 577
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDeVFEIAD-RVTvLRDGRV 160
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
360-576 |
1.59e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 89.39 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSpKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQIS 439
Cdd:PRK10790 340 RIDIDNVSFAYR-DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRPTLFHGTILDNLTMFRSDQVEIMQRALElaaKLHLDEVFARLPNGYDTEVGDsSADLLPAGVAQRITIVRALINR 519
Cdd:PRK10790 419 MVQQDPVVLADTFLANVTLGRDISEEQVWQALE---TVQLAELARSLPDGLYTPLGE-QGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551959 520 PSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGR 576
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQ 551
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
360-599 |
1.68e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 87.12 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSpkDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ------PPHDfdaes 433
Cdd:COG1118 2 SIEVRNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftnlPPRE----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 434 vfNQISYIPQRPTLF-HGTILDN----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQ 508
Cdd:COG1118 75 --RRVGFVFQHYALFpHMTVAENiafgLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQ------------LSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 509 RITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL----KGTVsmILVS------YRpsllaLADQRFSLEDGRL- 577
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhdelGGTT--VFVThdqeeaLE-----LADRVVVMNQGRIe 213
|
250 260 270
....*....|....*....|....*....|....*..
gi 1733551959 578 ----------KP-----LDFADHKNLSRTNENSGHLQ 599
Cdd:COG1118 214 qvgtpdevydRPatpfvARFLGCVNVLRGRVIGGQLE 250
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
360-595 |
2.18e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 89.80 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQIS 439
Cdd:PLN03130 1237 SIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRPTLFHGTILDNLTMFRSDQVEIMQRALELAaklHLDEVFARLPNGYDTEVGDSSADLlpaGVAQR--ITIVRALI 517
Cdd:PLN03130 1317 IIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERA---HLKDVIRRNSLGLDAEVSEAGENF---SVGQRqlLSLARALL 1390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1733551959 518 NRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRLkpLDFADHKNLsRTNENS 595
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRV--VEFDTPENL-LSNEGS 1465
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
360-577 |
2.67e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 83.37 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHF----RYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVP--TKGSALLNGQPphdFDAES 433
Cdd:cd03213 3 TLSFRNLTVtvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRP---LDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 434 VFNQISYIPQrptlfHGTILDNLTmfrsdqveiMQRALELAAKLhldevfarlpngydtevgdSSadlLPAGVAQRITIV 513
Cdd:cd03213 80 FRKIIGYVPQ-----DDILHPTLT---------VRETLMFAAKL-------------------RG---LSGGERKRVSIA 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551959 514 RALINRPSLILFDESNTSLDGYSDRALCDLMRSL-KGTVSMILVSYRPS--LLALADQRFSLEDGRL 577
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSseIFELFDKLLLLSQGRV 190
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
296-582 |
3.08e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.33 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 296 INGTLSVGALAASTLLAGRtVQPALRalglWSRFQSVSLAE------------DNLRDIDAIPaESRGRFKMDRFTSLDL 363
Cdd:COG4178 292 FAGEITLGGLMQAASAFGQ-VQGALS----WFVDNYQSLAEwratvdrlagfeEALEAADALP-EAASRIETSEDGALAL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 364 KNLHFRySPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGqIVP-TKGSALLngqPPHDfdaesvfnQISYIP 442
Cdd:COG4178 366 EDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPyGSGRIAR---PAGA--------RVLFLP 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 443 QRPTLFHGTILDNLTM-FRSDQV--EIMQRALElaaKLHLDEVFARLpngyDTEvgDSSADLLPAGVAQRITIVRALINR 519
Cdd:COG4178 433 QRPYLPLGTLREALLYpATAEAFsdAELREALE---AVGLGHLAERL----DEE--ADWDQVLSLGEQQRLAFARLLLHK 503
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 520 PSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLE---DGRLKPLDF 582
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTgdgSWQLLPAEA 569
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
361-548 |
4.17e-18 |
|
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: 83.89 E-value: 4.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYsPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISY 440
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTLF-HGTILDNLTMFRS----DQVEIMQRALELAAKLHLDevfarlPNGYdtevGDSSADLLPAGVAQRITIVRA 515
Cdd:cd03295 80 VIQQIGLFpHMTVEENIALVPKllkwPKEKIRERADELLALVGLD------PAEF----ADRYPHELSGGQQQRVGVARA 149
|
170 180 190
....*....|....*....|....*....|...
gi 1733551959 516 LINRPSLILFDESNTSLDGYSDRALCDLMRSLK 548
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQ 182
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
383-577 |
4.98e-18 |
|
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: 82.93 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 383 LRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ-----PPHDFDAESVFnqisyipQRPTLF-HGTILDNL 456
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaaPPADRPVSMLF-------QENNLFaHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 457 TMFRSDQV---EIMQRALE-LAAKLHLDEVFARLPngydtevgdssaDLLPAGVAQRITIVRALINRPSLILFDESNTSL 532
Cdd:cd03298 92 GLGLSPGLkltAEDRQAIEvALARVGLAGLEKRLP------------GELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1733551959 533 DGYSDRALCDLMRSLKGTVSM--ILVSYRPS-LLALADQRFSLEDGRL 577
Cdd:cd03298 160 DPALRAEMLDLVLDLHAETKMtvLMVTHQPEdAKRLAQRVVFLDNGRI 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
361-547 |
6.02e-18 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 83.39 E-value: 6.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYsPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPH---DFDAESVFNQ 437
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYIPQRPTLF-HGTILDNL------------TMFRSDQVEIMQRALELAAKLHLDE-VFARlpngydtevgdssADLLP 503
Cdd:cd03256 80 IGMIFQQFNLIeRLSVLENVlsgrlgrrstwrSLFGLFPKEEKQRALAALERVGLLDkAYQR-------------ADQLS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1733551959 504 AGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL 547
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRI 190
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
363-579 |
6.59e-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: 6.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQpphdfdaesvfNQISYIP 442
Cdd:COG0488 1 LENLSKSFGGR--PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 443 QRPTLF-HGTILDNLTMFRSDQVEIMQRALELAAKL-----------HLDEVFARLpNGYD---------------TEVG 495
Cdd:COG0488 68 QEPPLDdDLTVLDTVLDGDAELRALEAELEELEAKLaepdedlerlaELQEEFEAL-GGWEaearaeeilsglgfpEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 496 DSSADLLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVsmILVSYRPSLL-ALADQRFSLED 574
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTV--LVVSHDRYFLdRVATRILELDR 224
|
....*
gi 1733551959 575 GRLKP 579
Cdd:COG0488 225 GKLTL 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
122-559 |
1.05e-17 |
|
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: 87.69 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 122 AGCIAIKRLATGDLAH---------VESTPSGMHLDRLSsieliRDFYASQASLVlidlPFILLFLGILALITGWLVLI- 191
Cdd:TIGR00957 1031 IGGIQASRVLHQDLLHnklrspmsfFERTPSGNLVNRFS-----KELDTVDSMIP----PVIKMFMGSLFNVIGALIVIl 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 192 ---PIIM-----LGIAGFMAWKIGKSLQEQLEERREWDRR-RYSFLIEVLSGIHTVKAMAMEammlRRYERLLESNAFAS 262
Cdd:TIGR00957 1102 latPIAAviippLGLLYFFVQRFYVASSRQLKRLESVSRSpVYSHFNETLLGVSVIRAFEEQ----ERFIHQSDLKVDEN 1177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 263 AQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVING--TLSVGalaastlLAGRTVQPALRA-------LGLWSRFQSVS 333
Cdd:TIGR00957 1178 QKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISrhSLSAG-------LVGLSVSYSLQVtfylnwlVRMSSEMETNI 1250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 334 LAEDNLRDIDAIPAESRGRFKMDRFTS-------LDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLN 406
Cdd:TIGR00957 1251 VAVERLKEYSETEKEAPWQIQETAPPSgwpprgrVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTL 1330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 407 LVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIPQRPTLFHGTILDNLTMFRSDQVEIMQRALELAaklHLDEVFARL 486
Cdd:TIGR00957 1331 GLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELA---HLKTFVSAL 1407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733551959 487 PNGYDTEVGDSSADlLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYR 559
Cdd:TIGR00957 1408 PDKLDHECAEGGEN-LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHR 1479
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
361-558 |
1.97e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.06 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHD---------FDA 431
Cdd:PRK09493 2 IEFKNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvderlirQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 432 ESVFNQISYIPqrptlfHGTILDNLtMFRSDQV------EIMQRALELAAKLHLDEvfaRLpNGYDTEvgdssadlLPAG 505
Cdd:PRK09493 80 GMVFQQFYLFP------HLTALENV-MFGPLRVrgaskeEAEKQARELLAKVGLAE---RA-HHYPSE--------LSGG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 506 VAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL--KGtVSMILVSY 558
Cdd:PRK09493 141 QQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLaeEG-MTMVIVTH 194
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
373-557 |
2.28e-17 |
|
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: 81.11 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 373 KDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQppHDFDAESVFNQISYIPQRPTLFhgti 452
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALIEAPGFY---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 453 lDNLTMFrsDQVEIMQRALELAAKLH---LDEVfaRLPNGYDTEVGDSSadllpAGVAQRITIVRALINRPSLILFDESN 529
Cdd:cd03268 85 -PNLTAR--ENLRLLARLLGIRKKRIdevLDVV--GLKDSAKKKVKGFS-----LGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180
....*....|....*....|....*...
gi 1733551959 530 TSLDGYSDRALCDLMRSLKGTVSMILVS 557
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLIS 182
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
361-577 |
2.76e-17 |
|
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: 80.87 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEV--LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGqpphdFDAES----V 434
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-----FDVVKepaeA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 435 FNQISYIPQRPTLFHG-TILDNLTMFRS----DQVEIMQRALELAAKLHLDEVFARLPNGYDTevgdssadllpaGVAQR 509
Cdd:cd03266 77 RRRLGFVSDSTGLYDRlTARENLEYFAGlyglKGDELTARLEELADRLGMEELLDRRVGGFST------------GMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 510 ITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYR--PSLLALADQRFSLEDGRL 577
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHimQEVERLCDRVVVLHRGRV 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
363-547 |
3.62e-17 |
|
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: 81.09 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLH--FRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFN---Q 437
Cdd:cd03258 4 LKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKarrR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYIPQRPTLFHG-TILDN----LTMFRSDQVEIMQRALELaakLHLdevfarlpngydteVGDSS-ADLLPA----GVA 507
Cdd:cd03258 84 IGMIFQHFNLLSSrTVFENvalpLEIAGVPKAEIEERVLEL---LEL--------------VGLEDkADAYPAqlsgGQK 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1733551959 508 QRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL 547
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDI 186
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
361-577 |
3.65e-17 |
|
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: 80.53 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYsPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAesvfNQISY 440
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRG----RAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQR-PTLFHGT-ILDNLTMFrsDQVEImqrALELAAKLHlDEVFARLPNGYDtEVGDSS-ADLLPAGVA----QRITIV 513
Cdd:cd03292 76 LRRKiGVVFQDFrLLPDRNVY--ENVAF---ALEVTGVPP-REIRKRVPAALE-LVGLSHkHRALPAELSggeqQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 514 RALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLL--ALADQRFSLEDGRL 577
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELvdTTRHRVIALERGKL 214
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
84-318 |
4.73e-17 |
|
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: 81.54 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 84 STLAMLTIGVAIALVLDVLLKIARARLSGWAGAQYEHRAGCIAIKRLATGDLAHVESTPSGMHLDRLSS-IELIRDFYAS 162
Cdd:pfam00664 38 QALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNdTSKIRDGLGE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 163 QASLVLIDLpFILLFLGILALITGW-LVLIPIIMLGIAGFMAWKIGKSLQEQLEERREWDRRRYSFLIEVLSGIHTVKAM 241
Cdd:pfam00664 118 KLGLLFQSL-ATIVGGIIVMFYYGWkLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAF 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551959 242 AMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGALAASTLLAGRTVQP 318
Cdd:pfam00664 197 GREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGP 273
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
337-581 |
5.66e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 337 DNLRDIDaiPAESRGRFKMDRFTS-------LDLKNLHFRYspKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVA 409
Cdd:COG0488 287 EKLEREE--PPRRDKTVEIRFPPPerlgkkvLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 410 GQIVPTKGSALLngqpphdfdAESVfnQISYIPQRPTLFHG--TILDNLTMFRSDQVEIMQRALeLAAKL-HLDEVFarl 486
Cdd:COG0488 363 GELEPDSGTVKL---------GETV--KIGYFDQHQEELDPdkTVLDELRDGAPGGTEQEVRGY-LGRFLfSGDDAF--- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 487 pngydTEVGDssadlLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVsmILVSYRPSLL-AL 565
Cdd:COG0488 428 -----KPVGV-----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTV--LLVSHDRYFLdRV 495
|
250
....*....|....*.
gi 1733551959 566 ADQRFSLEDGRLKPLD 581
Cdd:COG0488 496 ATRILEFEDGGVREYP 511
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
361-533 |
6.52e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.90 E-value: 6.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPE---VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQpphDFDAESVFNQ 437
Cdd:COG1101 2 LELKNLSKTFNPGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK---DVTKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYI------PQRPTLFHGTILDNLTM---------FRSdQVEIMQRAL--ELAAKLHLDevfarLPNGYDTEVGdssad 500
Cdd:COG1101 79 AKYIgrvfqdPMMGTAPSMTIEENLALayrrgkrrgLRR-GLTKKRRELfrELLATLGLG-----LENRLDTKVG----- 147
|
170 180 190
....*....|....*....|....*....|...
gi 1733551959 501 LLPAGVAQRITIVRALINRPSLILFDESNTSLD 533
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-577 |
8.87e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.48 E-value: 8.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 374 DPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQI------VPTKGSALLNGQPPHDFDAESVFNQISYIPQRPTL 447
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 448 F-HGTILDNLTM-FRS----DQVEIMQRALELAAKLHL-DEVFARLpngydtevgDSSADLLPAGVAQRITIVRALINRP 520
Cdd:PRK14246 102 FpHLSIYDNIAYpLKShgikEKREIKKIVEECLRKVGLwKEVYDRL---------NSPASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1733551959 521 SLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLA-LADQRFSLEDGRL 577
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVArVADYVAFLYNGEL 230
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
365-575 |
1.83e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 78.53 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 365 NLHFRYSPKDPeVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQ----ISY 440
Cdd:cd03290 5 NGYFSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTLFHGTILDNLTM---FRSDQVEIMQRALELAAKLHLdevfarLPNGYDTEVGDSSADlLPAGVAQRITIVRALI 517
Cdd:cd03290 84 AAQKPWLLNATVEENITFgspFNKQRYKAVTDACSLQPDIDL------LPFGDQTEIGERGIN-LSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733551959 518 NRPSLILFDESNTSLDGY-SDR----ALCDLMRSLKGTVsmILVSYRPSLLALADQRFSLEDG 575
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHlSDHlmqeGILKFLQDDKRTL--VLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
76-335 |
1.85e-16 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 80.18 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 76 RILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQYEhragciaiKRLATGDLAHV--------ESTPSGMHL 147
Cdd:cd18570 31 DIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLD--------IRLILGYFKHLlklplsffETRKTGEII 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 148 DRLSSIELIRDFYASQASLVLIDLPFILLFLGILALI---TGWLVLIPIIMLGIAGFMAWKIGKSLQEQLEERREWDRrr 224
Cdd:cd18570 103 SRFNDANKIREAISSTTISLFLDLLMVIISGIILFFYnwkLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELN-- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 225 ySFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGA 304
Cdd:cd18570 181 -SYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQ 259
|
250 260 270
....*....|....*....|....*....|.
gi 1733551959 305 LAASTLLAGRTVQPALRALGLWSRFQSVSLA 335
Cdd:cd18570 260 LIAFNALLGYFLGPIENLINLQPKIQEAKVA 290
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
169-578 |
1.95e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 83.49 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 169 IDLPFILLF--LGILALItGWLVLIpiIMLGIAGFMAWKIGKSLQEQLEERREWDRRRYsfliEVLSGIHTVKAMAMEAM 246
Cdd:PLN03232 428 IIVSMVLLYqqLGVASLF-GSLILF--LLIPLQTLIVRKMRKLTKEGLQWTDKRVGIIN----EILASMDTVKCYAWEKS 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 247 MLRRYE--RLLESNAFASAQVSQisghAQTVGTITSHLTVAAVVGFGSLMVINGTLSvGALAASTLLAGRTVQPALRAL- 323
Cdd:PLN03232 501 FESRIQgiRNEELSWFRKAQLLS----AFNSFILNSIPVVVTLVSFGVFVLLGGDLT-PARAFTSLSLFAVLRSPLNMLp 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 324 GLWS----------RFQSVSLAEDnlRDIDAIPAESRGrfkmdrFTSLDLKNLHFRYSPK-DPEVLHNINLRLEQGQIIG 392
Cdd:PLN03232 576 NLLSqvvnanvslqRIEELLLSEE--RILAQNPPLQPG------APAISIKNGYFSWDSKtSKPTLSDINLEIPVGSLVA 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 393 ITGKNGVGKSTLLnlvagqivptkgSALLNGQPPHDFDAESVFNQISYIPQRPTLFHGTILDNLtMFRSD-QVEIMQRAL 471
Cdd:PLN03232 648 IVGGTGEGKTSLI------------SAMLGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENI-LFGSDfESERYWRAI 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 472 ELAAKLHLDEVFArlpnGYD-TEVGDSSADlLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCD--LMRSLK 548
Cdd:PLN03232 715 DVTALQHDLDLLP----GRDlTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELK 789
|
410 420 430
....*....|....*....|....*....|
gi 1733551959 549 GTvSMILVSYRPSLLALADQRFSLEDGRLK 578
Cdd:PLN03232 790 GK-TRVLVTNQLHFLPLMDRIILVSEGMIK 818
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
361-568 |
2.19e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.15 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRY--SPKDPeVLHNINLRLEQGQIIGITGKNGVGKSTLLNLV------------------------------ 408
Cdd:PTZ00265 1166 IEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 409 ----------AGQIVPTK--------------GSALLNGQPPHDFDAESVFNQISYIPQRPTLFHGTILDNLTMFRSDQV 464
Cdd:PTZ00265 1245 deeqnvgmknVNEFSLTKeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 465 -EIMQRALELAAklhLDEVFARLPNGYDTEVGDSSADLlPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDL 543
Cdd:PTZ00265 1325 rEDVKRACKFAA---IDEFIESLPNKYDTNVGPYGKSL-SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260
....*....|....*....|....*..
gi 1733551959 544 MRSLKGTV--SMILVSYRPSLLALADQ 568
Cdd:PTZ00265 1401 IVDIKDKAdkTIITIAHRIASIKRSDK 1427
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
361-576 |
2.48e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 78.09 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPphdfDAESVFNQISY 440
Cdd:cd03269 1 LEVENVTKRFGRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP----LDIAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTLFHG-TILDNLTMFRS----DQVEIMQRALELAAKLHLdevfarlpngydTEVGDSSADLLPAGVAQRITIVRA 515
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVYLAQlkglKKEEARRRIDEWLERLEL------------SEYANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733551959 516 LINRPSLILFDESNTSLDGYSDRALCDLMRSLKGT-VSMILVSYRPSLL-ALADQRFSLEDGR 576
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVeELCDRVLLLNKGR 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
378-577 |
4.51e-16 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 78.15 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESvfNQISYIPQRPTLF-HGTILDNL 456
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFrHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 457 TM--------FRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQRITIVRALINRPSLILFDES 528
Cdd:cd03296 96 AFglrvkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQ------------LSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 529 NTSLDGYSDRALCDLMRSL--KGTVSMILVSY-RPSLLALADQRFSLEDGRL 577
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLhdELHVTTVFVTHdQEEALEVADRVVVMNKGRI 215
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
361-548 |
6.29e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 79.38 E-value: 6.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSpkDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQpphDFDAESVFNQ-IS 439
Cdd:PRK11432 7 VVLKNITKRFG--SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE---DVTHRSIQQRdIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRPTLF-HGTILDN----LTMFRSDQVEIMQRALELAAKLHLDevfarlpnGYdtevGDSSADLLPAGVAQRITIVR 514
Cdd:PRK11432 82 MVFQSYALFpHMSLGENvgygLKMLGVPKEERKQRVKEALELVDLA--------GF----EDRYVDQISGGQQQRVALAR 149
|
170 180 190
....*....|....*....|....*....|....
gi 1733551959 515 ALINRPSLILFDESNTSLDGYSDRALCDLMRSLK 548
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQ 183
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
360-575 |
6.71e-16 |
|
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: 81.88 E-value: 6.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSPkdpeVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGqpphdfdaesvfnQIS 439
Cdd:TIGR01271 428 GLFFSNFSLYVTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RIS 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRPTLFHGTILDNLtMFRSDQVEIMQRALELAAKlhLDEVFARLPNGYDTEVGDSSADlLPAGVAQRITIVRALINR 519
Cdd:TIGR01271 491 FSPQTSWIMPGTIKDNI-IFGLSYDEYRYTSVIKACQ--LEEDIALFPEKDKTVLGEGGIT-LSGGQRARISLARAVYKD 566
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551959 520 PSLILFDESNTSLDGYS-----DRALCDLMRSlkgtVSMILVSYRPSLLALADQRFSLEDG 575
Cdd:TIGR01271 567 ADLYLLDSPFTHLDVVTekeifESCLCKLMSN----KTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
376-557 |
9.04e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.45 E-value: 9.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 376 EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDfdaESVFNQISYIPQR----PTLfhgT 451
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD---PDVAEACHYLGHRnamkPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 452 ILDNLTMFRSDQVEIMQRALELAAKLHLDEVfARLPNGYdtevgdssadlLPAGVAQRITIVRALI-NRPSLILfDESNT 530
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIAAALEAVGLAPL-AHLPFGY-----------LSAGQKRRVALARLLVsNRPIWIL-DEPTA 156
|
170 180
....*....|....*....|....*..
gi 1733551959 531 SLDGYSDRALCDLMRSLKGTVSMILVS 557
Cdd:PRK13539 157 ALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
134-330 |
1.52e-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: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 134 DLAHVESTPSGMHLDRLSS-IELIRDFyASQASLVLIDLPFILLFLGILALITGW-LVLIPIIMLGIAGFMAWKIGKSLQ 211
Cdd:cd18552 86 PLSFFDRNSSGDLISRITNdVNQVQNA-LTSALTVLVRDPLTVIGLLGVLFYLDWkLTLIALVVLPLAALPIRRIGKRLR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 212 EQLEERREWDRRRYSFLIEVLSGIHTVKAMAMEAMMLRRYERLLESN-------AFASAQVSQISghaQTVGTItshlTV 284
Cdd:cd18552 165 KISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLrrlsmkiARARALSSPLM---ELLGAI----AI 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1733551959 285 AAVVGFGSLMVINGTLSVGALAASTLLAGRTVQPaLRALG-LWSRFQ 330
Cdd:cd18552 238 ALVLWYGGYQVISGELTPGEFISFITALLLLYQP-IKRLSnVNANLQ 283
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
359-576 |
2.04e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.95 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 359 TSLDLKNLhfRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDfDAESVFNQI 438
Cdd:PRK13536 40 VAIDLAGV--SKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 439 SYIPQRPTL-FHGTILDNLTMFrSDQVEIMQRALELAAKLHLDevFARLPNGYDTEVGDssadlLPAGVAQRITIVRALI 517
Cdd:PRK13536 117 GVVPQFDNLdLEFTVRENLLVF-GRYFGMSTREIEAVIPSLLE--FARLESKADARVSD-----LSGGMKRRLTLARALI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551959 518 NRPSLILFDESNTSLDGYSDRALCDLMRSL--KGTVSMILVSYRPSLLALADQRFSLEDGR 576
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLlaRGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
361-536 |
4.16e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.51 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAES--VFNQI 438
Cdd:PRK11248 2 LQISHLYADYGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERgvVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 439 SYIPQRptlfhgTILDN----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQRITIVR 514
Cdd:PRK11248 80 GLLPWR------NVQDNvafgLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ------------LSGGQRQRVGIAR 141
|
170 180
....*....|....*....|..
gi 1733551959 515 ALINRPSLILFDESNTSLDGYS 536
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAFT 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
361-527 |
4.59e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYspkdPEV--LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQP-----PHD-FDAe 432
Cdd:COG3845 6 LELRGITKRF----GGVvaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrirsPRDaIAL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 433 svfnQISYIPQRPTLFHG-TILDNLTM-------FRSDQVEIMQRALELAAK--LHLDevfarlPngyDTEVGDssadlL 502
Cdd:COG3845 81 ----GIGMVHQHFMLVPNlTVAENIVLgleptkgGRLDRKAARARIRELSERygLDVD------P---DAKVED-----L 142
|
170 180
....*....|....*....|....*
gi 1733551959 503 PAGVAQRITIVRALINRPSLILFDE 527
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDE 167
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
376-577 |
4.75e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.92 E-value: 4.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 376 EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQ-ISYIPQRPTLF-HGTIL 453
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAIVPEGRRVFsRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 454 DNLTM--FRSDQVEIMQRalelaaklhLDEVFARLPNGYDTEVgdSSADLLPAGVAQRITIVRALINRPSLILFDESNTS 531
Cdd:PRK11614 99 ENLAMggFFAERDQFQER---------IKWVYELFPRLHERRI--QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1733551959 532 LDGYSDRALCDLMRSLKGT-VSMILVSYRPS-LLALADQRFSLEDGRL 577
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQgMTIFLVEQNANqALKLADRGYVLENGHV 215
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
52-333 |
5.26e-15 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 76.01 E-value: 5.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 52 ILAASLGINILALALPLLILQVYNRILPYEGLSTLAMLTIGVAIALVLDVLLKIARARLsgwagaqyehragcIAI---- 127
Cdd:cd18555 7 ILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYI--------------IIKlqtk 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 128 --KRLATGDLAHV--------ESTPSGMHLDRLSSIELIRDFYASQASLVLIDLPFILLFLGIL----ALITGWLVLIPI 193
Cdd:cd18555 73 ldKSLMSDFFEHLlklpysffENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMlyysPLLTLIVLLLGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 194 IMLGIAGFMAWKIGKSLQEQLEERREWdrrrYSFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQ 273
Cdd:cd18555 153 LIVLLLLLTRKKIKKLNQEEIVAQTKV----QSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILN 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 274 TVGTITSHLTVAAVVGFGSLMVINGTLSVGALAASTLLAGRTVQPALRALGLWSRFQSVS 333
Cdd:cd18555 229 SISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLK 288
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
361-533 |
5.27e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.19 E-value: 5.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSpkDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISY 440
Cdd:PRK09536 4 IDVSDLSVEFG--DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTL-FHGTILDNLTMFRSDQVEIMQRALElAAKLHLDEVFARlpnGYDTEVGDSSADLLPAGVAQRITIVRALINR 519
Cdd:PRK09536 82 VPQDTSLsFEFDVRQVVEMGRTPHRSRFDTWTE-TDRAAVERAMER---TGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170
....*....|....
gi 1733551959 520 PSLILFDESNTSLD 533
Cdd:PRK09536 158 TPVLLLDEPTASLD 171
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
361-557 |
6.58e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.00 E-value: 6.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSpkDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQP-PHDfdAESVFNQIS 439
Cdd:PRK13537 8 IDFRNVEKRYG--DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvPSR--ARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRPTL---FhgTILDNLTMFRSDQVEIMQRALELAAKLhLDevFARLPNGYDTEVGDssadlLPAGVAQRITIVRAL 516
Cdd:PRK13537 84 VVPQFDNLdpdF--TVRENLLVFGRYFGLSAAAARALVPPL-LE--FAKLENKADAKVGE-----LSGGMKRRLTLARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1733551959 517 INRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVS 557
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLT 194
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
363-557 |
7.80e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 75.03 E-value: 7.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQpphDFDAESVF---NQIS 439
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI---TISKENLKeirKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRP-TLFHG-TILDN----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQRITIV 513
Cdd:PRK13632 87 IIFQNPdNQFIGaTVEDDiafgLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQN------------LSGGQKQRVAIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1733551959 514 RALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVS 557
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIS 198
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
377-578 |
8.35e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.05 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAES-----------VFNQISYIP--- 442
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklrakhvgfVFQSFMLIPtln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 443 -----QRPTLFHGtildnltmfRSDQvEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQRITIVRALI 517
Cdd:PRK10584 105 alenvELPALLRG---------ESSR-QSRNGAKALLEQLGLGKRLDHLPAQ------------LSGGEQQRVALARAFN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 518 NRPSLILFDESNTSLDGYSDRALCDLMRSLK---GTvSMILVSYRPSLLALADQRFSLEDGRLK 578
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNrehGT-TLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
359-548 |
1.05e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.28 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 359 TSLDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQI 438
Cdd:PRK11231 1 MTLRTENLTVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 439 SYIPQRPTLFHGTILDNLTMF-RS------------DQvEIMQRALElaaKLHLDEVFARLpngydteVGDssadlLPAG 505
Cdd:PRK11231 79 ALLPQHHLTPEGITVRELVAYgRSpwlslwgrlsaeDN-ARVNQAME---QTRINHLADRR-------LTD-----LSGG 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1733551959 506 VAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLK 548
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELN 185
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
359-577 |
1.11e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.33 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 359 TSLDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGsALLNGQPP-HDF--DAESVF 435
Cdd:PRK11247 11 TPLLLNAVSKRYGER--TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-ELLAGTAPlAEAreDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 436 NQISYIPQRptlfhgTILDNLTM-FRSDQVEIMQRALElaaklhldevfarlpngydtEVGDSS-ADLLPA----GVAQR 509
Cdd:PRK11247 88 QDARLLPWK------KVIDNVGLgLKGQWRDAALQALA--------------------AVGLADrANEWPAalsgGQKQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551959 510 ITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL--KGTVSMILVSYRPS-LLALADQRFSLEDGRL 577
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
352-423 |
1.23e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.96 E-value: 1.23e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 352 RFKMDRFTSLDLKNLHFRYSPKDPE---VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNG 423
Cdd:COG1134 13 SYRLYHEPSRSLKELLLRRRRTRREefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
360-575 |
1.28e-14 |
|
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: 74.51 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSPkdpeVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGqpphdfdaesvfnQIS 439
Cdd:cd03291 39 NLFFSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRPTLFHGTILDNLTMFRS-DQVeimqRALELAAKLHLDEVFARLPNGYDTEVGDSSADlLPAGVAQRITIVRALIN 518
Cdd:cd03291 102 FSSQFSWIMPGTIKENIIFGVSyDEY----RYKSVVKACQLEEDITKFPEKDNTVLGEGGIT-LSGGQRARISLARAVYK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 519 RPSLILFDESNTSLDGYS-----DRALCDLMRSlkgtVSMILVSYRPSLLALADQRFSLEDG 575
Cdd:cd03291 177 DADLYLLDSPFGYLDVFTekeifESCVCKLMAN----KTRILVTSKMEHLKKADKILILHEG 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
343-533 |
1.66e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 75.64 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 343 DAIPaesRGRFKMDRFTS--LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSAL 420
Cdd:PRK11607 3 DAIP---RPQAKTRKALTplLEIRNLTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 421 LNGQ-----PPHDFDAESVFNQISYIPqrptlfHGTILDNLTM-FRSDQV---EIMQRALELAAKLHLDEVFARLPNGyd 491
Cdd:PRK11607 78 LDGVdlshvPPYQRPINMMFQSYALFP------HMTVEQNIAFgLKQDKLpkaEIASRVNEMLGLVHMQEFAKRKPHQ-- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1733551959 492 tevgdssadlLPAGVAQRITIVRALINRPSLILFDESNTSLD 533
Cdd:PRK11607 150 ----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
180-577 |
1.92e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 76.91 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 180 ILALITGWLVLIPIIMLGIA---------GFMAWKIgKSLQeqlEERREWDRRRYSFLIEVLSGIHTVKAMAMEAMMLRR 250
Cdd:TIGR00957 446 ILALYFLWLNLGPSVLAGVAvmvlmvplnAVMAMKT-KTYQ---VAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDK 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 251 YERLLESnafaSAQVSQISGHAQTVGTITSHLT--VAAVVGFGSLMVI--NGTLSVGALAASTLLAGRTVQPALRALGLW 326
Cdd:TIGR00957 522 VEGIRQE----ELKVLKKSAYLHAVGTFTWVCTpfLVALITFAVYVTVdeNNILDAEKAFVSLALFNILRFPLNILPMVI 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 327 SRFQSVSLAEDNLR--------DIDAIpaeSRGRFKMDRFTSLDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNG 398
Cdd:TIGR00957 598 SSIVQASVSLKRLRiflsheelEPDSI---ERRTIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVG 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 399 VGKSTLLNLVAGQIVPTKGSALLNGqpphdfdaesvfnQISYIPQRPTLFHGTILDNLTMFRSDQVEIMQRALELAAKLH 478
Cdd:TIGR00957 675 CGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLP 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 479 LDEVfarLPNGYDTEVGDSSADlLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTV---SMIL 555
Cdd:TIGR00957 742 DLEI---LPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLknkTRIL 817
|
410 420
....*....|....*....|..
gi 1733551959 556 VSYRPSLLALADQRFSLEDGRL 577
Cdd:TIGR00957 818 VTHGISYLPQVDVIIVMSGGKI 839
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
360-550 |
2.16e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.12 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSpkDPEVLHNINLRLEQGQIIGITGKNGVGKSTL---LNLVAgqiVPTKGSALLNGqppHDFDAES--- 433
Cdd:PRK11124 2 SIQLNGINCFYG--AHQALFDITLDCPQGETLVLLGPSGAGKSSLlrvLNLLE---MPRSGTLNIAG---NHFDFSKtps 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 434 -------------VFNQISYIPqrptlfHGTILDNLT-----MFRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevg 495
Cdd:PRK11124 74 dkairelrrnvgmVFQQYNLWP------HLTVQQNLIeapcrVLGLSKDQALARAEKLLERLRLKPYADRFPLH------ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 496 dssadlLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGT 550
Cdd:PRK11124 142 ------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET 190
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
361-576 |
3.18e-14 |
|
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: 70.17 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDpeVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSallngqPPHDFDAEsvfnqISY 440
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI------VTWGSTVK-----IGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQrptlfhgtildnltmfrsdqveimqralelaaklhldevfarlpngydtevgdssadlLPAGVAQRITIVRALINRP 520
Cdd:cd03221 68 FEQ----------------------------------------------------------LSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551959 521 SLILFDESNTSLDGYSDRALCDLMRSLKGTVsmILVSYRPSLL-ALADQRFSLEDGR 576
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALKEYPGTV--ILVSHDRYFLdQVATKIIELEDGK 144
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
368-577 |
3.89e-14 |
|
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: 72.37 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 368 FRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDfDAESVFNQISYI-PQRPT 446
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVfGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 447 LFHG-TILDNLTM----FRSDQVEIMQRALELAAKLHLDEVFarlpngydtevgDSSADLLPAGVAQRITIVRALINRPS 521
Cdd:cd03267 106 LWWDlPVIDSFYLlaaiYDLPPARFKKRLDELSELLDLEELL------------DTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551959 522 LILFDESNTSLDGYSDRALCDLMRSL---KGTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYnreRGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
128-331 |
4.22e-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: 72.98 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 128 KRLATGDLAHVESTPSGMHLDRLSS-IELIRDFYASQASLVLIDLPFILLFLGILaLITGW------LVLIPIIMLGIA- 199
Cdd:cd18557 77 SSLLRQEIAFFDKHKTGELTSRLSSdTSVLQSAVTDNLSQLLRNILQVIGGLIIL-FILSWkltlvlLLVIPLLLIASKi 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 200 -GFMAWKIGKSLQEQLEERRewdrrrySFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTI 278
Cdd:cd18557 156 yGRYIRKLSKEVQDALAKAG-------QVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSL 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 279 TSHLTVAAVVGFGSLMVINGTLSVGALAASTLLAGrTVQPALRAL-GLWSRFQS 331
Cdd:cd18557 229 LIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTI-MVASSVGGLsSLLADIMK 281
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
360-559 |
5.18e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.59 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLnLVAGQIVPTKGSAL-LNGQPPHDFDAESVFNQI 438
Cdd:PTZ00243 1308 SLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLL-LTFMRMVEVCGGEIrVNGREIGAYGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 439 SYIPQRPTLFHGTILDNLTMFRSDQVEIMQRALELAAklhLDEVFARLPNGYDTEVGDSSADLlpaGVAQR--ITIVRAL 516
Cdd:PTZ00243 1387 SMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVG---LRERVASESEGIDSRVLEGGSNY---SVGQRqlMCMARAL 1460
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1733551959 517 INRPS-LILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYR 559
Cdd:PTZ00243 1461 LKKGSgFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHR 1504
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
363-533 |
6.03e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 73.19 E-value: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLHFRYSPKDPEV--LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFN---Q 437
Cdd:COG1135 4 LENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAarrK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYIPQRPTLFHG-TILDN----LTMFRSDQVEIMQRALELaakLHLdevfarlpngydteVG-DSSADLLPA----GVA 507
Cdd:COG1135 84 IGMIFQHFNLLSSrTVAENvalpLEIAGVPKAEIRKRVAEL---LEL--------------VGlSDKADAYPSqlsgGQK 146
|
170 180
....*....|....*....|....*..
gi 1733551959 508 QRITIVRALINRPSLILFDESnTS-LD 533
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEA-TSaLD 172
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
361-557 |
6.12e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 72.12 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLV--AGQIVP---TKGSALLNGqppHDF-----D 430
Cdd:PRK14239 6 LQVSDLSVYYNKK--KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNG---HNIysprtD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 431 AESVFNQISYIPQRPTLFHGTILDN------LTMFRSDQV--EIMQRALELAAKLhlDEVFARLpngYDTEVGdssadlL 502
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFPMSIYENvvyglrLKGIKDKQVldEAVEKSLKGASIW--DEVKDRL---HDSALG------L 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 503 PAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVS 557
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT 204
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
363-577 |
8.41e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.94 E-value: 8.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLHFRYsPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDA-ESVFNQISYI 441
Cdd:PRK13644 4 LENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 442 PQRP-TLFHGTILDNLTMFRSDQ-----VEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQRITIVRA 515
Cdd:PRK13644 83 FQNPeTQFVGRTVEEDLAFGPENlclppIEIRKRVDRALAEIGLEKYRHRSPKT------------LSGGQGQCVALAGI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 516 LINRPSLILFDESNTSLDGYSDRALCDLMRSL--KGTvSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLheKGK-TIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
361-577 |
9.62e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.65 E-value: 9.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYsPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPhDFDAESVFN---Q 437
Cdd:PRK13639 2 LETRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEvrkT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYIPQRP--TLFHGTILDNLTM------FRSDQVEimQRALELAAKLHLdEVFARLPNGYdtevgdssadlLPAGVAQR 509
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFgplnlgLSKEEVE--KRVKEALKAVGM-EGFENKPPHH-----------LSGGQKKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 510 ITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL-KGTVSMILVSYRPSLLAL-ADQRFSLEDGRL 577
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVyADKVYVMSDGKI 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
361-578 |
9.63e-14 |
|
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: 74.07 E-value: 9.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYspKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAG--QIVPTKGSALLN---------------- 422
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 423 GQP---------PHDFD----AESVF----NQISYIPQRPTLFHG--TILDN----LTMFRSDQVEIMQRALELAAKLHL 479
Cdd:TIGR03269 79 GEPcpvcggtlePEEVDfwnlSDKLRrrirKRIAIMLQRTFALYGddTVLDNvleaLEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 480 DEVFARLpngydtevgdssADLLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL--KGTVSMILVS 557
Cdd:TIGR03269 159 SHRITHI------------ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTS 226
|
250 260
....*....|....*....|..
gi 1733551959 558 YRPSLLA-LADQRFSLEDGRLK 578
Cdd:TIGR03269 227 HWPEVIEdLSDKAIWLENGEIK 248
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
378-558 |
1.24e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.35 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLL-------NLVAGQIVptKGSALLNGQPPHD--FDAESVFNQISYIPQRPTLF 448
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRV--EGKVTFHGKNLYApdVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 449 HGTILDNLTM------FRSDQVEIMQRALELAAKLhlDEVFARLpngydtevgDSSADLLPAGVAQRITIVRALINRPSL 522
Cdd:PRK14243 104 PKSIYDNIAYgaringYKGDMDELVERSLRQAALW--DEVKDKL---------KQSGLSLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 1733551959 523 ILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSY 558
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
83-318 |
1.39e-13 |
|
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: 71.77 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 83 LSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQ---------YEHragciaIKRLatgDLAHVESTPSGMHLDRLSS- 152
Cdd:cd18563 39 TSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERitadlrrdlYEH------LQRL---SLSFFDKRQTGSLMSRVTSd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 153 IELIRDFYASQASLVLIDlpfILLFLGILA-LIT-----GWLVLIPIImlgIAGFMAWKIGKSLQEQLEERREWDRRRYS 226
Cdd:cd18563 110 TDRLQDFLSDGLPDFLTN---ILMIIGIGVvLFSlnwklALLVLIPVP---LVVWGSYFFWKKIRRLFHRQWRRWSRLNS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 227 FLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGALA 306
Cdd:cd18563 184 VLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLV 263
|
250
....*....|..
gi 1733551959 307 ASTLLAGRTVQP 318
Cdd:cd18563 264 AFLSYLGMFYGP 275
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
361-575 |
1.49e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 71.32 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISY 440
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRP-TLFHGTI--------LDNLTMFRSDQVEIMQRALELAAKLhldevfarlpngydtEVGDSSADLLPAGVAQRIT 511
Cdd:PRK13648 88 VFQNPdNQFVGSIvkydvafgLENHAVPYDEMHRRVSEALKQVDML---------------ERADYEPNALSGGQKQRVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 512 IVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGT--VSMILVSYRPSLLALADQRFSLEDG 575
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAMEADHVIVMNKG 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
361-576 |
1.66e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.17 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYspkdPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ-----PPHdfdaesvf 435
Cdd:COG3840 2 LRLDDLTYRY----GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalPPA-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 436 nqisyipQRP--------TLF-HGTILDN----------LTmfRSDQveimQRALELAAKLHLDEVFARLPngydtevgd 496
Cdd:COG3840 70 -------ERPvsmlfqenNLFpHLTVAQNiglglrpglkLT--AEQR----AQVEQALERVGLAGLLDRLP--------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 497 ssaDLLPAGVAQRITIVRALI-NRPSLILfDESNTSLdgysDRALCDLMRSLKGTV------SMILVSYRPS-LLALADQ 568
Cdd:COG3840 128 ---GQLSGGQRQRVALARCLVrKRPILLL-DEPFSAL----DPALRQEMLDLVDELcrerglTVLMVTHDPEdAARIADR 199
|
....*...
gi 1733551959 569 RFSLEDGR 576
Cdd:COG3840 200 VLLVADGR 207
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
377-562 |
1.82e-13 |
|
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: 69.44 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHdFDAESVFNQISYIPQRPTLFHG-TILDN 455
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-FQRDSIARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 456 LTMFRSDQVEimqralelaaklhlDEVFARLPNGYDTEVGDSSADLLPAGVAQRITIVRALINRPSLILFDESNTSLDGY 535
Cdd:cd03231 94 LRFWHADHSD--------------EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....*..
gi 1733551959 536 SDRALCDLMRSLKGTVSMILVSYRPSL 562
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTHQDL 186
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
361-577 |
2.01e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.81 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPphdFDAESVFN---Q 437
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETVWDvrrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYIPQRP-TLFHGTI--------LDNLTMFRSDQVEIMQRALELaakLHLDEVFARLPNGydtevgdssadlLPAGVAQ 508
Cdd:PRK13635 83 VGMVFQNPdNQFVGATvqddvafgLENIGVPREEMVERVDQALRQ---VGMEDFLNREPHR------------LSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551959 509 RITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLK--GTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQADRVIVMNKGEI 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
360-561 |
2.35e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.26 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSpkDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLN-----LVAGQIVPTKGSALLNGQPPH--DFDAE 432
Cdd:PRK14267 4 AIETVNLRVYYG--SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYspDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 433 SVFNQISYIPQRPTLF-HGTILDN---------LTMFRSDQVEIMQRALELAAKLhlDEVFARLpNGYDTEvgdssadlL 502
Cdd:PRK14267 82 EVRREVGMVFQYPNPFpHLTIYDNvaigvklngLVKSKKELDERVEWALKKAALW--DEVKDRL-NDYPSN--------L 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551959 503 PAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPS 561
Cdd:PRK14267 151 SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPA 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
361-557 |
3.37e-13 |
|
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: 70.85 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEV--LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVP---TKGSALLNGQPPHDFDAESV- 434
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 435 ---FNQISYIPQRPT-----LFhgTILDNLT-MFRSDQV----EIMQRALELAAKLHLDEVFARLpngydtevgdssaDL 501
Cdd:COG0444 82 kirGREIQMIFQDPMtslnpVM--TVGDQIAePLRIHGGlskaEARERAIELLERVGLPDPERRL-------------DR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 502 LP----AGVAQRITIVRALINRPSLILFDESNTSLDGySDRA--LcDLMRSLK---GTvSMILVS 557
Cdd:COG0444 147 YPhelsGGMRQRVMIARALALEPKLLIADEPTTALDV-TIQAqiL-NLLKDLQrelGL-AILFIT 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
359-533 |
3.56e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.78 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 359 TSLDLKNLHFRYspKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLL---NLV----AGQI----VPTKGSALLNGQPPH 427
Cdd:PRK11264 2 SAIEVKNLVKKF--HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLrciNLLeqpeAGTIrvgdITIDTARSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 428 dfdAESVFNQISYIPQRPTLF-HGTILDN-----LTMFRSDQVEIMQRALELAAKLHLdevfarlpNGYDtevgDSSADL 501
Cdd:PRK11264 80 ---IRQLRQHVGFVFQNFNLFpHRTVLENiiegpVIVKGEPKEEATARARELLAKVGL--------AGKE----TSYPRR 144
|
170 180 190
....*....|....*....|....*....|..
gi 1733551959 502 LPAGVAQRITIVRALINRPSLILFDESNTSLD 533
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
359-533 |
3.82e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 69.61 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 359 TSLDLKNLHFRYSpkDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPH---DFDAE-SV 434
Cdd:PRK10619 4 NKLNVIDLHKRYG--EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrDKDGQlKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 435 F--NQISYIPQRPTLF--------HGTILDNLtMFRSDQV------EIMQRALELAAKLHLDEvfaRLPNGYDTEvgdss 498
Cdd:PRK10619 82 AdkNQLRLLRTRLTMVfqhfnlwsHMTVLENV-MEAPIQVlglskqEARERAVKYLAKVGIDE---RAQGKYPVH----- 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1733551959 499 adlLPAGVAQRITIVRALINRPSLILFDESNTSLD 533
Cdd:PRK10619 153 ---LSGGQQQRVSIARALAMEPEVLLFDEPTSALD 184
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
86-307 |
4.33e-13 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 70.18 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 86 LAMLTIGVAIALVLDVLLKIARARLSGWAGAQ--------------------YEHRAgciaikrlaTGDLahvestpsgm 145
Cdd:cd18567 41 LTVLAIGFGLLLLLQALLSALRSWLVLYLSTSlnlqwtsnlfrhllrlplsyFEKRH---------LGDI---------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 146 hLDRLSSIELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIMLGIAGFMAWKIGKSLQEQLEERREWDRRRY 225
Cdd:cd18567 102 -VSRFGSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 226 SFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGAL 305
Cdd:cd18567 181 SHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGML 260
|
..
gi 1733551959 306 AA 307
Cdd:cd18567 261 FA 262
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
361-577 |
4.59e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.06 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDP--EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVF--- 435
Cdd:PRK10535 5 LELKDIRRSYPSGEEqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 436 -NQISYIPQRptlFHgtILDNLTMfrSDQVEI------------MQRALELAAKLHLDEVFARLPNGydtevgdssadlL 502
Cdd:PRK10535 85 rEHFGFIFQR---YH--LLSHLTA--AQNVEVpavyaglerkqrLLRAQELLQRLGLEDRVEYQPSQ------------L 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1733551959 503 PAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKG---TVsmILVSYRPSLLALADQRFSLEDGRL 577
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrghTV--IIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
359-581 |
5.78e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.83 E-value: 5.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 359 TSLDLKNLHFRYSpkDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ-----PPHDFDAES 433
Cdd:PRK11000 2 ASVTLRNVTKAYG--DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 434 VFNQISYIPqrptlfHGTILDN----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQR 509
Cdd:PRK11000 80 VFQSYALYP------HLSVAENmsfgLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKA------------LSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 510 ITIVRALINRPSLILFDESNTSLDGysdrALCDLMRS--------LKGTvsMILVSY-RPSLLALADQRFSLEDGRL--- 577
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLDA----ALRVQMRIeisrlhkrLGRT--MIYVTHdQVEAMTLADKIVVLDAGRVaqv 215
|
....*
gi 1733551959 578 -KPLD 581
Cdd:PRK11000 216 gKPLE 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
362-554 |
7.46e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.21 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 362 DLKNLHFRYSPKDPEV--LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQpphDFDAESVFN--- 436
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQ---DLTALSEKElrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 437 ---QISYIPQRPTLFHG-TILDN----LTMFRSDQVEIMQRALELaakLHLdevfarlpngydteVGDSS-ADLLPA--- 504
Cdd:PRK11153 80 arrQIGMIFQHFNLLSSrTVFDNvalpLELAGTPKAEIKARVTEL---LEL--------------VGLSDkADRYPAqls 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 505 -GVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLM----RSLKGTVSMI 554
Cdd:PRK11153 143 gGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLkdinRELGLTIVLI 197
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
361-564 |
8.02e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.79 E-value: 8.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSpkDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQI-----VPTKGSALLNGQPPHDFDAESVF 435
Cdd:PRK14247 4 IEIRDLKVSFG--QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 436 NQISYIPQRP------TLFHGTILD-NLTMFRSDQVEIMQRALELAAKLHL-DEVFARLpngydtevgDSSADLLPAGVA 507
Cdd:PRK14247 82 RRVQMVFQIPnpipnlSIFENVALGlKLNRLVKSKKELQERVRWALEKAQLwDEVKDRL---------DAPAGKLSGGQQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551959 508 QRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLA 564
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAA 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
359-447 |
8.99e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 68.64 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 359 TSLDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQI 438
Cdd:PRK13548 1 AMLEARNLSVRLGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
....*....
gi 1733551959 439 SYIPQRPTL 447
Cdd:PRK13548 79 AVLPQHSSL 87
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
361-577 |
1.21e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 67.17 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHfrYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAG--QIVPTKGSALLNGQ-----PPHDFDAES 433
Cdd:cd03217 1 LEIKDLH--VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEditdlPPEERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 434 VFnqISYipQRPTLFHGtiLDNLTMFRSdqveimqralelaaklhLDEVFArlpngydtevgdssadllpAGVAQRITIV 513
Cdd:cd03217 79 IF--LAF--QYPPEIPG--VKNADFLRY-----------------VNEGFS-------------------GGEKKRNEIL 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551959 514 RALINRPSLILFDESNTSLDGYSDRALCDLMRSLKG-TVSMILVSYRPSLLAL--ADQRFSLEDGRL 577
Cdd:cd03217 117 QLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREeGKSVLIITHYQRLLDYikPDRVHVLYDGRI 183
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
169-578 |
1.39e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.92 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 169 IDLPFILLF--LGILALItGWLVLIpiIMLGIAGFMAWKIGKSLQEQLEERREWDrrrySFLIEVLSGIHTVKAMAMEam 246
Cdd:PLN03130 428 IIIAMVLLYqqLGVASLI-GSLMLV--LMFPIQTFIISKMQKLTKEGLQRTDKRI----GLMNEVLAAMDTVKCYAWE-- 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 247 mlrryerllesNAFASaQVSQISG-------HAQTVGTITSHL-----TVAAVVGFGSLMVINGTLS-VGALAASTLLA- 312
Cdd:PLN03130 499 -----------NSFQS-KVQTVRDdelswfrKAQLLSAFNSFIlnsipVLVTVVSFGVFTLLGGDLTpARAFTSLSLFAv 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 313 --------GRTVQPALRALGLWSRFQSVSLAE-----DNLRDIDAIPAESrgrfkmdrftsldLKNLHFRYSPK-DPEVL 378
Cdd:PLN03130 567 lrfplfmlPNLITQAVNANVSLKRLEELLLAEervllPNPPLEPGLPAIS-------------IKNGYFSWDSKaERPTL 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 379 HNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTK-GSALLNGqpphdfdaesvfnQISYIPQRPTLFHGTILDNLt 457
Cdd:PLN03130 634 SNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRG-------------TVAYVPQVSWIFNATVRDNI- 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 458 MFRSD-QVEIMQRALELAAklhLDEVFARLPNGYDTEVGDSSADlLPAGVAQRITIVRALINRPSLILFDESNTSLDGYS 536
Cdd:PLN03130 700 LFGSPfDPERYERAIDVTA---LQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1733551959 537 DRALCD--LMRSLKGTvSMILVSYRPSLLALADQRFSLEDGRLK 578
Cdd:PLN03130 776 GRQVFDkcIKDELRGK-TRVLVTNQLHFLSQVDRIILVHEGMIK 818
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
361-581 |
1.58e-12 |
|
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: 68.01 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTlLNLVAGQIVPT-KGSALLNGQPPHDFDAESVFNQIS 439
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSS-LSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQRPTLFHGTILDNLTMFRSDQVEIMQRALELAaklHLDEVFARLPNGYDTEVGDSSADlLPAGVAQRITIVRALINR 519
Cdd:cd03288 99 IILQDPILFSGSIRFNLDPECKCTDDRLWEALEIA---QLKNMVKSLPGGLDAVVTEGGEN-FSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 520 PSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRLKPLD 581
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECD 236
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
370-574 |
2.21e-12 |
|
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: 65.25 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 370 YSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGqIVP-TKGSAllnGQPPHdfdaesvfNQISYIPQRPTLF 448
Cdd:cd03223 9 ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPwGSGRI---GMPEG--------EDLLFLPQRPYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 449 HGTILDNLTmfrsdqveimqralelaaklhldevfarLPngydtevgdsSADLLPAGVAQRITIVRALINRPSLILFDES 528
Cdd:cd03223 77 LGTLREQLI----------------------------YP----------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1733551959 529 NTSLDGYSDRALCDLMRSLKGTVsmILVSYRPSLLALADQRFSLED 574
Cdd:cd03223 119 TSALDEESEDRLYQLLKELGITV--ISVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
360-577 |
2.42e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 67.85 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRY---SPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ----PPHDFDAE 432
Cdd:PRK13649 2 GINLQNVSYTYqagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitsTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 433 SVFNQISYIPQRP--TLFHGTILDNLTM----FRSDQVEIMQRALElaaKLHLdevfarlpNGYDTEVGDSSADLLPAGV 506
Cdd:PRK13649 82 QIRKKVGLVFQFPesQLFEETVLKDVAFgpqnFGVSQEEAEALARE---KLAL--------VGISESLFEKNPFELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733551959 507 AQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL-KGTVSMILVSYRPSLLA-LADQRFSLEDGRL 577
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVAnYADFVYVLEKGKL 223
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
368-578 |
2.55e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.19 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 368 FRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALlngqpphdfdAEsvfNQISYIPQRPTL 447
Cdd:PTZ00243 668 FELEPK--VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW----------AE---RSIAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 448 FHGTILDNLTMFRSDQVEIMQRALELAaklHLDEVFARLPNGYDTEVGDSSADlLPAGVAQRITIVRALINRPSLILFDE 527
Cdd:PTZ00243 733 MNATVRGNILFFDEEDAARLADAVRVS---QLEADLAQLGGGLETEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 528 SNTSLDGY-SDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSLEDGRLK 578
Cdd:PTZ00243 809 PLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
361-577 |
2.86e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSpkDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFN---Q 437
Cdd:PRK11831 8 VDMRGVSFTRG--NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrkR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYIPQRPTLFHG-TILDNLTMFRSDQVEIMQRALELAAKLHLDEVFARlpngydtevgdSSADLLPA----GVAQRITI 512
Cdd:PRK11831 86 MSMLFQSGALFTDmNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLR-----------GAAKLMPSelsgGMARRAAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1733551959 513 VRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGT--VSMILVSYR-PSLLALADQRFSLEDGRL 577
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlgVTCVVVSHDvPEVLSIADHAYIVADKKI 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
361-577 |
3.34e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.45 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPE-VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQpphDFDAESVFN--- 436
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 437 QISYIPQRP-TLFHGTI--------LDNLTMFRSDQVEIMQRALELAAKLHLDEvfaRLPNgydtevgdssadLLPAGVA 507
Cdd:PRK13650 82 KIGMVFQNPdNQFVGATveddvafgLENKGIPHEEMKERVNEALELVGMQDFKE---REPA------------RLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 508 QRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSL--LALADQRFSLEDGRL 577
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLdeVALSDRVLVMKNGQV 218
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
132-335 |
3.47e-12 |
|
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: 67.46 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 132 TGDLahvestpsgmhLDRLSS-IELIRDFYASQA-----SLVLIDLPFILLFL--GILALITgwLVLIPIImLGIAGFMA 203
Cdd:cd18542 95 TGDL-----------MSRCTSdVDTIRRFLAFGLvelvrAVLLFIGALIIMFSinWKLTLIS--LAIIPFI-ALFSYVFF 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 204 WKIGKS---LQEQLEERRewdrrrySFLIEVLSGIHTVKAMAMEAMMLRRYERllESNAFASAQVSQISGHA--QTVGTI 278
Cdd:cd18542 161 KKVRPAfeeIREQEGELN-------TVLQENLTGVRVVKAFAREDYEIEKFDK--ENEEYRDLNIKLAKLLAkyWPLMDF 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 279 TSHLTVAAVVGFGSLMVINGTLSVGALAASTLLAGRTVQPaLRALG-LWSRFQ--SVSLA 335
Cdd:cd18542 232 LSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWP-VRQLGrLINDMSraSASAE 290
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
361-581 |
3.79e-12 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 67.19 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAgQIVPTKGSALLNGQPPHDFDAESVFNQISY 440
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTLFHGTILDNLTMFR--SDQvEIMQRALELAAKLhldeVFARLPNGYDTEVGDSSAdLLPAGVAQRITIVRALIN 518
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGkwSDE-EIWKVAEEVGLKS----VIEQFPGQLDFVLVDGGC-VLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 519 RPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLaLADQRF-SLEDGRLKPLD 581
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAM-LECQRFlVIEENKVRQYD 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
360-527 |
5.87e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 66.67 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDfdaeSVFNQIS 439
Cdd:COG4152 1 MLELKGLTKRFGDK--TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQ----RPTLfhgTILDNLTMFRS----DQVEIMQRALELAAKLHLDEVfarlpngYDTEVGDssadlLPAGVAQRIT 511
Cdd:COG4152 75 YLPEerglYPKM---KVGEQLVYLARlkglSKAEAKRRADEWLERLGLGDR-------ANKKVEE-----LSKGNQQKVQ 139
|
170
....*....|....*.
gi 1733551959 512 IVRALINRPSLILFDE 527
Cdd:COG4152 140 LIAALLHDPELLILDE 155
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
377-576 |
7.65e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 65.15 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ---------PPHDfdaesVF----NQISY--- 440
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlaqaSPRE-----ILalrrRTIGYvsq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 ----IPQRPTLfhGTILDNLTMFRSDQVEIMQRALELAAKLHLDEvfaRLpngydtevgdssADLLPA----GVAQRITI 512
Cdd:COG4778 101 flrvIPRVSAL--DVVAEPLLERGVDREEARARARELLARLNLPE---RL------------WDLPPAtfsgGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551959 513 VRALINRPSLILFDESNTSLDGYSDRALCDLMRSLK--GTvSMILVSYRPSLL-ALADQRFSLEDGR 576
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKarGT-AIIGIFHDEEVReAVADRVVDVTPFS 229
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
153-307 |
1.08e-11 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 65.90 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 153 IELIRDfYASQASLVLIDLPFILLF-LGILALITGWLVLIPIIMLGIAGFMAWKIGKSL-------QEQLEERRewdrrr 224
Cdd:cd18541 107 LNAVRM-ALGPGILYLVDALFLGVLvLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIhkrfrkvQEAFSDLS------ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 225 ySFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGA 304
Cdd:cd18541 180 -DRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGD 258
|
...
gi 1733551959 305 LAA 307
Cdd:cd18541 259 LVA 261
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
376-533 |
1.57e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 66.26 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 376 EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESvfNQISYIPQRPTLF-HGTILD 454
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFrHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 455 N----LTMF----RSDQVEIMQRALELaaklhLDEV-FARLPNGYDTEvgdssadlLPAGVAQRITIVRALINRPSLILF 525
Cdd:PRK10851 94 NiafgLTVLprreRPNAAAIKAKVTQL-----LEMVqLAHLADRYPAQ--------LSGGQKQRVALARALAVEPQILLL 160
|
....*...
gi 1733551959 526 DESNTSLD 533
Cdd:PRK10851 161 DEPFGALD 168
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
363-577 |
1.58e-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: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPhDFDAESVFNQISYIP 442
Cdd:TIGR01257 931 VKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 443 QRPTLFHGTILDNLTMFRSdqvEIMQRALElAAKLHLDEVFArlPNGYDTEVGDSSADlLPAGVAQRITIVRALINRPSL 522
Cdd:TIGR01257 1010 QHNILFHHLTVAEHILFYA---QLKGRSWE-EAQLEMEAMLE--DTGLHHKRNEEAQD-LSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 523 ILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFS-LEDGRL 577
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAiISQGRL 1138
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
378-576 |
2.04e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.39 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGqIVPT---KGSALLNGQP---PHDFDAESvfNQISYIPQRPTLFHG- 450
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPlkaSNIRDTER--AGIVIIHQELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 451 TILDNLTM--------FRSDQVEIMQRALELAAKLHLDEVFARLPngydteVGDssadlLPAGVAQRITIVRALINRPSL 522
Cdd:TIGR02633 94 SVAENIFLgneitlpgGRMAYNAMYLRAKNLLRELQLDADNVTRP------VGD-----YGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 523 ILFDESNTSLDGYSDRALCDLMRSLKG-TVSMILVSYR-PSLLALADQRFSLEDGR 576
Cdd:TIGR02633 163 LILDEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKlNEVKAVCDTICVIRDGQ 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
362-430 |
2.28e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 64.33 E-value: 2.28e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551959 362 DLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFD 430
Cdd:COG4604 3 EIKNVSKRYGGK--VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTP 69
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
359-557 |
3.32e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.04 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 359 TSLDLKNLH--FRYSP-----KDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDA 431
Cdd:PRK15112 3 TLLEVRNLSktFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 432 ESVFNQISYIPQRPTLFH------GTILDnLTMFRSDQVEIMQRALELAAKLHLDEVFARLPNGYdtevgdssADLLPAG 505
Cdd:PRK15112 83 SYRSQRIRMIFQDPSTSLnprqriSQILD-FPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYY--------PHMLAPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 506 VAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL--KGTVSMILVS 557
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVT 207
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
83-318 |
3.64e-11 |
|
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: 64.43 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 83 LSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQ--YEHRAGCIA-IKRLatgDLAHVESTPSGMHLDRLSS-IELIRD 158
Cdd:cd18546 35 LGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERllYDLRLRVFAhLQRL---SLDFHERETSGRIMTRMTSdIDALSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 159 FYASQASLVLIDLpfiLLFLGILA--LITGW-LVLIPIIMLGIAGFMAWKIGKSLQEQLEERREWDRRRYSFLIEVLSGI 235
Cdd:cd18546 112 LLQTGLVQLVVSL---LTLVGIAVvlLVLDPrLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 236 HTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGALAASTLLAGRT 315
Cdd:cd18546 189 RVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRF 268
|
...
gi 1733551959 316 VQP 318
Cdd:cd18546 269 FAP 271
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
377-548 |
3.69e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPphdfdaesvfnQISYIPQR----PTLfhgti 452
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL-----------RIGYVPQKlyldTTL----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 453 ldNLTmfrsdqveiMQRALELAAKLHLDEVFARLPNGYDTEVGDSSADLLPAGVAQRITIVRALINRPSLILFDESNTSL 532
Cdd:PRK09544 83 --PLT---------VNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170
....*....|....*.
gi 1733551959 533 DGYSDRALCDLMRSLK 548
Cdd:PRK09544 152 DVNGQVALYDLIDQLR 167
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
352-425 |
4.06e-11 |
|
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: 62.94 E-value: 4.06e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551959 352 RFKMDRFTSLDLKNLHFRYSPKDPE---VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQP 425
Cdd:cd03220 9 SYPTYKGGSSSLKKLGILGRKGEVGefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV 85
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
373-557 |
5.34e-11 |
|
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: 62.67 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 373 KDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVP---TKGSALLNGQPPHdfdAESVFNQISYIPQrptlfH 449
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK---PDQFQKCVAYVRQ-----D 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 450 GTILDNLT---------MFRsdqveiMQRALELAAKLHLDEVFaRLPNGYDTEVGDSSADLLPAGVAQRITIVRALINRP 520
Cdd:cd03234 90 DILLPGLTvretltytaILR------LPRKSSDAIRKKRVEDV-LLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1733551959 521 SLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVS 557
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILT 199
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
360-536 |
5.90e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.99 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYspKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ-----PPHdfdaESV 434
Cdd:PRK10895 3 TLTAKNLAKAY--KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLH----ARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 435 FNQISYIPQRPTLFHG-TILDNLTM---FRSD--QVEIMQRALELAAKLHLdevfarlpngydTEVGDSSADLLPAGVAQ 508
Cdd:PRK10895 77 RRGIGYLPQEASIFRRlSVYDNLMAvlqIRDDlsAEQREDRANELMEEFHI------------EHLRDSMGQSLSGGERR 144
|
170 180
....*....|....*....|....*...
gi 1733551959 509 RITIVRALINRPSLILFDESNTSLDGYS 536
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVDPIS 172
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
359-576 |
6.09e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 63.71 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 359 TSLDLKNLHFRYsPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPhDFDAESVFN-- 436
Cdd:PRK13636 4 YILKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 437 -QISYIPQRPtlfhgtilDNLTMFRSDQVEIMQRALELaaKLHLDEVFARLPNGYD----TEVGDSSADLLPAGVAQRIT 511
Cdd:PRK13636 82 eSVGMVFQDP--------DNQLFSASVYQDVSFGAVNL--KLPEDEVRKRVDNALKrtgiEHLKDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551959 512 IVRALINRPSLILFDESNTSLDgysDRALCDLMRSLKGT-----VSMILVSYRPSLLAL-ADQRFSLEDGR 576
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLD---PMGVSEIMKLLVEMqkelgLTIIIATHDIDIVPLyCDNVFVMKEGR 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
377-533 |
7.15e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.17 E-value: 7.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAES----------VF-NQISYIPQRP 445
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrrdiqmVFqDSISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 446 TLfhGTILDN-----LTMFRSDQVEimqRALELaaklhLDEVfarlpngydtEVGDSSADLLPA----GVAQRITIVRAL 516
Cdd:PRK10419 107 TV--REIIREplrhlLSLDKAERLA---RASEM-----LRAV----------DLDDSVLDKRPPqlsgGQLQRVCLARAL 166
|
170
....*....|....*..
gi 1733551959 517 INRPSLILFDESNTSLD 533
Cdd:PRK10419 167 AVEPKLLILDEAVSNLD 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
372-554 |
8.39e-11 |
|
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: 64.57 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 372 PKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGqiVPTkgsallngqpphDFDAESVFNQ---ISYIPQRPTL- 447
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--VDK------------DFNGEARPQPgikVGYLPQEPQLd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 448 FHGTILDNLTMFRSDQVEIMQRALELAAKL--------HLDEVFARLP------NGYDTEV-------------GDSSAD 500
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKDALDRFNEISAKYaepdadfdKLAAEQAELQeiidaaDAWDLDSqleiamdalrcppWDADVT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 501 LLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMI 554
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAV 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
361-533 |
8.53e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.59 E-value: 8.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEV--LHNINLRLEQGQIIGITGKNGVGKS----TLLNLVA--GQIvptKGSALLNGQ-----PPH 427
Cdd:PRK09473 13 LDVKDLRVTFSTPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGRI---GGSATFNGReilnlPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 428 DFD---AEsvfnQISYIPQRPTlfhgTILdNLTMFRSDQV-EIMQ--------RALELAAKLhLDEVfaRLP------NG 489
Cdd:PRK09473 90 ELNklrAE----QISMIFQDPM----TSL-NPYMRVGEQLmEVLMlhkgmskaEAFEESVRM-LDAV--KMPearkrmKM 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1733551959 490 YDTEvgdssadlLPAGVAQRITIVRALINRPSLILFDESNTSLD 533
Cdd:PRK09473 158 YPHE--------FSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
371-577 |
8.91e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.26 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 371 SPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPH----DFDAESVFNQISYIPQRP- 445
Cdd:PRK13646 16 TPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRPVRKRIGMVFQFPe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 446 -TLFHgtildnltmfrsDQVEimqRALELAAK---LHLDEVFAR-----LPNGYDTEVGDSSADLLPAGVAQRITIVRAL 516
Cdd:PRK13646 96 sQLFE------------DTVE---REIIFGPKnfkMNLDEVKNYahrllMDLGFSRDVMSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 517 INRPSLILFDESNTSLDGYSDRALCDLMRSL--KGTVSMILVSYRPSLLA-LADQRFSLEDGRL 577
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqtDENKTIILVSHDMNEVArYADEVIVMKEGSI 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
376-575 |
1.06e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 376 EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFD-AESVFNQISYIPQRPTLFHG-TIL 453
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 454 DNLTMFRSDQVEIMQRALELAAKL--HLDEvfarlpngydtevgDSSADLLPAGVAQRITIVRALINRPSLILFDESNTS 531
Cdd:PRK15439 105 ENILFGLPKRQASMQKMKQLLAALgcQLDL--------------DSSAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1733551959 532 LDGYSDRALCDLMRSLKGT-VSMILVSYR-PSLLALADQRFSLEDG 575
Cdd:PRK15439 171 LTPAETERLFSRIRELLAQgVGIVFISHKlPEIRQLADRISVMRDG 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
360-577 |
1.08e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 62.92 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSPKDP---EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGqppHDFDAES--- 433
Cdd:PRK13641 2 SIKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAG---YHITPETgnk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 434 ----VFNQISYIPQRP--TLFHGTILDNLtMFRSDQVEIMQRALELAAKLHLDEVfarlpnGYDTEVGDSSADLLPAGVA 507
Cdd:PRK13641 79 nlkkLRKKVSLVFQFPeaQLFENTVLKDV-EFGPKNFGFSEDEAKEKALKWLKKV------GLSEDLISKSPFELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 508 QRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL-KGTVSMILVSYRPSLLA-LADQRFSLEDGRL 577
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAeYADDVLVLEHGKL 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
380-578 |
1.19e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.35 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 380 NINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPhdFDAESVFN------QISYIPQRPTLF-HGTI 452
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL--FDAEKGIClppekrRIGYVFQDARLFpHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 453 LDNLT--MFRSDQVEIMQraleLAAKLHLDEVFARLPngydtevgdSSadlLPAGVAQRITIVRALINRPSLILFDESNT 530
Cdd:PRK11144 94 RGNLRygMAKSMVAQFDK----IVALLGIEPLLDRYP---------GS---LSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1733551959 531 SLDGYSDRALCDLMRSLKGTVS--MILVSYrpSL---LALADQRFSLEDGRLK 578
Cdd:PRK11144 158 SLDLPRKRELLPYLERLAREINipILYVSH--SLdeiLRLADRVVVLEQGKVK 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
382-533 |
1.44e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.52 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 382 NLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ-----PPHDfdaesvfNQISYIPQRPTLF-HGTILDN 455
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttPPSR-------RPVSMLFQENNLFsHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 456 LTM-------FRSDQVEIMQralELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQRITIVRALINRPSLILFDES 528
Cdd:PRK10771 92 IGLglnpglkLNAAQREKLH---AIARQMGIEDLLARLPGQ------------LSGGQRQRVALARCLVREQPILLLDEP 156
|
....*
gi 1733551959 529 NTSLD 533
Cdd:PRK10771 157 FSALD 161
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
361-581 |
2.09e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.16 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAgQIVPTKGSALLNGQPPHDFDAESVFNQISY 440
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRPTLFHGTILDNLTMFR--SDQvEIMQRALELAaklhLDEVFARLPNGYDTEVGDSSAdLLPAGVAQRITIVRALIN 518
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLDPYEqwSDE-EIWKVAEEVG----LKSVIEQFPDKLDFVLVDGGY-VLSNGHKQLMCLARSILS 1370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 519 RPSLILFDESNTSLDGYSDRAlcdLMRSLKGTVS---MILVSYRPSLLALADQRFSLEDGRLKPLD 581
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQI---IRKTLKQSFSnctVILSEHRVEALLECQQFLVIEGSSVKQYD 1433
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
360-567 |
2.25e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.59 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLL------NLVAGQiVPTKGSALLNGQPPHD--FDA 431
Cdd:PRK14258 7 AIKVNNLSFYYDTQ--KILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnrmNELESE-VRVEGRVEFFNQNIYErrVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 432 ESVFNQISYIPQRPTLFHGTILDNltmfrsdqVEIMQRALELAAKLHLDEVF------ARLPNGYDTEVGDSSADLlPAG 505
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDN--------VAYGVKIVGWRPKLEIDDIVesalkdADLWDEIKHKIHKSALDL-SGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 506 VAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRS--LKGTVSMILVSYR-PSLLALAD 567
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNlHQVSRLSD 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
378-576 |
2.43e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGqIVPT---KGSALLNGQP---PHDFDAESvfNQISYIPQRPTLF-HG 450
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEElqaSNIRDTER--AGIAIIHQELALVkEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 451 TILDNltMF---------RSDQVEIMQRALELAAKLHLD-EVfarlpngyDTEVGDssadlLPAGVAQRITIVRALINRP 520
Cdd:PRK13549 98 SVLEN--IFlgneitpggIMDYDAMYLRAQKLLAQLKLDiNP--------ATPVGN-----LGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1733551959 521 SLILFDESNTSLDGYSDRALCDLMRSLK-GTVSMILVSYR-PSLLALADQRFSLEDGR 576
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKaHGIACIYISHKlNEVKAISDTICVIRDGR 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
359-444 |
3.13e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.34 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 359 TSLDLKNLHFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQI 438
Cdd:PRK10575 10 TTFALRNVSFRVPGR--TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKV 87
|
....*.
gi 1733551959 439 SYIPQR 444
Cdd:PRK10575 88 AYLPQQ 93
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
134-303 |
4.79e-10 |
|
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: 60.95 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 134 DLAHVESTPSGMHLDRLSS-IELIRDFYASQASLVLIDLP-FILLFlgILALITGW---LVLIPII--MLGIAGFMAWKI 206
Cdd:cd18577 94 DIAWFDKNGAGELTSRLTSdTNLIQDGIGEKLGLLIQSLStFIAGF--IIAFIYSWkltLVLLATLplIAIVGGIMGKLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 207 GKSLQEQLEErrewdrrrY----SFLIEVLSGIHTVKAMAMEAMMLRRYERLLEsnafASAQVSQISGHAQTVGTITSHL 282
Cdd:cd18577 172 SKYTKKEQEA--------YakagSIAEEALSSIRTVKAFGGEEKEIKRYSKALE----KARKAGIKKGLVSGLGLGLLFF 239
|
170 180
....*....|....*....|....*
gi 1733551959 283 TV--AAVVGF--GSLMVINGTLSVG 303
Cdd:cd18577 240 IIfaMYALAFwyGSRLVRDGEISPG 264
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
83-305 |
4.85e-10 |
|
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: 60.99 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 83 LSTLAMLTIGVAialVLDVLLKIARARLSGWAGAQ---------YEHragciaIKRLAtgdLAHVESTPSGMHLDRLSS- 152
Cdd:cd18564 53 LLLAAAALVGIA---LLRGLASYAGTYLTALVGQRvvldlrrdlFAH------LQRLS---LSFHDRRRTGDLLSRLTGd 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 153 IELIRDFYASQASLVLIDLPFILLFLGI-------LALITgwLVLIPIIMLGIAGFmAWKIGKSLQEQleerREWDRRRY 225
Cdd:cd18564 121 VGAIQDLLVSGVLPLLTNLLTLVGMLGVmfwldwqLALIA--LAVAPLLLLAARRF-SRRIKEASREQ----RRREGALA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 226 SFLIEVLSGIHTVKAMAMEAMMLRRYERllESNAFASAQVSQI---SGHAQTVGTITShLTVAAVVGFGSLMVINGTLSV 302
Cdd:cd18564 194 SVAQESLSAIRVVQAFGREEHEERRFAR--ENRKSLRAGLRAArlqALLSPVVDVLVA-VGTALVLWFGAWLVLAGRLTP 270
|
...
gi 1733551959 303 GAL 305
Cdd:cd18564 271 GDL 273
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
380-580 |
5.52e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.39 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 380 NINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ-----PPHD---------FDAESVFNQISYIPQ-- 443
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhieglPGHQiarmgvvrtFQHVRLFREMTVIENll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 444 -------RPTLFHGtiLDNLTMFRSDQVEIMQRALELAAKLHLdevfarlpngydTEVGDSSADLLPAGVAQRITIVRAL 516
Cdd:PRK11300 103 vaqhqqlKTGLFSG--LLKTPAFRRAESEALDRAATWLERVGL------------LEHANRQAGNLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551959 517 INRPSLILFDESNTSLDGYSDRALCDLMRSLKGT--VSMILVSYRPSL-LALADQRFSLEDGrlKPL 580
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAELRNEhnVTVLLIEHDMKLvMGISDRIYVVNQG--TPL 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
361-576 |
6.91e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.13 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYsPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISY 440
Cdd:PRK13647 5 IEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRP--TLFHGTILDNLTM----FRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQRITIVR 514
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVAFgpvnMGLDKDEVERRVEEALKAVRMWDFRDKPPYH------------LSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 515 ALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLAL--ADQRFSLEDGR 576
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAewADQVIVLKEGR 215
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
361-577 |
6.92e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.20 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSpKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISY 440
Cdd:PRK13652 4 IETRDLCYSYS-GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRP--TLFHGTILDNL----TMFRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQRITIVR 514
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIafgpINLGLDEETVAHRVSSALHMLGLEELRDRVPHH------------LSGGEKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 515 ALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILV--SYRPSLLA-LADQRFSLEDGRL 577
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVPeMADYIYVMDKGRI 216
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
127-307 |
7.19e-10 |
|
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: 60.52 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 127 IKRLATGDLAHVESTPSGMHLDRLSS-IELIRDFYASQ-----ASLVLIDLPFILLFL--GILALITgwLVLIPIIMLGI 198
Cdd:cd18551 76 WRRLLRLPVSFFDRRRSGDLVSRVTNdTTLLRELITSGlpqlvTGVLTVVGAVVLMFLldWVLTLVT--LAVVPLAFLII 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 199 AGFMAW--KIGKSLQEQLEERRewdrrrySFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVG 276
Cdd:cd18551 154 LPLGRRirKASKRAQDALGELS-------AALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLM 226
|
170 180 190
....*....|....*....|....*....|.
gi 1733551959 277 TITSHLTVAAVVGFGSLMVINGTLSVGALAA 307
Cdd:cd18551 227 GLAVQLALLVVLGVGGARVASGALTVGTLVA 257
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
360-576 |
9.52e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 60.06 E-value: 9.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYSPKDP---EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAE--SV 434
Cdd:PRK13637 2 SIKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 435 FNQISYIPQRP--TLFHGTI-------LDNLTMfrSDQvEIMQRALELAAKLHLDevfarlpngYDTeVGDSSADLLPAG 505
Cdd:PRK13637 82 RKKVGLVFQYPeyQLFEETIekdiafgPINLGL--SEE-EIENRVKRAMNIVGLD---------YED-YKDKSPFELSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 506 VAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSM--ILVSYRPSLLA-LADQRFSLEDGR 576
Cdd:PRK13637 149 QKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMtiILVSHSMEDVAkLADRIIVMNKGK 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
376-576 |
1.05e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.22 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 376 EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQI---VPTKGSALLNGQPphdFDAESvFNQISYIPQRPTLFHG-- 450
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGMP---IDAKE-MRAISAYVQQDDLFIPtl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 451 TILDNLT---MFRsdqveiMQRALELAAKLH-LDEVFAR--LPNGYDTEVGD-SSADLLPAGVAQRITIVRALINRPSLI 523
Cdd:TIGR00955 115 TVREHLMfqaHLR------MPRRVTKKEKRErVDEVLQAlgLRKCANTRIGVpGRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551959 524 LFDESNTSLDGYSDRALCDLMRSL--KGTvSMILVSYRPS--LLALADQRFSLEDGR 576
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLaqKGK-TIICTIHQPSseLFELFDKIILMAEGR 244
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
354-432 |
1.12e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.27 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 354 KMDRFTSLDLKNLHfrYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQivP----TKGSALLNGQPPHDF 429
Cdd:CHL00131 1 MNKNKPILEIKNLH--ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PaykiLEGDILFKGESILDL 76
|
...
gi 1733551959 430 DAE 432
Cdd:CHL00131 77 EPE 79
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
385-533 |
2.04e-09 |
|
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: 58.57 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 385 LEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGsallngqpphdfDAESVFNQISYIPQRPTL-FHGTILDNLTMFRSDQ 463
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG------------DIEIELDTVSYKPQYIKAdYEGTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 464 VEIMQRALELAAKLHLDEVfarlpngYDTEVGDssadlLPAGVAQRITIVRALINRPSLILFDESNTSLD 533
Cdd:cd03237 90 YTHPYFKTEIAKPLQIEQI-------LDREVPE-----LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
377-567 |
2.53e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.46 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIPQRPTLFHGTILDNL 456
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 457 ------------TMFRSDQVEIMQRALELAAKLHLdevfarlpngydtevGDSSADLLPAGVAQRITIVRALINRPSLIL 524
Cdd:PRK10253 102 vargryphqplfTRWRKEDEEAVTKAMQATGITHL---------------ADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1733551959 525 FDESNTSLDGYSDRALCDLMRSL---KG-TVSMIL------VSYRPSLLALAD 567
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELnreKGyTLAAVLhdlnqaCRYASHLIALRE 219
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
361-547 |
2.54e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.40 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPevLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSAL--LNGQPPHDFDAESVfnqi 438
Cdd:PRK11701 7 LSVRGLTKLYGPRKG--CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrMRDGQLRDLYALSE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 439 syiPQRPTLF-------HGTILDNLTMFRSDQVEIMQRALELAAKlH-----------LDEVfarlpngydtEVGDSSAD 500
Cdd:PRK11701 81 ---AERRRLLrtewgfvHQHPRDGLRMQVSAGGNIGERLMAVGAR-HygdiratagdwLERV----------EIDAARID 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 501 LLPA----GVAQRITIVRALINRPSLILFDESNTSLDgYSDRA-LCDLMRSL 547
Cdd:PRK11701 147 DLPTtfsgGMQQRLQIARNLVTHPRLVFMDEPTGGLD-VSVQArLLDLLRGL 197
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
364-578 |
2.88e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.56 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 364 KNLHFRY----SPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFD--------A 431
Cdd:PRK13633 8 KNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwdirnkA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 432 ESVF----NQISyipqrptlfhGTILDNLTMFRSDQVEIMQRALelaaKLHLDEVFARLpNGYdtEVGDSSADLLPAGVA 507
Cdd:PRK13633 88 GMVFqnpdNQIV----------ATIVEEDVAFGPENLGIPPEEI----RERVDESLKKV-GMY--EYRRHAPHLLSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733551959 508 QRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL--KGTVSMILVSYRPSLLALADQRFSLEDGRLK 578
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
361-577 |
3.24e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.59 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDP---EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSA----LLNGQPPHDFDAES 433
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 434 VFNQISYIPQRP--TLFHGTILDNLTmFRSDQVEIMQRALELAAKLHLDEVfarlpnGYDTEVGDSSADLLPAGVAQRIT 511
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVA-FGPQNFGIPKEKAEKIAAEKLEMV------GLADEFWEKSPFELSGGQMRRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1733551959 512 IVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGT-VSMILVSYRPSLLA-LADQRFSLEDGRL 577
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVAdYADYVYLLEKGHI 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
361-533 |
3.41e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.43 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEVLH---NINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSA-LLNGQPPHDFDAESVFN 436
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 437 Q------ISYIPQRPTLF-HGTILDNLTmfRSDQVEI-----MQRALELAAKLHLDEVFARlpngydtEVGDSSADLLPA 504
Cdd:TIGR03269 360 RgrakryIGILHQEYDLYpHRTVLDNLT--EAIGLELpdelaRMKAVITLKMVGFDEEKAE-------EILDKYPDELSE 430
|
170 180
....*....|....*....|....*....
gi 1733551959 505 GVAQRITIVRALINRPSLILFDESNTSLD 533
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
360-533 |
3.49e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 58.70 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 360 SLDLKNLHFRYsPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQP-----PHDFDAESV 434
Cdd:PRK11650 3 GLKLQAVRKSY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvnelePADRDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 435 FnqisyipQRPTLF-HGTILDN----LTMFRSDQVEIMQRALELAAKLHLDEVFARLPNGydtevgdssadlLPAGVAQR 509
Cdd:PRK11650 82 F-------QNYALYpHMSVRENmaygLKIRGMPKAEIEERVAEAARILELEPLLDRKPRE------------LSGGQRQR 142
|
170 180
....*....|....*....|....*.
gi 1733551959 510 ITIVRALINRPSLILFDE--SNtsLD 533
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEplSN--LD 166
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
378-577 |
4.60e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQ-ISYIPQR----PTLfhgTI 452
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgVAIIYQElhlvPEM---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 453 LDNLTMFR-------SDQVEIMQRALELAAKLHLDeVFARLPNGYdtevgdssadlLPAGVAQRITIVRALINRPSLILF 525
Cdd:PRK11288 97 AENLYLGQlphkggiVNRRLLNYEAREQLEHLGVD-IDPDTPLKY-----------LSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 526 DESNTSLDGYSDRALCDLMRSLK--GTVsMILVSYR-PSLLALADQRFSLEDGRL 577
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRaeGRV-ILYVSHRmEEIFALCDAITVFKDGRY 218
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
77-318 |
4.96e-09 |
|
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: 57.78 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 77 ILPYEG-LSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQyehragciAIKRLATgDL-AHVES--------TPSGMH 146
Cdd:cd18544 30 IVPGQGdLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQR--------IIYDLRR-DLfSHIQRlplsffdrTPVGRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 147 LDRLSS-IELIRDFYASQASLVLIDlpfILLFLGI----------LALITgwLVLIPIIMLGIAGFMAwKIGKSLQE--- 212
Cdd:cd18544 101 VTRVTNdTEALNELFTSGLVTLIGD---LLLLIGIliamfllnwrLALIS--LLVLPLLLLATYLFRK-KSRKAYREvre 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 213 ---QLeerrewdrrrYSFLIEVLSGIHTVKAMAMEAMMLRRYERLleSNAFASAQVSQISGHA--QTVGTITSHLTVAAV 287
Cdd:cd18544 175 klsRL----------NAFLQESISGMSVIQLFNREKREFEEFDEI--NQEYRKANLKSIKLFAlfRPLVELLSSLALALV 242
|
250 260 270
....*....|....*....|....*....|.
gi 1733551959 288 VGFGSLMVINGTLSVGALAASTLLAGRTVQP 318
Cdd:cd18544 243 LWYGGGQVLSGAVTLGVLYAFIQYIQRFFRP 273
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
372-562 |
5.19e-09 |
|
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: 58.99 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 372 PKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNlVAGQIVPTKGSALLNGQPphdfdaesvfNQISYIPQRPTLFHGT 451
Cdd:TIGR00954 462 PNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLTKPAK----------GKLFYVPQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 452 ILDNLT-------MFR---SDQVeiMQRALELaakLHLDEVFARlpngydtEVGDSS----ADLLPAGVAQRITIVRALI 517
Cdd:TIGR00954 531 LRDQIIypdssedMKRrglSDKD--LEQILDN---VQLTHILER-------EGGWSAvqdwMDVLSGGEKQRIAMARLFY 598
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1733551959 518 NRPSLILFDESNTSLDGYSDRALCDLMRslKGTVSMILVSYRPSL 562
Cdd:TIGR00954 599 HKPQFAILDECTSAVSVDVEGYMYRLCR--EFGITLFSVSHRKSL 641
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
300-527 |
5.21e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.83 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 300 LSVGALAASTLLAGRTvqPALRALGLWSRFQSVSLAEDNLRDIDAipAESRGRFKM----DRFTSLDLKNLHFRYsPKDP 375
Cdd:PRK10522 262 TNVAATYSLTLLFLRT--PLLSAVGALPTLLSAQVAFNKLNKLAL--APYKAEFPRpqafPDWQTLELRNVTFAY-QDNG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 376 EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQISYIPQRPTLFHGTILDN 455
Cdd:PRK10522 337 FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPE 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 456 LTMFRSDQVEIMQRALELAAKLHLDEVFARLPNgydtevgdssadlLPAGVAQRITIVRALINRPSLILFDE 527
Cdd:PRK10522 417 GKPANPALVEKWLERLKMAHKLELEDGRISNLK-------------LSKGQKKRLALLLALAEERDILLLDE 475
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
361-533 |
5.70e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.18 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNL--HFRYS---------PKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDF 429
Cdd:PRK15079 9 LEVADLkvHFDIKdgkqwfwqpPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 430 DAE---SVFNQISYIPQ------RPTLFHGTIL-DNLTMFRS--DQVEIMQRALELAAKLHLdevfarLP---NGYDTEv 494
Cdd:PRK15079 89 KDDewrAVRSDIQMIFQdplaslNPRMTIGEIIaEPLRTYHPklSRQEVKDRVKAMMLKVGL------LPnliNRYPHE- 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1733551959 495 gdssadlLPAGVAQRITIVRALINRPSLILFDESNTSLD 533
Cdd:PRK15079 162 -------FSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
361-557 |
6.67e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.32 E-value: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYspKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQpPHDFDAESVF---NQ 437
Cdd:PRK13638 2 LATSDLWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK-PLDYSKRGLLalrQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYIPQRP--TLFHGTI-------LDNLTMFRSDQVEIMQRALELAAKLHldevFARLPngydtevgdssADLLPAGVAQ 508
Cdd:PRK13638 79 VATVFQDPeqQIFYTDIdsdiafsLRNLGVPEAEITRRVDEALTLVDAQH----FRHQP-----------IQCLSHGQKK 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1733551959 509 RITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVS 557
Cdd:PRK13638 144 RVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIS 192
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
361-548 |
7.64e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.11 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYspKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPhDFDAESVFNQISY 440
Cdd:PRK13540 2 LDVIELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 441 IPQRptlfhGTILDNLTMFRSDQVEIMQRalelAAKLHLDEVFARLPNGYdteVGDSSADLLPAGVAQRITIVRALINRP 520
Cdd:PRK13540 79 VGHR-----SGINPYLTLRENCLYDIHFS----PGAVGITELCRLFSLEH---LIDYPCGLLSSGQKRQVALLRLWMSKA 146
|
170 180
....*....|....*....|....*...
gi 1733551959 521 SLILFDESNTSLDgysDRALCDLMRSLK 548
Cdd:PRK13540 147 KLWLLDEPLVALD---ELSLLTIITKIQ 171
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
361-577 |
1.30e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 56.35 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFN---Q 437
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDireK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYIPQRP-TLFHGTI--------LDNLTMFRSDQVEIMQRALELAAKLhldevfarlpngydtEVGDSSADLLPAGVAQ 508
Cdd:PRK13640 86 VGIVFQNPdNQFVGATvgddvafgLENRAVPRPEMIKIVRDVLADVGML---------------DYIDSEPANLSGGQKQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551959 509 RITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSL--LALADQRFSLEDGRL 577
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIdeANMADQVLVLDDGKL 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
361-557 |
1.84e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 55.87 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPK-DPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQpphDFDAESVFN--- 436
Cdd:PRK13642 5 LEVENLVFKYEKEsDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 437 QISYIPQRP--TLFHGTILDNLTMFRSDQ----VEIMQRALELAAKLHLDEVFARLPNgydtevgdssadLLPAGVAQRI 510
Cdd:PRK13642 82 KIGMVFQNPdnQFVGATVEDDVAFGMENQgiprEEMIKRVDEALLAVNMLDFKTREPA------------RLSGGQKQRV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1733551959 511 TIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILVS 557
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLS 196
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
363-427 |
2.09e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.25 E-value: 2.09e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 363 LKNL-HFRYSPKdpEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPH 427
Cdd:COG4586 24 LKGLfRREYREV--EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPF 87
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
377-548 |
2.41e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.64 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKST----LLNLVAGQivptkGSALLNGQPPHDFDAES---VFNQISYIPQRPTLFH 449
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 450 GTILDNLTM----FRSDQVEIMQRALELAAKLHLDEVfarlpnGYDTEVGDSSADLLPAGVAQRITIVRALINRPSLILF 525
Cdd:PRK15134 376 NPRLNVLQIieegLRVHQPTLSAAQREQQVIAVMEEV------GLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180
....*....|....*....|...
gi 1733551959 526 DESNTSLDGYSDRALCDLMRSLK 548
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQ 472
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
128-307 |
2.62e-08 |
|
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: 55.57 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 128 KRLATGDLAHVESTPSGMHLDRLSS-IELIRDFYASQASLVLIDLpfiLLFLG--ILALITGW------LVLIPIIMLGI 198
Cdd:cd18575 77 AHLLRLSPSFFETTRTGEVLSRLTTdTTLIQTVVGSSLSIALRNL---LLLIGglVMLFITSPkltllvLLVIPLVVLPI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 199 AGFMAW--KIGKSLQEQLEERRewdrrrySFLIEVLSGIHTVKAMAMEAMMLRRYERLLEsNAFASAQvSQISGHAQTVG 276
Cdd:cd18575 154 ILFGRRvrRLSRASQDRLADLS-------AFAEETLSAIKTVQAFTREDAERQRFATAVE-AAFAAAL-RRIRARALLTA 224
|
170 180 190
....*....|....*....|....*....|....
gi 1733551959 277 TITShLTVAAVVG---FGSLMVINGTLSVGALAA 307
Cdd:cd18575 225 LVIF-LVFGAIVFvlwLGAHDVLAGRMSAGELSQ 257
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
376-577 |
2.74e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.88 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 376 EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGqppHDF----DAESVF--NQISYIPQ-RPTLF 448
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSG---HDItrlkNREVPFlrRQIGMIFQdHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 449 HGTILDNLTMfrsdqveimqraLELAAKLHLDEVFARLPNGYDtEVG--DSSADL---LPAGVAQRITIVRALINRPSLI 523
Cdd:PRK10908 93 DRTVYDNVAI------------PLIIAGASGDDIRRRVSAALD-KVGllDKAKNFpiqLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 524 LFDESNTSLDGYSDRALCDLMRSLKGT-VSMILVSYRPSLLALADQR-FSLEDGRL 577
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVgVTVLMATHDIGLISRRSYRmLTLSDGHL 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
378-533 |
3.13e-08 |
|
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: 56.62 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTL----LNLvagqiVPTKGSALLNGQPPHDFDAES----------VFnQ------ 437
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRL-----IPSEGEIRFDGQDLDGLSRRAlrplrrrmqvVF-Qdpfgsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 -----ISYIPQRPTLFHGTILDnltmfRSDQVEIMQRALElaaklhldevfarlpngydtEVGdssadlLPAGVA----- 507
Cdd:COG4172 376 sprmtVGQIIAEGLRVHGPGLS-----AAERRARVAEALE--------------------EVG------LDPAARhryph 424
|
170 180 190
....*....|....*....|....*....|...
gi 1733551959 508 -------QRITIVRALINRPSLILFDESNTSLD 533
Cdd:COG4172 425 efsggqrQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
378-575 |
3.37e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.33 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFD-AESVFNQISYIPQRPTLFHG-TILDN 455
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 456 LTMFRS-----------DQVEIMQRALELAAK--LHLDevfarlpngYDTEVGDssadlLPAGVAQRITIVRALINRPSL 522
Cdd:PRK09700 101 LYIGRHltkkvcgvniiDWREMRVRAAMMLLRvgLKVD---------LDEKVAN-----LSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 523 ILFDESNTSLDGYSDRALCDLMRSLKGT-VSMILVSYR-PSLLALADQRFSLEDG 575
Cdd:PRK09700 167 IIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
149-330 |
3.87e-08 |
|
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: 55.18 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 149 RLSS-IELIRDFYAS------QASLVLI-DLPFILLFLGILALITgwLVLIPIIMLGIAGFMAW--KIGKSLQEQLEERR 218
Cdd:cd18576 98 RLSNdVTQIQDTLTTtlaeflRQILTLIgGVVLLFFISWKLTLLM--LATVPVVVLVAVLFGRRirKLSKKVQDELAEAN 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 219 ewdrrrySFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVING 298
Cdd:cd18576 176 -------TIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAG 248
|
170 180 190
....*....|....*....|....*....|...
gi 1733551959 299 TLSVGALAASTLLAGRTVQPaLRALG-LWSRFQ 330
Cdd:cd18576 249 ELTAGDLVAFLLYTLFIAGS-IGSLAdLYGQLQ 280
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
361-576 |
4.12e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.81 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKDPE--VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPT---KGSALLNGQPPHDFdAESVF 435
Cdd:cd03233 4 LSWRNISFTTGKGRSKipILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEF-AEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 436 NQISYIPQRPTLFHgtildNLTmfrsdqveiMQRALELAAKLHLDEvFARLPNGydtevgdssadllpaGVAQRITIVRA 515
Cdd:cd03233 83 GEIIYVSEEDVHFP-----TLT---------VRETLDFALRCKGNE-FVRGISG---------------GERKRVSIAEA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551959 516 LINRPSLILFDESNTSLDgySDRALcDLMRSLK------GTVSMILVsYRPS--LLALADQRFSLEDGR 576
Cdd:cd03233 133 LVSRASVLCWDNSTRGLD--SSTAL-EILKCIRtmadvlKTTTFVSL-YQASdeIYDLFDKVLVLYEGR 197
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
379-533 |
4.37e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.65 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 379 HNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAEsvFNQIsyipqrpTLF---HGTILDN 455
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE--YHQD-------LLYlghQPGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 456 LTMFrsdqvEIMQRALELAAKLHLDEVFARLpngydTEVG-----DSSADLLPAGVAQRITIVRALINRPSLILFDESNT 530
Cdd:PRK13538 89 LTAL-----ENLRFYQRLHGPGDDEALWEAL-----AQVGlagfeDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
...
gi 1733551959 531 SLD 533
Cdd:PRK13538 159 AID 161
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
376-556 |
5.11e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.63 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 376 EVLHNINLRLEQGQIIGITGKNGVGKSTLL----NLVAGQIVPTKGSALLN------GQPPHDFDAESVfnQISYIPQRP 445
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIELLGrtvqreGRLARDIRKSRA--NTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 446 TLFHG-TILDNL------------TMFRSDQVEIMQRALELAAKLHLDEvFARlpngydtevgdSSADLLPAGVAQRITI 512
Cdd:PRK09984 96 NLVNRlSVLENVligalgstpfwrTCFSWFTREQKQRALQALTRVGMVH-FAH-----------QRVSTLSGGQQQRVAI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1733551959 513 VRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMILV 556
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVV 207
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
378-533 |
5.37e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.08 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGqIVPTKGSALLNGQPPHDFDAESVFNQISYIPQR-PTLFHGTILDNL 456
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 457 TMFRSDQV---EIMQRALELAAKLHLDEVFARlpngydtevgdsSADLLPAGVAQRITIVRAL------IN-RPSLILFD 526
Cdd:COG4138 91 ALHQPAGAsseAVEQLLAQLAEALGLEDKLSR------------PLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLD 158
|
....*..
gi 1733551959 527 ESNTSLD 533
Cdd:COG4138 159 EPMNSLD 165
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
174-336 |
6.46e-08 |
|
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: 54.47 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 174 ILLFLGILA--LITGW------LVLIPIIML--GIAGFMAWKIGKSLQEQLEERRewdrrrySFLIEVLSGIHTVKAMAM 243
Cdd:cd18572 121 LVQLVGGLAfmFSLSWrltllaFITVPVIALitKVYGRYYRKLSKEIQDALAEAN-------QVAEEALSNIRTVRSFAT 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 244 EAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGALAASTLLAGrTVQPALRAL 323
Cdd:cd18572 194 EEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQ-QLGEAFQSL 272
|
170
....*....|....*
gi 1733551959 324 G-LWSRF-QSVSLAE 336
Cdd:cd18572 273 GdVFSSLmQAVGAAE 287
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
378-577 |
7.23e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQP-----PHDFDAesvfNQISYIPQ---RPTLFH 449
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEvvtrsPQDGLA----NGIVYISEdrkRDGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 450 G-TILDNLTM-----FRSDQVEIMQRALELAAklhldEVFARLPNgYDTEVGDSSADLLPAGVAQRITIVRALINRPSLI 523
Cdd:PRK10762 344 GmSVKENMSLtalryFSRAGGSLKHADEQQAV-----SDFIRLFN-IKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 524 LFDESNTSLDGYSDRALCDLMRSLKGT-VSMILVSYR-PSLLALADQRFSLEDGRL 577
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEmPEVLGMSDRILVMHEGRI 473
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
352-423 |
9.50e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 9.50e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 352 RFKMDRFTSLDLKNLHFRysPKDPE---VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNG 423
Cdd:PRK13545 13 KYKMYNKPFDKLKDLFFR--SKDGEyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
388-567 |
9.94e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.52 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 388 GQIIGITGKNGVGKSTLLNLVAGQIVPTKGsallNGQPPHDFDA----------ESVFNQI-----------SYIPQRPT 446
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLG----KFDDPPDWDEildefrgselQNYFTKLlegdvkvivkpQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 447 LFHGTILDNLTmfRSDQVEIMQralELAAKLHLDEVFARlpngydtevgdsSADLLPAGVAQRITIVRALINRPSLILFD 526
Cdd:cd03236 102 AVKGKVGELLK--KKDERGKLD---ELVDQLELRHVLDR------------NIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1733551959 527 ESNTSLDGYSDRALCDLMRSL-KGTVSMILVSYRPSLL-ALAD 567
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELaEDDNYVLVVEHDLAVLdYLSD 207
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
149-302 |
1.41e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 53.61 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 149 RLSS-IELIRDFYASQASLVLIDlpFILLFLG-ILALITGW------LVLIPIIMlgIAGFMAWKIGKSLQEQLEERREW 220
Cdd:cd18578 116 RLSTdASDVRGLVGDRLGLILQA--IVTLVAGlIIAFVYGWklalvgLATVPLLL--LAGYLRMRLLSGFEEKNKKAYEE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 221 DRrrySFLIEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTL 300
Cdd:cd18578 192 SS---KIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEY 268
|
..
gi 1733551959 301 SV 302
Cdd:cd18578 269 TF 270
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
361-524 |
1.45e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.26 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRySPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAESVFNQ-IS 439
Cdd:COG3845 258 LEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 440 YIPQ-RptLFHGTILD-----NLTMFRSDQVE-----IMQRAlelAAKLHLDEVFARlpngYD--TEVGDSSADLLPAGV 506
Cdd:COG3845 337 YIPEdR--LGRGLVPDmsvaeNLILGRYRRPPfsrggFLDRK---AIRAFAEELIEE----FDvrTPGPDTPARSLSGGN 407
|
170
....*....|....*...
gi 1733551959 507 AQRITIVRALINRPSLIL 524
Cdd:COG3845 408 QQKVILARELSRDPKLLI 425
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
380-527 |
1.54e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.75 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 380 NINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQP--PHDFDAESvfnQISYIPQRPTLFhG--TILDN 455
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPvdAGDIATRR---RVGYMSQAFSLY-GelTVRQN 359
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551959 456 LTM----FRSDQVEIMQRALELAAKLHLdevfarlpngydTEVGDSSADLLPAGVAQRITIVRALINRPSLILFDE 527
Cdd:NF033858 360 LELharlFHLPAAEIAARVAEMLERFDL------------ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
387-533 |
1.90e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 387 QGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSAllngqpphDFDAEsvfnqISYIPQR-PTLFHGTILDNL----TMFRS 461
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELK-----ISYKPQYiKPDYDGTVEDLLrsitDDLGS 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 462 D--QVEIMQRalelaakLHLDEVfarlpngYDTEVGDssadlLPAGVAQRITIVRALINRPSLILFDESNTSLD 533
Cdd:PRK13409 431 SyyKSEIIKP-------LQLERL-------LDKNVKD-----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
149-330 |
1.96e-07 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 52.86 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 149 RLSSIELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIMLGIAGFMAWKIGKSLQEQLEERREWDRRRYSFL 228
Cdd:cd18569 104 RVQSNDRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGTT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 229 IEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGALAAS 308
Cdd:cd18569 184 MSGLQMIETLKASGAESDFFSRWAGYQAKVLNAQQELGRTNQLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAF 263
|
170 180
....*....|....*....|..
gi 1733551959 309 TLLAGRTVQPALRALGLWSRFQ 330
Cdd:cd18569 264 QSLMASFLAPVNSLVGLGGTLQ 285
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
174-331 |
2.12e-07 |
|
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: 52.79 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 174 ILLFLGILAL---ITGWLVLIPIIMLGIAGFMAWKIGKSLQEQLEERREWDRRRYSFLIEVLSGIHTVKAMAMEAMMLRR 250
Cdd:cd18547 130 ILTIVGTLIMmlyISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 251 YERLlesnafaSAQVSQISGHAQTVGTIT-------SHLTVAAVVGFGSLMVINGTLSVGALAASTLLAGRTVQPALRAL 323
Cdd:cd18547 210 FDEI-------NEELYKASFKAQFYSGLLmpimnfiNNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQIS 282
|
....*...
gi 1733551959 324 GLWSRFQS 331
Cdd:cd18547 283 QQINSLQS 290
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
385-556 |
2.30e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 385 LEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSalLNGQPPHD-----FDAESVFN--------------QISYIPQRP 445
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEPSWDevlkrFRGTELQNyfkklyngeikvvhKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 446 TLFHGTILDNLTmfRSDQVEIMQralELAAKLHLDEVFarlpngyDTEVGDssadlLPAGVAQRITIVRALINRPSLILF 525
Cdd:PRK13409 174 KVFKGKVRELLK--KVDERGKLD---EVVERLGLENIL-------DRDISE-----LSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|.
gi 1733551959 526 DESNTSLDGYSDRALCDLMRSLKGTVSMILV 556
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELAEGKYVLVV 267
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
382-533 |
2.48e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.11 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 382 NLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDF-DAE----------SVFNQISYIPqrptlfHG 450
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsDAElrevrrkkiaMVFQSFALMP------HM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 451 TILDNlTMFRSD-----QVEIMQRALELAAKLHLDEvfarLPNGYDTEvgdssadlLPAGVAQRITIVRALINRPSLILF 525
Cdd:PRK10070 122 TVLDN-TAFGMElaginAEERREKALDALRQVGLEN----YAHSYPDE--------LSGGMRQRVGLARALAINPDILLM 188
|
....*...
gi 1733551959 526 DESNTSLD 533
Cdd:PRK10070 189 DEAFSALD 196
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
342-418 |
2.83e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 342 IDAIPAESRG----RFKMDR---FTSLDLKNLHFRYspkDPEVL-HNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIV 413
Cdd:PRK15064 294 LEEVKPSSRQnpfiRFEQDKklhRNALEVENLTKGF---DNGPLfKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELE 370
|
....*
gi 1733551959 414 PTKGS 418
Cdd:PRK15064 371 PDSGT 375
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
82-324 |
2.90e-07 |
|
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: 52.48 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 82 GLSTLAMLTIGVAIALVLDVLLKIARARLSGWAGAQYEHRagciaikrLATGDLAHVESTPSGMHlDRLSS--------- 152
Cdd:cd18543 34 DRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHD--------LRTDLFAHLQRLDGAFH-DRWQSgqllsrats 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 153 -IELIRDFYAsQASLVLIDLPFILLFLGILALITGWLVLIPIIMLGIAGFMAWKIGKSL-------QEQLEERREWDRrr 224
Cdd:cd18543 105 dLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYfpasrraQDQAGDLATVVE-- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 225 ysfliEVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGA 304
Cdd:cd18543 182 -----ESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGT 256
|
250 260
....*....|....*....|
gi 1733551959 305 LAASTLLAGRTVQPAlRALG 324
Cdd:cd18543 257 LVAFSAYLTMLVWPV-RMLG 275
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
378-557 |
3.13e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.19 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPHDFDAEsvfNQISYIPQRPTL---FHGTILD 454
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK---NLVAYVPQSEEVdwsFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 455 NLTMFRSDQVEIMQRALELAAKLhLDEVFAR--LPNGYDTEVGDssadlLPAGVAQRITIVRALINRPSLILFDESNTSL 532
Cdd:PRK15056 100 VVMMGRYGHMGWLRRAKKRDRQI-VTAALARvdMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180
....*....|....*....|....*
gi 1733551959 533 DGYSDRALCDLMRSLKGTVSMILVS 557
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVS 198
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
377-577 |
3.62e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.02 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLL---NLVAGQIVPTK--GSALLNGQPPHDF-DAESVFNQISYIPQRPTLFHG 450
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlNRMNDKVSGYRysGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 451 TILDNLTMFRSDQVEIMQRALELAAKLHLDEVfarlpnGYDTEVGDSSAD---LLPAGVAQRITIVRALINRPSLILFDE 527
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV------GLWDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1733551959 528 SNTSLDGYSDRALCDLMRSLKGTVSMILVSYRPSLLALADQRFSL-EDGRL 577
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALfFDGRL 240
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
377-576 |
4.46e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.96 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPT--KGSALLNGQPPhdfdAESVFNQISYIPQRPTLF-HGTIL 453
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKP----TKQILKRTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 454 DNL---TMFRSDQVEIMQRALELAAKLHLDEVFARLPNgydTEVGDSSADLLPAGVAQRITIVRALINRPSLILFDESNT 530
Cdd:PLN03211 159 ETLvfcSLLRLPKSLTKQEKILVAESVISELGLTKCEN---TIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1733551959 531 SLDGYSDRALCDLMRSLKGTVSMILVS-YRPS--LLALADQRFSLEDGR 576
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSsrVYQMFDSVLVLSEGR 284
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
174-330 |
6.25e-07 |
|
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: 51.30 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 174 ILLFLG---ILALITGWLVLIPIIMLGIAGFMAWKIGKSLQEQLEERREWDRRRYSFLIEVLSGIHTVKAMAMEAMMLRR 250
Cdd:cd18549 127 IITIIGsfiILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEK 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 251 YERllESNAFASAQVSQISGHAQTVGTIT--SHLTVAAVVGFGSLMVINGTLSVGALAASTLLAGRTVQPALRALGLWSR 328
Cdd:cd18549 207 FDE--GNDRFLESKKKAYKAMAYFFSGMNffTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQ 284
|
..
gi 1733551959 329 FQ 330
Cdd:cd18549 285 YQ 286
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
368-591 |
6.72e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.55 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 368 FRYsPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSAllngqpphdFDAESVfnqisyipqRPTL 447
Cdd:PLN03073 516 FGY-PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV---------FRSAKV---------RMAV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 448 FHGTILDNLTMfRSDQVEIMQR----ALELAAKLHLDEVfarlpnGYDTEVGDSSADLLPAGVAQRITIVRALINRPSLI 523
Cdd:PLN03073 577 FSQHHVDGLDL-SSNPLLYMMRcfpgVPEQKLRAHLGSF------GVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIL 649
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551959 524 LFDESNTSLDGYSDRALCDLMRSLKGTVSMilVSYRPSLLALA-DQRFSLEDGRLKPL--DFADHKNLSRT 591
Cdd:PLN03073 650 LLDEPSNHLDLDAVEALIQGLVLFQGGVLM--VSHDEHLISGSvDELWVVSEGKVTPFhgTFHDYKKTLQS 718
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
377-564 |
8.99e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 50.34 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIV--PTKGSALLngqPPHDFDAESvfnqisyipqrptlfhgTILD 454
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV---PDNQFGREA-----------------SLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 455 NltmfrsdqveimqraleLAAKLHLDEVFARLPNgydteVGDSSADL-------LPAGVAQRITIVRALINRPSLILFDE 527
Cdd:COG2401 105 A-----------------IGRKGDFKDAVELLNA-----VGLSDAVLwlrrfkeLSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1733551959 528 SNTSLDGYS----DRALCDLMRSLKGTVsmILVSYRPSLLA 564
Cdd:COG2401 163 FCSHLDRQTakrvARNLQKLARRAGITL--VVATHHYDVID 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
385-568 |
9.50e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.71 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 385 LEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGsallNGQPPHDFDA--------------ESVFNQ---ISYIPQR--- 444
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLG----DYDEEPSWDEvlkrfrgtelqdyfKKLANGeikVAHKPQYvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 445 -PTLFHGTILDNLTmfRSDQVEImqrALELAAKLHLDEVFarlpngyDTEVGDssadlLPAGVAQRITIVRALINRPSLI 523
Cdd:COG1245 172 iPKVFKGTVRELLE--KVDERGK---LDELAEKLGLENIL-------DRDISE-----LSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1733551959 524 LFDESNTSLDGYSDRALCDLMRSL-KGTVSMILVSYRPSLL-ALADQ 568
Cdd:COG1245 235 FFDEPSSYLDIYQRLNVARLIRELaEEGKYVLVVEHDLAILdYLADY 281
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
385-533 |
1.09e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.71 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 385 LEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSAllngqpphDFDAEsvfnqISYIPQR-PTLFHGTILDNLTMFRSDQ 463
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLK-----ISYKPQYiSPDYDGTVEEFLRSANTDD 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 464 VEIMQRALELAAKLHLDEVFarlpngydtevgDSSADLLPAGVAQRITIVRALINRPSLILFDESNTSLD 533
Cdd:COG1245 430 FGSSYYKTEIIKPLGLEKLL------------DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
374-581 |
1.09e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 374 DPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLngqpphdfdAESVfnQISYIPQRptlfhgtil 453
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGI--KLGYFAQH--------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 454 dNLTMFRSDQVEImQRALELAAKlHLDEVFARLPNGYDTEvGDSSADL---LPAGVAQRitIVRALI--NRPSLILFDES 528
Cdd:PRK10636 384 -QLEFLRADESPL-QHLARLAPQ-ELEQKLRDYLGGFGFQ-GDKVTEEtrrFSGGEKAR--LVLALIvwQRPNLLLLDEP 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 529 NTSLDGYSDRALCDLMRSLKGtvSMILVSYRPSLL-ALADQRFSLEDGRLKPLD 581
Cdd:PRK10636 458 TNHLDLDMRQALTEALIDFEG--ALVVVSHDRHLLrSTTDDLYLVHDGKVEPFD 509
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
340-577 |
1.47e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.94 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 340 RDI-DAIPAESRGRFKMDRFTSLDLKNLhfrySPKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGS 418
Cdd:PRK09700 244 RELqNRFNAMKENVSNLAHETVFEVRNV----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 419 ALLNGQ---PPHDFDAesVFNQISYIPQ--RPTLFHG--TILDNLTMFRS-------------DQVEIMQRALELAAKLH 478
Cdd:PRK09700 320 IRLNGKdisPRSPLDA--VKKGMAYITEsrRDNGFFPnfSIAQNMAISRSlkdggykgamglfHEVDEQRTAENQRELLA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 479 LDevfARLPNGYDTEvgdssadlLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL--KGTVSMILV 556
Cdd:PRK09700 398 LK---CHSVNQNITE--------LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLadDGKVILMVS 466
|
250 260
....*....|....*....|.
gi 1733551959 557 SYRPSLLALADQRFSLEDGRL 577
Cdd:PRK09700 467 SELPEIITVCDRIAVFCEGRL 487
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
361-527 |
1.55e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.79 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHfryspkDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQP-----PHDfdaeSVF 435
Cdd:COG1129 257 LEVEGLS------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPvrirsPRD----AIR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 436 NQISYIPQ-RPT--LFHG-TILDNLTMFRSDQVE---IMQRALELAAklhLDEVFARL---PNGYDTEVGDssadlLPAG 505
Cdd:COG1129 327 AGIAYVPEdRKGegLVLDlSIRENITLASLDRLSrggLLDRRRERAL---AEEYIKRLrikTPSPEQPVGN-----LSGG 398
|
170 180
....*....|....*....|..
gi 1733551959 506 VAQRITIVRALINRPSLILFDE 527
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDE 420
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
378-533 |
1.93e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.96 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ----PPHDFDAES------VFnQISYIPQRPTL 447
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdllkADPEAQKLLrqkiqiVF-QNPYGSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 448 FHGTILD-----NLTMFRSDQVEimqRALELAAKLHLD-EVFARLPNgydtevgdssadLLPAGVAQRITIVRALINRPS 521
Cdd:PRK11308 110 KVGQILEeplliNTSLSAAERRE---KALAMMAKVGLRpEHYDRYPH------------MFSGGQRQRIAIARALMLDPD 174
|
170
....*....|..
gi 1733551959 522 LILFDESNTSLD 533
Cdd:PRK11308 175 VVVADEPVSALD 186
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
355-533 |
2.24e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 50.45 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 355 MDRFTSLDLKNLH--FRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKS----TLLNLVAGQIVPTKGSALLNGQPPHD 428
Cdd:COG4172 1 MMSMPLLSVEDLSvaFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 429 FDaESVF-----NQISYIPQRPT-----LFhgTIldnltmfrSDQV-------------EIMQRALELAAKLHLDEVFAR 485
Cdd:COG4172 81 LS-ERELrrirgNRIAMIFQEPMtslnpLH--TI--------GKQIaevlrlhrglsgaAARARALELLERVGIPDPERR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1733551959 486 LpNGYDTEvgdssadlLPAGVAQRITIVRALINRPSLILFDESNTSLD 533
Cdd:COG4172 150 L-DAYPHQ--------LSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
181-307 |
2.64e-06 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 49.43 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 181 LALITgwLVLIPIIMLGIAGF--MAWKIGKSLQEQLEERRewdrrrySFLIEVLSGIHTVKAMAMEAMMLRRYERLLESN 258
Cdd:cd18573 143 LTLVM--LLVVPPIAVGAVFYgrYVRKLSKQVQDALADAT-------KVAEERLSNIRTVRAFAAERKEVERYAKKVDEV 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1733551959 259 AFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGALAA 307
Cdd:cd18573 214 FDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTS 262
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
376-575 |
4.16e-06 |
|
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: 47.62 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 376 EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQ--IVPTKGSALLNGQPPhdfdAESVFNQISYIPQRPTLFhgtil 453
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRktAGVITGEILINGRPL----DKNFQRSTGYVEQQDVHS----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 454 DNLTmfrsdqveiMQRALELaaklhldevfarlpngydtevgdsSADLLPAGVAQR--ITIVRALINRPSLILFDESNTS 531
Cdd:cd03232 92 PNLT---------VREALRF------------------------SALLRGLSVEQRkrLTIGVELAAKPSILFLDEPTSG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1733551959 532 LDGYSDRALCDLMRSLKGTVSMILVS-YRPS--LLALADQRFSLEDG 575
Cdd:cd03232 139 LDSQAAYNIVRFLKKLADSGQAILCTiHQPSasIFEKFDRLLLLKRG 185
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
378-576 |
5.34e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGqIVPT---KGSALLNGQPPHdF----DAESVfnQISYIPQR----PT 446
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVCR-FkdirDSEAL--GIVIIHQElaliPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 447 LfhgTILDNltMF----RS-----DQVEIMQRALELAAKLHLDEVfarlPngyDTEVGDssadlLPAGVAQRITIVRALI 517
Cdd:NF040905 93 L---SIAEN--IFlgneRAkrgviDWNETNRRARELLAKVGLDES----P---DTLVTD-----IGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551959 518 NRPSLILFDESNTSLDGYSDRALCDLMRSLKGT-VSMILVSYR-PSLLALADQRFSLEDGR 576
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKlNEIRRVADSITVLRDGR 216
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
377-443 |
7.00e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 7.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQI--------VPTKGSALLNGQPPHDFDAESVFNQISYIPQ 443
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
363-533 |
8.42e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.16 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLHFRYSPKDP---EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSA--LLNGQPPHDFDAESVFNQ 437
Cdd:PRK13651 5 VKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 438 ISYIPQRPT------------------------LFHGTILDNLtMF--RSDQVEiMQRALELAAKlHLDEVfarlpnGYD 491
Cdd:PRK13651 85 EKLVIQKTRfkkikkikeirrrvgvvfqfaeyqLFEQTIEKDI-IFgpVSMGVS-KEEAKKRAAK-YIELV------GLD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1733551959 492 TEVGDSSADLLPAGVAQRITIVRALINRPSLILFDESNTSLD 533
Cdd:PRK13651 156 ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
380-418 |
1.33e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.01 E-value: 1.33e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1733551959 380 NINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGS 418
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT 378
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
372-554 |
1.46e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 372 PKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGqiVPTkgsallngqpphDFDAESVFNQ---ISYIPQRPTLF 448
Cdd:PRK11819 17 PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--VDK------------EFEGEARPAPgikVGYLPQEPQLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 449 HG-TILDNLTMFRSDQVEIMQRALELAAKL-----HLDEVFARL---------PNGYDTEV-------------GDSSAD 500
Cdd:PRK11819 83 PEkTVRENVEEGVAEVKAALDRFNEIYAAYaepdaDFDALAAEQgelqeiidaADAWDLDSqleiamdalrcppWDAKVT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1733551959 501 LLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMI 554
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAV 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
363-558 |
1.46e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 47.32 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLHFRYSPKDP---EVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ--------------- 424
Cdd:PRK13634 5 FQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitagkknkklkplr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 425 ---------PPHDFDAESVFNQISYIPQrptlfhgtildNLTMFRSDqveimqrALELAAKLhLDEVfarlpnGYDTEVG 495
Cdd:PRK13634 85 kkvgivfqfPEHQLFEETVEKDICFGPM-----------NFGVSEED-------AKQKAREM-IELV------GLPEELL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 496 DSSADLLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL--KGTVSMILVSY 558
Cdd:PRK13634 140 ARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTH 204
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
378-424 |
2.11e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 2.11e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQ 424
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE 86
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
380-468 |
2.19e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 380 NINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLngqpphdfdAESVfnQISYIPQrptlFHGTILDNLTMF 459
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI---------GETV--KLAYVDQ----SRDALDPNKTVW 406
|
90
....*....|.
gi 1733551959 460 R--SDQVEIMQ 468
Cdd:PRK11819 407 EeiSGGLDIIK 417
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
83-319 |
2.23e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 46.71 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 83 LSTLAMLTIGVAialVLDVLLKIARARLSGWAG---------AQYEH------------RAGCIaIKRLaTGDLAHVEST 141
Cdd:cd18550 38 LVLLALGMVAVA---VASALLGVVQTYLSARIGqgvmydlrvQLYAHlqrmslafftrtRTGEI-QSRL-NNDVGGAQSV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 142 PSGMhldrLSSIelirdfyASQASLVLIDLPFILLFLGILALITgwLVLIPIIML--GIAGFMAWKIGKSLQEQLEERRe 219
Cdd:cd18550 113 VTGT----LTSV-------VSNVVTLVATLVAMLALDWRLALLS--LVLLPLFVLptRRVGRRRRKLTREQQEKLAELN- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 220 wdrrrySFLIEVLS--GIHTVKAMAMEAMMLRRYERllESNAFASAQVSQ-ISGHAQTVG-TITSHLTVAAVVGFGSLMV 295
Cdd:cd18550 179 ------SIMQETLSvsGALLVKLFGREDDEAARFAR--RSRELRDLGVRQaLAGRWFFAAlGLFTAIGPALVYWVGGLLV 250
|
250 260
....*....|....*....|....
gi 1733551959 296 INGTLSVGALAASTLLAGRTVQPA 319
Cdd:cd18550 251 IGGGLTIGTLVAFTALLGRLYGPL 274
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
363-533 |
3.37e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.04 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 363 LKNLHFRYspKDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSA-LLNG---QPPHdfdAESVFNQI 438
Cdd:NF033858 4 LEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGdmaDARH---RRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 439 SYIPQ------RPTLfhgTILDNL----TMFRSDQVEIMQRALELAAKLHLDEvFARLPNGYdtevgdssadlLPAGVAQ 508
Cdd:NF033858 79 AYMPQglgknlYPTL---SVFENLdffgRLFGQDAAERRRRIDELLRATGLAP-FADRPAGK-----------LSGGMKQ 143
|
170 180
....*....|....*....|....*
gi 1733551959 509 RITIVRALINRPSLILFDESNTSLD 533
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
367-561 |
3.53e-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: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 367 HFRYSPKDPEV--LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSA----LLNGQPPHD----FDAESVFN 436
Cdd:TIGR00956 64 KLKKFRDTKTFdiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVegviTYDGITPEEikkhYRGDVVYN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 437 QISYIpQRPTLFHGTILDNLTMFRSDQVEIMQRALELAAKlHLDEVFAR---LPNGYDTEVGDSSADLLPAGVAQRITIV 513
Cdd:TIGR00956 144 AETDV-HFPHLTVGETLDFAARCKTPQNRPDGVSREEYAK-HIADVYMAtygLSHTRNTKVGNDFVRGVSGGERKRVSIA 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 514 RALINRPSLILFDESNTSLDGYSD----RALCDLMRSLKGTVSMILvsYRPS 561
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATAlefiRALKTSANILDTTPLVAI--YQCS 271
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
387-524 |
8.24e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 387 QGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLngqpphdFDAESvfnqisyIPQRPTLFHGTILDNLTMFRSDQVEI 466
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGED-------ILEEVLDQLLLIIVGGKKASGSGELR 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733551959 467 MQRALELAAKLH-----LDEVFARLPngydtevgDSSADLLPAGVAQRITIVRALINRPSLIL 524
Cdd:smart00382 67 LRLALALARKLKpdvliLDEITSLLD--------AEQEALLLLLEELRLLLLLKSEKNLTVIL 121
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
366-533 |
9.15e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 366 LHFRYSPkdpeVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGS---------ALLNGQPP-------HDF 429
Cdd:PRK11147 11 LSFSDAP----LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRiiyeqdlivARLQQDPPrnvegtvYDF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 430 DAESVFNQISYIPQrptlFHgTILDNLTMFRSD----QVEIMQRALELAAKLHLD----EVFARLpnGYDtevGDSSADL 501
Cdd:PRK11147 87 VAEGIEEQAEYLKR----YH-DISHLVETDPSEknlnELAKLQEQLDHHNLWQLEnrinEVLAQL--GLD---PDAALSS 156
|
170 180 190
....*....|....*....|....*....|..
gi 1733551959 502 LPAGVAQRITIVRALINRPSLILFDESNTSLD 533
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
164-331 |
9.15e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 44.83 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 164 ASLVLIDLPFILLFLG-ILALITgwLVLIPIIMLGiagfmAWKIGKSLQEQLEERREWDRRRYSFLIEVLSGIHTVKAMA 242
Cdd:cd18778 124 NVLTLVGVAIILFSINpKLALLT--LIPIPFLALG-----AWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 243 MEAMMLRRYERLLESNAFASAQVSQISGHAQ-TVGTITSHLTVAaVVGFGSLMVINGTLSVGALAASTLLAGRTVQPALR 321
Cdd:cd18778 197 REEEEAKRFEALSRRYRKAQLRAMKLWAIFHpLMEFLTSLGTVL-VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITS 275
|
170
....*....|
gi 1733551959 322 ALGLWSRFQS 331
Cdd:cd18778 276 LHGLNEMLQR 285
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
361-555 |
1.04e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLH--FRYSPKDPEVLHNINLRLEQGQIIGITGKNGVGKS-TLLN----LVAGQIVPTKGSALLNGQPPHDFDAES 433
Cdd:PRK15134 6 LAIENLSvaFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSilrlLPSPPVVYPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 434 VF----NQISYIPQRPTL-----------------FH---------GTILDNLtmfrsDQVEIMQRALELAAKLHLdevf 483
Cdd:PRK15134 86 LRgvrgNKIAMIFQEPMVslnplhtlekqlyevlsLHrgmrreaarGEILNCL-----DRVGIRQAAKRLTDYPHQ---- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 484 arlpngydtevgdssadlLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSLKGTVSMIL 555
Cdd:PRK15134 157 ------------------LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGL 210
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
385-533 |
1.39e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 43.77 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 385 LEQGQIIGITGKNGVGKSTLLNLVAGqIVPTKGSALLNGQPPHDFDAESVFNQISYIPQR-PTLFHGTILDNLTMFRSDQ 463
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTLHQPDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 464 VEI--MQRAL-ELAAKLHLDEVFARlpngydtevgdsSADLLPAGVAQRITIVRAL------INRPS-LILFDESNTSLD 533
Cdd:PRK03695 98 TRTeaVASALnEVAEALGLDDKLGR------------SVNQLSGGEWQRVRLAAVVlqvwpdINPAGqLLLLDEPMNSLD 165
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
370-585 |
1.50e-04 |
|
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: 44.82 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 370 YSPKDPEV--LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGqIVPTK--GSALLNGQPPHDFD-AESVFNQISYIPQR 444
Cdd:TIGR02633 266 WDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKfeGNVFINGKPVDIRNpAQAIRAGIAMVPED 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 445 PTLfHGTILD-----NLTMFRSDQVEIMQRALELAAKLHLDEVFARLpngydtEVGDSSADL----LPAGVAQRITIVRA 515
Cdd:TIGR02633 345 RKR-HGIVPIlgvgkNITLSVLKSFCFKMRIDAAAELQIIGSAIQRL------KVKTASPFLpigrLSGGNQQKAVLAKM 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733551959 516 LINRPSLILFDESNTSLDGYSDRALCDLMRSL-KGTVSMILVSYR-PSLLALADQRFSLEDGRLKPlDFADH 585
Cdd:TIGR02633 418 LLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSElAEVLGLSDRVLVIGEGKLKG-DFVNH 488
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
172-307 |
2.89e-04 |
|
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: 43.16 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 172 PFILLFLGILALITGW------LVLIPIIMLGIAGFMAW-------------KIGKSLQEQLeerrewdrrrysflievl 232
Cdd:cd18548 124 PIMLIGAIIMAFRINPklalilLVAIPILALVVFLIMKKaiplfkkvqkkldRLNRVVRENL------------------ 185
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551959 233 SGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGALAA 307
Cdd:cd18548 186 TGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVA 260
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
385-426 |
5.38e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.40 E-value: 5.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1733551959 385 LEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPP 426
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP 63
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
134-325 |
5.52e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 42.15 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 134 DLAHVESTPSGMHLDRLSSIelIRDFYASQASLVLIDLPFILLFLGI---LALI----TGWLVLI-PIIMLGIAGFMAW- 204
Cdd:cd18574 89 DIAFFDTHRTGELVNRLTAD--VQEFKSSFKQCVSQGLRSVTQTVGCvvsLYLIspklTLLLLVIvPVVVLVGTLYGSFl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 205 -KIGKSLQEQLEERREWDRrrysfliEVLSGIHTVKAMAMEAMMLRRYERLLEsnafASAQVSQISGHAQTVGTITSHLT 283
Cdd:cd18574 167 rKLSRRAQAQVAKATGVAD-------EALGNIRTVRAFAMEDRELELYEEEVE----KAAKLNEKLGLGIGIFQGLSNLA 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1733551959 284 ----VAAVVGFGSLMVINGTLSVGALaASTLLAGRTVQPALRALGL 325
Cdd:cd18574 236 lngiVLGVLYYGGSLVSRGELTAGDL-MSFLVATQTIQRSLAQLSV 280
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
377-558 |
6.14e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 377 VLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLngqpPHDFDAESVfNQISYIPQRPTLFHgtILDNL 456
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF----PGNWQLAWV-NQETPALPQPALEY--VIDGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 457 TMFRSDQVEiMQRALE-----LAAKLH--LDEVFA--------RLPN--GYDTEVGDSSADLLPAGVAQRITIVRALINR 519
Cdd:PRK10636 89 REYRQLEAQ-LHDANErndghAIATIHgkLDAIDAwtirsraaSLLHglGFSNEQLERPVSDFSGGWRMRLNLAQALICR 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 1733551959 520 PSLILFDESNTSLDGYSDRALCDLMRSLKGTvsMILVSY 558
Cdd:PRK10636 168 SDLLLLDEPTNHLDLDAVIWLEKWLKSYQGT--LILISH 204
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
362-410 |
7.71e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 7.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1733551959 362 DLKNLHFRYSpkDPEVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAG 410
Cdd:PRK10938 262 VLNNGVVSYN--DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
378-460 |
8.06e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 378 LHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALLNGQPPhDFDA--ESVFNQISYIPQRPTLF-HGTILD 454
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSskEALENGISMVHQELNLVlQRSVMD 92
|
....*.
gi 1733551959 455 NLTMFR 460
Cdd:PRK10982 93 NMWLGR 98
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
353-585 |
9.54e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 353 FKMDRFTSLDLKNLHFRyspkdpeVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGqIVPTK--GSALLNGQP----- 425
Cdd:PRK13549 260 LEVRNLTAWDPVNPHIK-------RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGKPvkirn 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 426 PHDfdaeSVFNQISYIPQ-RPTlfHGTILD-----NLTMFRSDQVEIMQRaLELAAKLH-LDEVFARLpngydtEVGDSS 498
Cdd:PRK13549 332 PQQ----AIAQGIAMVPEdRKR--DGIVPVmgvgkNITLAALDRFTGGSR-IDDAAELKtILESIQRL------KVKTAS 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 499 ADL----LPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDRALCDLMRSL-KGTVSMILVSYR-PSLLALADQRFSL 572
Cdd:PRK13549 399 PELaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSElPEVLGLSDRVLVM 478
|
250
....*....|...
gi 1733551959 573 EDGRLKPlDFADH 585
Cdd:PRK13549 479 HEGKLKG-DLINH 490
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
179-318 |
1.28e-03 |
|
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: 41.40 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 179 GILALITGWLVLIPIIMLGIAGFMAWKIGKSLQEQLEERREWDRRRYSFLIEVLSGIHTVKAMAMEAMMLRRYERllESN 258
Cdd:cd18565 147 AILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVAD--ASE 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1733551959 259 AFASAQVSQI---SGHAQTVGTITShLTVAAVVGFGSLMVING------TLSVGALAASTLLAGRTVQP 318
Cdd:cd18565 225 EYRDANWRAIrlrAAFFPVIRLVAG-AGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRLLWP 292
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
362-418 |
1.84e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.09 E-value: 1.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551959 362 DLKNLHFRYSPKDpeVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGS 418
Cdd:PRK11147 321 EMENVNYQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGR 375
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
462-577 |
2.51e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 462 DQVEIMQRALELA---AKLHLDEVFARLPNgydTEVGDSSADLLPAGVAQRITIVRALINRPSLILFDESNTSLDGYSDR 538
Cdd:NF000106 105 ENLYMIGR*LDLSrkdARARADELLERFSL---TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN 181
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1733551959 539 ALCDLMRSL--KGTVSMILVSYRPSLLALADQRFSLEDGRL 577
Cdd:NF000106 182 EVWDEVRSMvrDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
230-329 |
3.80e-03 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 39.54 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 230 EVLSGIHTVKAMAMEAMMLRRYERLLESNAFASAQVSQISGHAQTVGTITSHLTVAAVVGFGSLMVINGTLSVGALaAST 309
Cdd:cd18780 186 ESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLL-TSF 264
|
90 100
....*....|....*....|.
gi 1733551959 310 LLAGRTVQPALRAL-GLWSRF 329
Cdd:cd18780 265 LLYTLTVAMSFAFLsSLYGDF 285
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
361-533 |
5.26e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 361 LDLKNLHFRYSPKdpeVLHNINLRLEQGQIIGITGKNGVGKSTLLNLVAGQIVPTKGSALL------NGQPPHdfdaesv 434
Cdd:PRK13541 2 LSLHQLQFNIEQK---NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYkncninNIAKPY------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 435 fnqISYIPQRPTL-FHGTILDNLTMFRsdqvEIMQRALELAAKLHldevFARLpngydTEVGDSSADLLPAGVAQRITIV 513
Cdd:PRK13541 72 ---CTYIGHNLGLkLEMTVFENLKFWS----EIYNSAETLYAAIH----YFKL-----HDLLDEKCYSLSSGMQKIVAIA 135
|
170 180
....*....|....*....|
gi 1733551959 514 RALINRPSLILFDESNTSLD 533
Cdd:PRK13541 136 RLIACQSDLWLLDEVETNLS 155
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
153-307 |
5.87e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 38.94 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551959 153 IELIRDFYASQASLVLIDLPFILLFLGILALITGWLVLIPIIMLGIAGFMAWKIGKSLQEQLEERREWDRRRYSFLIEVL 232
Cdd:cd18554 113 VEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERI 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1733551959 233 SGIHTVKAMAMEAMMLRRYERllESNAFASAQVSQISGHAQT---VGTITShLTVAAVVGFGSLMVINGTLSVGALAA 307
Cdd:cd18554 193 QGMSVIKSFALEKHEQKQFDK--RNGHFLTRALKHTRWNAKTfsaVNTITD-LAPLLVIGFAAYLVIEGNLTVGTLVA 267
|
|
| |
