|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-571 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 572.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 1 MKRENP-LFFLFKKLSWPV-GLIVAAITISSLGSLSGLLVPLFTGRIVDKF----SVSHInWNLIALFGGIFVINALLSG 74
Cdd:COG1132 1 MSKSPRkLLRRLLRYLRPYrGLLILALLLLLLSALLELLLPLLLGRIIDALlaggDLSAL-LLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 75 LGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFIL 154
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 155 DWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLK 234
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 235 QAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRIYEIMQ 314
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 315 EPIEPTEAlEDSENVLIDDGVLSFEHVDFKYDV-KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIK 393
Cdd:COG1132 320 EPPEIPDP-PGAVPLPPVRGEIEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 394 YGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKL 473
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYG-RPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 474 SGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGT 553
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570
....*....|....*...
gi 616431502 554 HSELMASHAKYKNFVVSQ 571
Cdd:COG1132 558 HEELLARGGLYARLYRLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
38-571 |
1.67e-148 |
|
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: 444.28 E-value: 1.67e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSVSHIN---WNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQ 114
Cdd:COG2274 175 TPLFTQVVIDRVLPNQDLstlWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 115 LMSRLTDdTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANF 194
Cdd:COG2274 255 LASRFRD-VESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKR 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 195 SGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGT 274
Cdd:COG2274 334 QSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQ 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 275 LIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRIYEIMQEPIEPTEALEDSENVLIDdGVLSFEHVDFKY--DVKKILD 352
Cdd:COG2274 414 LIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLK-GDIELENVSFRYpgDSPPVLD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 353 DVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNILYG 432
Cdd:COG2274 493 NISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLG 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 433 iNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQ 512
Cdd:COG2274 573 -DPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL 651
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 513 EALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHAKYKNFVVSQ 571
Cdd:COG2274 652 ENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
2-571 |
1.82e-130 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 393.30 E-value: 1.82e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 2 KRENPLFFLFKKLSWPVGLIVAAITISSLGSLSGLLVPLFTGRIVDK-FSVSHINW--NLIALFGGIFVINALLSGLGLY 78
Cdd:TIGR02204 1 KRLRPLAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHgFSKDSSGLlnRYFAFLLVVALVLALGTAARFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 79 LLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKM 158
Cdd:TIGR02204 81 LVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 159 TLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKI 238
Cdd:TIGR02204 161 TSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 239 AAVVQPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRIYEIMQEpiE 318
Cdd:TIGR02204 241 RALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQA--E 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 319 PTEALEDSENVLIDD--GVLSFEHVDFKYDVK---KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIK 393
Cdd:TIGR02204 319 PDIKAPAHPKTLPVPlrGEIEFEQVNFAYPARpdqPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 394 YGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKL 473
Cdd:TIGR02204 399 LDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG-RPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 474 SGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGT 553
Cdd:TIGR02204 478 SGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGT 557
|
570
....*....|....*...
gi 616431502 554 HSELMASHAKYKNFVVSQ 571
Cdd:TIGR02204 558 HAELIAKGGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
53-564 |
4.29e-113 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 348.63 E-value: 4.29e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 53 HINWNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQ 132
Cdd:TIGR02203 51 SVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 133 KLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKIStstqSEIANFSGLLGRVLTEM----RLV 208
Cdd:TIGR02203 131 AFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRIS----KEIQNSMGQVTTVAEETlqgyRVV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 209 KISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMP 288
Cdd:TIGR02203 207 KLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 289 LINLSTLVTDYKKAVGASSRIYEIMQEPIEP---TEALEDSEnvliddGVLSFEHVDFKY--DVKKILDDVSFQIPQGQV 363
Cdd:TIGR02203 287 LKSLTNVNAPMQRGLAAAESLFTLLDSPPEKdtgTRAIERAR------GDVEFRNVTFRYpgRDRPALDSISLVIEPGET 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 364 SAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNILYGINRHVSDEELI 443
Cdd:TIGR02203 361 VALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 444 NYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRT 523
Cdd:TIGR02203 441 RALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRT 520
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 616431502 524 TIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHAKY 564
Cdd:TIGR02203 521 TLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-568 |
3.90e-110 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 345.17 E-value: 3.90e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 2 KRENPLFFLFK--KLSWPvgLIVAAITISSLGSLSGLLVPLFTGRIVD----KFSVShinwnliALFGGIFVINALLSGL 75
Cdd:TIGR00958 144 ETADLLFRLLGlsGRDWP--WLISAFVFLTLSSLGEMFIPFYTGRVIDtlggDKGPP-------ALASAIFFMCLLSIAS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 76 GLYLLSKIG------EKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLI 149
Cdd:TIGR00958 215 SVSAGLRGGsfnytmARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 150 MLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIY 229
Cdd:TIGR00958 295 FMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 230 KLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:TIGR00958 375 QLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKV 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 310 YEIM-QEP-IEPTEALEDSEnvliDDGVLSFEHVDFKYDV---KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERM 384
Cdd:TIGR00958 455 FEYLdRKPnIPLTGTLAPLN----LEGLIEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 385 YEIESGDIkygleSVYDIPLSKW-----RRKIGYVMQSNSMMSGTIRDNILYGINRhVSDEELINYAKLANCHDFIMQFD 459
Cdd:TIGR00958 531 YQPTGGQV-----LLDGVPLVQYdhhylHRQVALVGQEPVLFSGSVRENIAYGLTD-TPDEEIMAAAKAANAHDFIMEFP 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 460 EGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALEtlMEGRTTIVIAHRLSTIKKAGQ 539
Cdd:TIGR00958 605 NGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQ 682
|
570 580
....*....|....*....|....*....
gi 616431502 540 IIFLDKGQVTGKGTHSELMASHAKYKNFV 568
Cdd:TIGR00958 683 ILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
40-561 |
1.92e-105 |
|
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: 328.26 E-value: 1.92e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 40 LFTGRIVDKFSVSHInWNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRL 119
Cdd:COG4988 43 LLAGLIIGGAPLSAL-LPLLGLLLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 120 TDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSG-LL 198
Cdd:COG4988 122 TEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGhFL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 199 GRV--LTEMRLvkisnterleLDNAHKNLNEIYKLG-------LKQAKIAAvvqpISGIVM----LLTIAIILGFGALEI 265
Cdd:COG4988 202 DRLrgLTTLKL----------FGRAKAEAERIAEASedfrkrtMKVLRVAF----LSSAVLeffaSLSIALVAVYIGFRL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 266 ATGAITAGT-----LIAMIFYviqlsMPLINLSTLVTDYKKAVGASSRIYEIMQEPIEPTEALEDSENVLiDDGVLSFEH 340
Cdd:COG4988 268 LGGSLTLFAalfvlLLAPEFF-----LPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAA-GPPSIELED 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 341 VDFKYDV-KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNS 419
Cdd:COG4988 342 VSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPY 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 420 MMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEA 499
Cdd:COG4988 422 LFAGTIRENLRLG-RPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEP 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616431502 500 TANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASH 561
Cdd:COG4988 501 TAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
38-309 |
2.66e-103 |
|
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: 313.22 E-value: 2.66e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSVSHINWNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMS 117
Cdd:cd18551 18 QPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 118 RLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGL 197
Cdd:cd18551 98 RVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 198 LGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGTLIA 277
Cdd:cd18551 178 LERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVA 257
|
250 260 270
....*....|....*....|....*....|..
gi 616431502 278 MIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18551 258 FLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
336-566 |
3.24e-103 |
|
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: 311.09 E-value: 3.24e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGY 413
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 414 VMQSNSMMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDI 493
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616431502 494 LLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHAKYKN 566
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
338-571 |
9.83e-103 |
|
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: 309.86 E-value: 9.83e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 338 FEHVDFKYDVK---KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYV 414
Cdd:cd03249 3 FKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSGTIRDNILYGINRhVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDIL 494
Cdd:cd03249 83 SQEPVLFDGTIAENIRYGKPD-ATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 495 LLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHAKYKNFVVSQ 571
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
123-564 |
1.75e-98 |
|
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: 311.37 E-value: 1.75e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 123 TKVINEFISQKLPNLLPSIVTLVGSLIMLFIL-DWKMTLLTFITIPIFVLIM-------IPLGRIMQKISTSTQSEIA-- 192
Cdd:COG5265 145 TKGIEFLLRFLLFNILPTLLEIALVAGILLVKyDWWFALITLVTVVLYIAFTvvvtewrTKFRREMNEADSEANTRAVds 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 193 --NFSgllgrvlTemrlVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAI 270
Cdd:COG5265 225 llNYE-------T----VKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTM 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 271 TAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRIYEIMQEPIEPTEAlEDSENVLIDDGVLSFEHVDFKYDVK-K 349
Cdd:COG5265 294 TVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADA-PDAPPLVVGGGEVRFENVSFGYDPErP 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 350 ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNI 429
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 430 LYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESEL 509
Cdd:COG5265 453 AYG-RPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTER 531
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 510 KIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHAKY 564
Cdd:COG5265 532 AIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLY 586
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
86-567 |
8.73e-96 |
|
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: 303.61 E-value: 8.73e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 86 KIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFIsqkLPNLLPSIVTLVGSLIMLFIL---DWKMTLLT 162
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLaffSPALALVL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 163 FITIpIFVLIMIPLgrIMQKISTSTQSEIANFSGLLGRVLTE----MRLVKISNTE---RLELDNAHKNLNeiyKLGLKQ 235
Cdd:COG4987 162 ALGL-LLAGLLLPL--LAARLGRRAGRRLAAARAALRARLTDllqgAAELAAYGALdraLARLDAAEARLA---AAQRRL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 236 AKIAAVVQPISGIVMLLTIAIILGFGALEIATGAItAGTLIAMIFYVIqLSM--PLINLSTLVTDYKKAVGASSRIYEIM 313
Cdd:COG4987 236 ARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGAL-SGPLLALLVLAA-LALfeALAPLPAAAQHLGRVRAAARRLNELL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 314 QEPiePTEALEDSENVLIDDGVLSFEHVDFKYD--VKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGD 391
Cdd:COG4987 314 DAP--PAVTEPAEPAPAPGGPSLELEDVSFRYPgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 392 IKYGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGL 471
Cdd:COG4987 392 ITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLA-RPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGR 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 472 KLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGK 551
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQ 550
|
490
....*....|....*.
gi 616431502 552 GTHSELMASHAKYKNF 567
Cdd:COG4987 551 GTHEELLAQNGRYRQL 566
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
336-565 |
1.62e-95 |
|
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: 291.44 E-value: 1.62e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDV-KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYV 414
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDIL 494
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616431502 495 LLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHAKYK 565
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYA 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
86-565 |
5.51e-94 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 299.24 E-value: 5.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 86 KIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFIT 165
Cdd:PRK11176 95 KVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 166 IPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPI 245
Cdd:PRK11176 175 APIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 246 SGIVMLLTIAIILGFGALEIATGAITAGTlIAMIF-YVIQLSMPLINLSTLVTDYKKAVGASSRIYEIMQEPIEPTEALE 324
Cdd:PRK11176 255 IQLIASLALAFVLYAASFPSVMDTLTAGT-ITVVFsSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKR 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 325 DSENVlidDGVLSFEHVDFKYDVKKI--LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDI 402
Cdd:PRK11176 334 VIERA---KGDIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 403 PLSKWRRKIGYVMQSNSMMSGTIRDNILYGINRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRID 482
Cdd:PRK11176 411 TLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIA 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 483 IARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHA 562
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNG 570
|
...
gi 616431502 563 KYK 565
Cdd:PRK11176 571 VYA 573
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
334-561 |
3.09e-88 |
|
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: 272.18 E-value: 3.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 334 GVLSFEHVDFKYDVKK-ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIG 412
Cdd:cd03254 1 GEIEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 413 YVMQSNSMMSGTIRDNILYGINRhVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPD 492
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPN-ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 493 ILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASH 561
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
95-564 |
1.79e-87 |
|
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: 285.10 E-value: 1.79e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 95 LWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDwKMTLLTFITIPIFVLIMI 174
Cdd:TIGR01846 218 LYRHLLGLPLGYFESRRVGDTVARVRELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSP-TLTGVVIGSLVCYALLSV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 175 PLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTI 254
Cdd:TIGR01846 297 FVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTF 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 255 AIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRIYEIMQEPIEPTEALEDSENVLidDG 334
Cdd:TIGR01846 377 AILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGLAALPEL--RG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkygLESVYDIPLSK--W-RR 409
Cdd:TIGR01846 455 AITFENIRFRYapDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQV---LVDGVDLAIADpaWlRR 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 410 KIGYVMQSNSMMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVK 489
Cdd:TIGR01846 532 QMGVVLQENVLFSRSIRDNIALC-NPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVG 610
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 490 NPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHAKY 564
Cdd:TIGR01846 611 NPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLY 685
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-560 |
1.16e-80 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 264.52 E-value: 1.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 12 KKLSWPV---GLIVAAITISSlgslsgllvPLFTGRIVDKFSVSHINWNLIALFGGIFVINALLSGLGLYLLSKIGEKII 88
Cdd:PRK13657 18 KRLGILLavaNVLLAAATFAE---------PILFGRIIDAISGKGDIFPLLAAWAGFGLFNIIAGVLVARHADRLAHRRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 89 YAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVIN----EFISQKLPNLLpSIVTLVGsliMLFILDWKMTLLTFI 164
Cdd:PRK13657 89 LAVLTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFglwlEFMREHLATLV-ALVVLLP---LALFMNWRLSLVLVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 165 TIPIFVLImiplGRIMQKISTSTQSEI-ANFSGLLGRV---LTEMRLVKISNTERLELDNAHKNLNEIYKLG---LKQAK 237
Cdd:PRK13657 165 LGIVYTLI----TTLVMRKTKDGQAAVeEHYHDLFAHVsdaIGNVSVVQSYNRIEAETQALRDIADNLLAAQmpvLSWWA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 238 IAAVVQPISGIvmlLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTdykKAVGASSRIYEIMqEPI 317
Cdd:PRK13657 241 LASVLNRAAST---ITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFIN---QVFMAAPKLEEFF-EVE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 318 EPTEALEDSENvLID----DGVLSFEHVDFKYDVKK-ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDI 392
Cdd:PRK13657 314 DAVPDVRDPPG-AIDlgrvKGAVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 393 KYGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLK 472
Cdd:PRK13657 393 LIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVG-RPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQ 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 473 LSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKG 552
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESG 551
|
....*...
gi 616431502 553 THSELMAS 560
Cdd:PRK13657 552 SFDELVAR 559
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
336-571 |
8.71e-80 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 250.87 E-value: 8.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkygLESVYDIPL--SKW-RRK 410
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV---LVDGHDLALadPAWlRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 411 IGYVMQSNSMMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKN 490
Cdd:cd03252 78 VGVVLQENVLFNRSIRDNIALA-DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 491 PDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHAKYKNFVVS 570
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 616431502 571 Q 571
Cdd:cd03252 237 Q 237
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
86-564 |
2.14e-78 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 261.42 E-value: 2.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 86 KIIYAIRS---VLWeHIIQLKMPFFDKNESGQLMSRLTDDTKViNEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLT 162
Cdd:TIGR03796 222 EIKLAVGMsarFLW-HILRLPVRFFAQRHAGDIASRVQLNDQV-AEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIG 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 163 FITIPIFVLIMIplgRIMQKISTSTQSEIANFSGLLGRVLTEMRL---VKISNTErlelDNAH--------KNLNEIYKL 231
Cdd:TIGR03796 300 IAFAAINVLALQ---LVSRRRVDANRRLQQDAGKLTGVAISGLQSietLKASGLE----SDFFsrwagyqaKLLNAQQEL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 232 GLKQAKIAAVVQpisgIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRIYE 311
Cdd:TIGR03796 373 GVLTQILGVLPT----LLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDD 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 312 IMQEPIEPteALEDSENVLIDD-------GVLSFEHVDFKYDV--KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIE 382
Cdd:TIGR03796 449 VLRNPVDP--LLEEPEGSAATSepprrlsGYVELRNITFGYSPlePPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVA 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 383 RMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNI-LYgiNRHVSDEELINYAKLANCHDFIMQFDEG 461
Cdd:TIGR03796 527 GLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLtLW--DPTIPDADLVRACKDAAIHDVITSRPGG 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 462 YDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETlmEGRTTIVIAHRLSTIKKAGQII 541
Cdd:TIGR03796 605 YDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEII 682
|
490 500
....*....|....*....|...
gi 616431502 542 FLDKGQVTGKGTHSELMASHAKY 564
Cdd:TIGR03796 683 VLERGKVVQRGTHEELWAVGGAY 705
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
56-543 |
2.54e-72 |
|
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: 240.65 E-value: 2.54e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 56 WNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLP 135
Cdd:TIGR02857 44 LPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 136 NL-LPSIVTLVgSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSG-LLGRV--LTEMRLVKIS 211
Cdd:TIGR02857 124 QLvLAVIVPLA-ILAAVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGhFLDRLrgLPTLKLFGRA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 212 NTERLELDNAHKNLNEIYKLGLKQAKI-AAVVQPISGIVMLLtIAIILGF----GALEIATGAITagTLIAMIFYviqls 286
Cdd:TIGR02857 203 KAQAAAIRRSSEEYRERTMRVLRIAFLsSAVLELFATLSVAL-VAVYIGFrllaGDLDLATGLFV--LLLAPEFY----- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 287 MPLINLSTLVTDYKKAVGASSRIYEIMQEPIEPTEALEDSENVliDDGVLSFEHVDFKY-DVKKILDDVSFQIPQGQVSA 365
Cdd:TIGR02857 275 LPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAA--PASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 366 FVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNILYGiNRHVSDEELINY 445
Cdd:TIGR02857 353 LVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLA-RPDASDAEIREA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 446 AKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTI 525
Cdd:TIGR02857 432 LERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVL 511
|
490
....*....|....*...
gi 616431502 526 VIAHRLSTIKKAGQIIFL 543
Cdd:TIGR02857 512 LVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
336-547 |
1.12e-70 |
|
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: 224.57 E-value: 1.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYD--VKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGY 413
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 414 VMQSNSMMSGTIRDNILyginrhvsdeelinyaklanchdfimqfdegydtlvgerglklSGGQRQRIDIARSFVKNPDI 493
Cdd:cd03228 81 VPQDPFLFSGTIRENIL-------------------------------------------SGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 616431502 494 LLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQ 547
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
102-564 |
2.98e-70 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 236.92 E-value: 2.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 102 LKMPF--FDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIplgrI 179
Cdd:PRK10790 109 LRQPLsaFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMV----I 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 180 MQKIST----STQSEIANFSGLLGRVLTEMRLVK-----ISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVM 250
Cdd:PRK10790 185 YQRYSTpivrRVRAYLADINDGFNEVINGMSVIQqfrqqARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSALIL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 251 --LLtiaIILGFGAleiaTGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRIYEIMQEPIEPTealeDSEN 328
Cdd:PRK10790 265 cgLL---MLFGFSA----SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQY----GNDD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 329 VLIDDGVLSFEHVDFKY-DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKW 407
Cdd:PRK10790 334 RPLQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 408 RRKIGYVMQSNSMMSGTIRDNILYGinRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSF 487
Cdd:PRK10790 414 RQGVAMVQQDPVVLADTFLANVTLG--RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVL 491
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 488 VKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHAKY 564
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
333-548 |
9.63e-66 |
|
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: 213.87 E-value: 9.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 333 DGVLSFEHVDFKYDVK---KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRR 409
Cdd:cd03248 9 KGIVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 410 KIGYVMQSNSMMSGTIRDNILYGINRhVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVK 489
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQS-CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 490 NPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQV 548
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
106-573 |
5.60e-65 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 222.28 E-value: 5.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 106 FFDKNESGQLMSRLTDDT-KVIneFISQKlpnllpSIVTLVGSLIM----LFI----LDWKMTLLTFITIPIFVLIMIPL 176
Cdd:PRK10789 86 FYLRHRTGDLMARATNDVdRVV--FAAGE------GVLTLVDSLVMgcavLIVmstqISWQLTLLALLPMPVMAIMIKRY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 177 GRIMQKISTSTQseiANFSGLLGRV---LTEMRLVKISNTERLE--------LDNAHKNLneiyklglKQAKIAAVVQPI 245
Cdd:PRK10789 158 GDQLHERFKLAQ---AAFSSLNDRTqesLTSIRMIKAFGLEDRQsalfaadaEDTGKKNM--------RVARIDARFDPT 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 246 SGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRIYEIMQEPieptEALED 325
Cdd:PRK10789 227 IYIAIGMANLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEA----PVVKD 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 326 -SENVLIDDGVLSFEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDI 402
Cdd:PRK10789 303 gSEPVPEGRGELDVNIRQFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 403 PLSKWRRKIGYVMQSNSMMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRID 482
Cdd:PRK10789 383 QLDSWRSRLAVVSQTPFLFSDTVANNIALG-RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRIS 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 483 IARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHA 562
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
490
....*....|.
gi 616431502 563 KYKNFVVSQKL 573
Cdd:PRK10789 542 WYRDMYRYQQL 552
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
89-571 |
6.40e-65 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 224.84 E-value: 6.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 89 YAIRSVLWEHIIQLKMPFFDKNESGQLMSRlTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPI 168
Cdd:TIGR03797 209 ASLQAAVWDRLLRLPVSFFRQYSTGDLASR-AMGISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALVAVALALV 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 169 FVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGI 248
Cdd:TIGR03797 288 AIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAV 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 249 VMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRIYEIMQEPIEPTEALedsen 328
Cdd:TIGR03797 368 LPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPEVDEAK----- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 329 vlIDDGVLS----FEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDI 402
Cdd:TIGR03797 443 --TDPGKLSgaieVDRVTFRYrpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 403 PLSKWRRKIGYVMQSNSMMSGTIRDNILYGInrHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRID 482
Cdd:TIGR03797 521 DVQAVRRQLGVVLQNGRLMSGSIFENIAGGA--PLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLL 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 483 IARSFVKNPDILLLDEATANLDSESELKIQEALETLmeGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHA 562
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREG 676
|
....*....
gi 616431502 563 KYKNFVVSQ 571
Cdd:TIGR03797 677 LFAQLARRQ 685
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
98-565 |
2.69e-64 |
|
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: 223.46 E-value: 2.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 98 HIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLP-SIVTLVGslIMLFILDWKMTLLTFITIPIFVLIMIPL 176
Cdd:TIGR01193 238 HLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDmWILVIVG--LFLVRQNMLLFLLSLLSIPVYAVIIILF 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 177 GRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAI 256
Cdd:TIGR01193 316 KRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVV 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 257 ILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRIYEIMQEPIEPTEALEDSENVLIDdGVL 336
Cdd:TIGR01193 396 ILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLN-GDI 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 337 SFEHVDFKYDV-KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVM 415
Cdd:TIGR01193 475 VINDVSYSYGYgSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLP 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSMMSGTIRDNILYGINRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILL 495
Cdd:TIGR01193 555 QEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLI 634
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 496 LDEATANLDSESELKIQEALETLMEgRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHAKYK 565
Cdd:TIGR01193 635 LDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYA 703
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
16-564 |
3.03e-61 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 212.83 E-value: 3.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 16 WPVGLIV------AAITISSlgslsgllvPLFTGRIVDKFSVSHINWNLIALFGGIFVINALLSGLGLYLLSKIGEKIIY 89
Cdd:TIGR01192 19 NRVLLIVianitlAAITIAE---------PILFGRIIDAISSKSDVLPTLALWAGFGVFNTIAYVLVAREADRLAHGRRA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 90 AIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVIN----EFISQKLPnllpSIVTLVGSLIMLFILDWKMTLLTFIT 165
Cdd:TIGR01192 90 TLLTEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFglwlEFMRQHLA----TFVALFLLIPTAFAMDWRLSIVLMVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 166 IPIFVLImiplGR-IMQKISTSTQSEIANFSGLLGRV---LTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAV 241
Cdd:TIGR01192 166 GILYILI----AKlVMQRTKNGQAAVEHHYHNVFKHVsdsISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVLDWWAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 242 VQPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTdykKAVGASSRIYE--IMQEPIEP 319
Cdd:TIGR01192 242 ASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFIT---QIFEARAKLEDffDLEDSVFQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 320 TEALEDSENVLIDDGVLSFEHVDFKY-DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLES 398
Cdd:TIGR01192 319 REEPADAPELPNVKGAVEFRHITFEFaNSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGID 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 399 VYDIPLSKWRRKIGYVMQSNSMMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQR 478
Cdd:TIGR01192 399 INTVTRESLRKSIATVFQDAGLFNRSIRENIRLG-REGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGER 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 479 QRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELM 558
Cdd:TIGR01192 478 QRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELI 557
|
....*.
gi 616431502 559 ASHAKY 564
Cdd:TIGR01192 558 QKDGRF 563
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
38-309 |
7.27e-61 |
|
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: 203.17 E-value: 7.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSVS---HINWNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQ 114
Cdd:cd07346 18 LPLLTKLLIDDVIPAgdlSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 115 LMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANF 194
Cdd:cd07346 98 LMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 195 SGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGT 274
Cdd:cd07346 178 SAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGE 257
|
250 260 270
....*....|....*....|....*....|....*
gi 616431502 275 LIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd07346 258 LVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
38-309 |
2.17e-60 |
|
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: 201.94 E-value: 2.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSVSHINWNL---IALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQ 114
Cdd:cd18576 15 FPLLAGQLIDAALGGGDTASLnqiALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 115 LMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANF 194
Cdd:cd18576 95 LTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 195 SGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGT 274
Cdd:cd18576 175 NTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGD 254
|
250 260 270
....*....|....*....|....*....|....*
gi 616431502 275 LIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18576 255 LVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
334-552 |
2.97e-60 |
|
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: 198.97 E-value: 2.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 334 GVLSFEHVDFKYDVKKI--LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKI 411
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 412 GYVMQSNSMMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNP 491
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLG-APLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616431502 492 DILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKG 552
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
254-567 |
9.71e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 200.46 E-value: 9.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 254 IAIILGFGAL-EIATGAITAG-TLIAMIFYVI---QLSMPLINLSTLVTDYKKAVGASSRIYEIMQEPIEPTEaleDSEN 328
Cdd:PRK11174 264 VAVYFGFSYLgELNFGHYGTGvTLFAGFFVLIlapEFYQPLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQ---QGEK 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 329 VLIDDGVLSFEHVD---FKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIermyeieSGDIKY-------GLEs 398
Cdd:PRK11174 341 ELASNDPVTIEAEDleiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL-------LGFLPYqgslkinGIE- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 399 VYDIPLSKWRRKIGYVMQSNSMMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQR 478
Cdd:PRK11174 413 LRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG-NPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQA 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 479 QRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELM 558
Cdd:PRK11174 492 QRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELS 571
|
....*....
gi 616431502 559 ASHAKYKNF 567
Cdd:PRK11174 572 QAGGLFATL 580
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
334-548 |
1.44e-55 |
|
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: 186.93 E-value: 1.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 334 GVLSFEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKI 411
Cdd:cd03244 1 GDIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 412 GYVMQSNSMMSGTIRDNiLYGINRHvSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNP 491
Cdd:cd03244 81 SIIPQDPVLFSGTIRSN-LDPFGEY-SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 492 DILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQV 548
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRV 215
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
38-309 |
9.47e-52 |
|
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: 178.91 E-value: 9.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVD----KFSVSHINWnLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESG 113
Cdd:cd18557 15 LPYLIGRLIDtiikGGDLDVLNE-LALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 114 QLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIAN 193
Cdd:cd18557 94 ELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 194 FSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAG 273
Cdd:cd18557 174 AGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVG 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 616431502 274 TLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18557 254 ELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
236-563 |
2.65e-50 |
|
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: 182.26 E-value: 2.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 236 AKIAAVVQPISGIV-MLLTIAIiLGFGALEIATGAITAGTLIA-MIFyviqLSMPLINLSTLVTDYKKAVGASS---RIY 310
Cdd:COG4618 235 SDRAGGFSALSKFLrLLLQSAV-LGLGAYLVIQGEITPGAMIAaSIL----MGRALAPIEQAIGGWKQFVSARQayrRLN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 311 EIMQE--PIEPTEALEDSEnvliddGVLSFEHVDFKYDVKK--ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYE 386
Cdd:COG4618 310 ELLAAvpAEPERMPLPRPK------GRLSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 387 IESGDIKYGlesvyDIPLSKWRRK-----IGYVMQSNSMMSGTIRDNIlygiNRH--VSDEELINYAKLANCHDFIMQFD 459
Cdd:COG4618 384 PTAGSVRLD-----GADLSQWDREelgrhIGYLPQDVELFDGTIAENI----ARFgdADPEKVVAAAKLAGVHEMILRLP 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 460 EGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETL-MEGRTTIVIAHRLSTIKKAG 538
Cdd:COG4618 455 DGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVD 534
|
330 340
....*....|....*....|....*
gi 616431502 539 QIIFLDKGQVTGKGTHSELMASHAK 563
Cdd:COG4618 535 KLLVLRDGRVQAFGPRDEVLARLAR 559
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
234-567 |
2.89e-50 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 182.33 E-value: 2.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 234 KQAKIAAVVQpisGIVML---LTIAIILGFGALEIAtGAITAGTLIAMIFY----VIQLSMPL----INLSTLVTdykka 302
Cdd:PRK11160 239 RQANLTGLSQ---ALMILangLTVVLMLWLAAGGVG-GNAQPGALIALFVFaalaAFEALMPVagafQHLGQVIA----- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 303 vgASSRIYEIMQEpiEPTEALEDSENVLIDDGVLSFEHVDFKYDVK--KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNL 380
Cdd:PRK11160 310 --SARRINEITEQ--KPEVTFPTTSTAAADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 381 IERMYEIESGDIKYGlesvyDIPLSKW-----RRKIGYVMQSNSMMSGTIRDNILYGINrHVSDEELINYAK---LANch 452
Cdd:PRK11160 386 LTRAWDPQQGEILLN-----GQPIADYseaalRQAISVVSQRVHLFSATLRDNLLLAAP-NASDEALIEVLQqvgLEK-- 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 453 dfIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLS 532
Cdd:PRK11160 458 --LLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLT 535
|
330 340 350
....*....|....*....|....*....|....*
gi 616431502 533 TIKKAGQIIFLDKGQVTGKGTHSELMASHAKYKNF 567
Cdd:PRK11160 536 GLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
269-543 |
4.98e-50 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 186.77 E-value: 4.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 269 AITAGTLIAMifYVIQLSMPLInlstlvTDYKKAVGASSRIYEIMQEpiEPTEALEDSENVLIDDGVLSFEHVDFKYDVK 348
Cdd:PTZ00265 326 SILLGVLISM--FMLTIILPNI------TEYMKSLEATNSLYEIINR--KPLVENNDDGKKLKDIKKIQFKNVRFHYDTR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 K---ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYG-LESVYDIPLSKWRRKIGYVMQSNSMMSGT 424
Cdd:PTZ00265 396 KdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLFSNS 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 425 IRDNILY------------------------GINRH--------------------------------VSDEELINYAKL 448
Cdd:PTZ00265 476 IKNNIKYslyslkdlealsnyynedgndsqeNKNKRnscrakcagdlndmsnttdsneliemrknyqtIKDSEVVDVSKK 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 449 ANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLM--EGRTTIV 526
Cdd:PTZ00265 556 VLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITII 635
|
330
....*....|....*..
gi 616431502 527 IAHRLSTIKKAGQIIFL 543
Cdd:PTZ00265 636 IAHRLSTIRYANTIFVL 652
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
56-309 |
3.30e-49 |
|
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: 172.22 E-value: 3.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 56 WNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLP 135
Cdd:cd18552 39 LLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 136 NLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTER 215
Cdd:cd18552 119 VLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAED 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 216 LELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTL 295
Cdd:cd18552 199 YEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNV 278
|
250
....*....|....
gi 616431502 296 VTDYKKAVGASSRI 309
Cdd:cd18552 279 NANLQRGLAAAERI 292
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
86-531 |
4.48e-49 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 178.32 E-value: 4.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 86 KIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFIsqkLPNLLPSIVT-LVGSLIMLFI--LDWKMTLLT 162
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLY---VRVIVPAGVAlVVGAAAVAAIavLSVPAALIL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 163 FITIPIFVLIMIPLGRIMQKisTSTQSEIANFSGLLGRVLT------EMRLVKISNTERLELDNAHKNLNEIYKlglKQA 236
Cdd:TIGR02868 160 AAGLLLAGFVAPLVSLRAAR--AAEQALARLRGELAAQLTDaldgaaELVASGALPAALAQVEEADRELTRAER---RAA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 237 KIAAVVQPISGIVMLLTIAiilgfGALEIATGAITAGTLIAMIFYVIQLsMPL------INLSTLVTDYKKAVGASSRIY 310
Cdd:TIGR02868 235 AATALGAALTLLAAGLAVL-----GALWAGGPAVADGRLAPVTLAVLVL-LPLaafeafAALPAAAQQLTRVRAAAERIV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 311 EIM-QEPIEPTEALEDSENVLIDDGVLSFEHVDFKY-DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIE 388
Cdd:TIGR02868 309 EVLdAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 389 SGDIKYGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGE 468
Cdd:TIGR02868 389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA-RPDATDEELWAALERVGLADWLRALPDGLDTVLGE 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616431502 469 RGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRL 531
Cdd:TIGR02868 468 GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
39-309 |
5.07e-49 |
|
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: 171.80 E-value: 5.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 39 PLFTGRIVDKFSVSHIN-----WNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESG 113
Cdd:cd18544 19 PLLIKRAIDDYIVPGQGdlqglLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 114 QLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIAN 193
Cdd:cd18544 99 RLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 194 FSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAG 273
Cdd:cd18544 179 LNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLG 258
|
250 260 270
....*....|....*....|....*....|....*.
gi 616431502 274 TLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18544 259 VLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
239-559 |
7.19e-48 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 175.23 E-value: 7.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 239 AAVVQPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRIYEIMQEPIE 318
Cdd:TIGR01842 224 AGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPS 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 319 PTEALEDSEnvliDDGVLSFEHVDFKYDVKK--ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGL 396
Cdd:TIGR01842 304 RDPAMPLPE----PEGHLSVENVTIVPPGGKkpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 397 ESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNILYgINRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGG 476
Cdd:TIGR01842 380 ADLKQWDRETFGKHIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGG 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 477 QRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETL-MEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHS 555
Cdd:TIGR01842 459 QRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERD 538
|
....
gi 616431502 556 ELMA 559
Cdd:TIGR01842 539 EVLA 542
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
39-309 |
1.89e-47 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 167.64 E-value: 1.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 39 PLFTGRIVDKFSVSHiNWN----LIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQ 114
Cdd:cd18545 20 PYLIKIAIDEYIPNG-DLSglliIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 115 LMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANF 194
Cdd:cd18545 99 ILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 195 SGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGT 274
Cdd:cd18545 179 NAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITVGV 258
|
250 260 270
....*....|....*....|....*....|....*
gi 616431502 275 LIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18545 259 LVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
38-309 |
2.36e-46 |
|
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: 164.53 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVD----KFSVSHInWNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESG 113
Cdd:cd18542 18 IPLLIRRIIDsvigGGLRELL-WLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 114 QLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIAN 193
Cdd:cd18542 97 DLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 194 FSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAG 273
Cdd:cd18542 177 LNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLG 256
|
250 260 270
....*....|....*....|....*....|....*.
gi 616431502 274 TLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18542 257 ELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
336-548 |
3.04e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 161.52 E-value: 3.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVM 415
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSMMSGTIRDNILYGI---NRHVSDEELINYAKLANCHDFIMqfdegyDTLVGErglkLSGGQRQRIDIARSFVKNPD 492
Cdd:COG4619 81 QEPALWGGTVRDNLPFPFqlrERKFDRERALELLERLGLPPDIL------DKPVER----LSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 493 ILLLDEATANLDSESELKIQEALETLM--EGRTTIVIAHRLSTIKK-AGQIIFLDKGQV 548
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
38-309 |
3.20e-46 |
|
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: 164.25 E-value: 3.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVD----KFSVSHInWNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESG 113
Cdd:cd18572 15 IPHYTGAVIDavvaDGSREAF-YRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 114 QLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIAN 193
Cdd:cd18572 94 ELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 194 FSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAG 273
Cdd:cd18572 174 ANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAG 253
|
250 260 270
....*....|....*....|....*....|....*.
gi 616431502 274 TLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18572 254 QLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-309 |
4.91e-44 |
|
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: 158.44 E-value: 4.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 39 PLFTGRIVDKFSVSHIN-------WNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNE 111
Cdd:cd18563 19 PYLTKILIDDVLIQLGPggntsllLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 112 SGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEI 191
Cdd:cd18563 99 TGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRW 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 192 ANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAIT 271
Cdd:cd18563 179 SRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMT 258
|
250 260 270
....*....|....*....|....*....|....*...
gi 616431502 272 AGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18563 259 LGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
336-548 |
1.83e-43 |
|
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: 154.65 E-value: 1.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIE-----SGDIKYGLESVY--DIPLSKWR 408
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYdlDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 409 RKIGYVMQSNSMMSGTIRDNILYGIN---------RHVSDEELINYAKLanchdfimqFDEGYDTLvgeRGLKLSGGQRQ 479
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRlhgiklkeeLDERVEEALRKAAL---------WDEVKDRL---HALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 480 RIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKK-AGQIIFLDKGQV 548
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRL 218
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
38-309 |
1.93e-43 |
|
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: 156.49 E-value: 1.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSVSH----INWNLIALFGGIFVInALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESG 113
Cdd:cd18575 15 LGQGLRLLIDQGFAAGntalLNRAFLLLLAVALVL-ALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 114 QLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIAN 193
Cdd:cd18575 94 EVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLAD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 194 FSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVvqpISGIVMLL---TIAIILGFGALEIATGAI 270
Cdd:cd18575 174 LSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARAL---LTALVIFLvfgAIVFVLWLGAHDVLAGRM 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 616431502 271 TAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18575 251 SAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
18-309 |
6.10e-43 |
|
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: 155.49 E-value: 6.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 18 VGLIVAAITISSlgslsgllVPLFTGRIVD----------KFSVSHINWNLIALfGGIFVINALLSGLGLYLLSKIGEKI 87
Cdd:cd18780 3 IALLVSSGTNLA--------LPYFFGQVIDavtnhsgsggEEALRALNQAVLIL-LGVVLIGSIATFLRSWLFTLAGERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 88 IYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIP 167
Cdd:cd18780 74 VARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 168 IFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISG 247
Cdd:cd18780 154 PLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616431502 248 IVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18780 234 AAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
336-548 |
9.94e-43 |
|
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: 150.83 E-value: 9.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKK--ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGY 413
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 414 VMQSNSMMSGTIRDNILyginrhvsdeelinyaklanchdfimqfdegydtlvgerglklSGGQRQRIDIARSFVKNPDI 493
Cdd:cd03246 81 LPQDDELFSGSIAENIL-------------------------------------------SGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 494 LLLDEATANLDSESELKIQEALETL-MEGRTTIVIAHRLSTIKKAGQIIFLDKGQV 548
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
336-561 |
3.72e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 151.37 E-value: 3.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPlSKWRRKIGYVM 415
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSMMSG-TIRDNI-----LYGINRHVSDEELINYAKLANCHDFImqfdegyDTLVGerglKLSGGQRQRIDIARSFVK 489
Cdd:COG1131 80 QEPALYPDlTVRENLrffarLYGLPRKEARERIDELLELFGLTDAA-------DRKVG----TLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616431502 490 NPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIA-HRLSTIKK-AGQIIFLDKGQVTGKGTHSELMASH 561
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
38-309 |
5.23e-42 |
|
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: 152.94 E-value: 5.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSVSHIN---------WNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFD 108
Cdd:cd18547 18 GPYLLGKAIDLIIEGLGGgggvdfsglLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 109 KNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQ 188
Cdd:cd18547 98 THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 189 SEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATG 268
Cdd:cd18547 178 KALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVING 257
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 616431502 269 AITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18547 258 ALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
39-309 |
6.42e-42 |
|
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: 152.63 E-value: 6.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 39 PLFT---GRIVDKFS---------------VSHINWNLIALFGGIFVINALLSGLGLYllskIGEKIIYAIRSVLWEHII 100
Cdd:cd18577 16 PLMTivfGDLFDAFTdfgsgesspdeflddVNKYALYFVYLGIGSFVLSYIQTACWTI----TGERQARRIRKRYLKALL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 101 QLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIM 180
Cdd:cd18577 92 RQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 181 QKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGF 260
Cdd:cd18577 172 SKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWY 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 616431502 261 GALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18577 252 GSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
39-289 |
1.04e-40 |
|
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: 148.56 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 39 PLFTGRIVDKFSV------SHINWNLIALFGgIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNES 112
Cdd:pfam00664 19 PLVLGRILDVLLPdgdpetQALNVYSLALLL-LGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 113 GQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIA 192
Cdd:pfam00664 98 GELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 193 NFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITA 272
Cdd:pfam00664 178 KASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSV 257
|
250
....*....|....*..
gi 616431502 273 GTLIAMIFYVIQLSMPL 289
Cdd:pfam00664 258 GDLVAFLSLFAQLFGPL 274
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
335-563 |
4.28e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 146.16 E-value: 4.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLsKWRRKIGYV 414
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSG-TIRDNI-----LYGINRHVSDEELINYAKLanchdfiMQFDEGYDTLVGErglkLSGGQRQRIDIARSFV 488
Cdd:COG4555 80 PDERGLYDRlTVRENIryfaeLYGLFDEELKKRIEELIEL-------LGLEEFLDRRVGE----LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 489 KNPDILLLDEATANLDSESELKIQEALETLM-EGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMASHAK 563
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
16-309 |
4.36e-40 |
|
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: 148.04 E-value: 4.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 16 WPVGLIVAAITISSLGSLSGLLVPLFTGRIVDKFSVSHINWNLIALFGGIFVInallsgLGLYLLSKIGEKIIYAIRSVL 95
Cdd:cd18564 20 WPLKVVIDDVLGDKPLPGLLGLAPLLGPDPLALLLLAAAALVGIALLRGLASY------AGTYLTALVGQRVVLDLRRDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 96 WEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIP 175
Cdd:cd18564 94 FAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 176 LGRIMQKISTSTQ---SEIAnfsGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLL 252
Cdd:cd18564 174 FSRRIKEASREQRrreGALA---SVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAV 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 253 TIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18564 251 GTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
333-548 |
1.29e-39 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 143.71 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 333 DGVLSFEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRK 410
Cdd:cd03369 4 HGEIEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 411 IGYVMQSNSMMSGTIRDNIlyGINRHVSDEELinYAKLAnchdfimqfdegydtlVGERGLKLSGGQRQRIDIARSFVKN 490
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNL--DPFDEYSDEEI--YGALR----------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 491 PDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQV 548
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
337-547 |
3.67e-39 |
|
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: 140.46 E-value: 3.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 337 SFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQ 416
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 417 snsmmsgtirdnilyginrhvsdeelinyaklanchdfimqfdegydtlvgerglkLSGGQRQRIDIARSFVKNPDILLL 496
Cdd:cd00267 81 --------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616431502 497 DEATANLDSESELKIQEALETLM-EGRTTIVIAHRLSTIKKAGQ-IIFLDKGQ 547
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAADrVIVLKDGK 157
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
336-547 |
5.81e-39 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 141.45 E-value: 5.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKK-----ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIerMYEIE--SGDIKYGlesvydiplskwr 408
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELEklSGSVSVP------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 409 RKIGYVMQSNSMMSGTIRDNILYGinrHVSDEELinYAK-LANCH---DfIMQFDEGYDTLVGERGLKLSGGQRQRIDIA 484
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFG---KPFDEER--YEKvIKACAlepD-LEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 485 RSFVKNPDILLLDEATANLDSESELKI-QEAL-ETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQ 547
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIfENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
38-309 |
9.11e-39 |
|
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: 143.81 E-value: 9.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSVSHI---------NWNLIALfGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFD 108
Cdd:cd18573 15 VPFAIGKLIDVASKESGdieifglslKTFALAL-LGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 109 KNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQ 188
Cdd:cd18573 94 KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 189 SEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATG 268
Cdd:cd18573 174 DALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASG 253
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 616431502 269 AITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18573 254 ELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
337-547 |
1.18e-38 |
|
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: 141.07 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 337 SFEHVDFKYD--VKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYV 414
Cdd:cd03225 1 ELKNLSFSYPdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQ-SNSMMSG-TIRDNILYGI-NRHVSDEELINYAKLANchdfimqfdegydTLVGERGLK------LSGGQRQRIDIAR 485
Cdd:cd03225 81 FQnPDDQFFGpTVEEEVAFGLeNLGLPEEEIEERVEEAL-------------ELVGLEGLRdrspftLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616431502 486 SFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIA-HRLSTIKK-AGQIIFLDKGQ 547
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-548 |
1.26e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.15 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKyglesVYDIPLSKWRRKIGYV 414
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVR-----LFGKPPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSG---TIRDNILYGINRHV--------SDEELINYA-KLANCHDFImqfdegyDTLVGErglkLSGGQRQRID 482
Cdd:COG1121 81 PQRAEVDWDfpiTVRDVVLMGRYGRRglfrrpsrADREAVDEAlERVGLEDLA-------DRPIGE----LSGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 483 IARSFVKNPDILLLDEATANLDSESELKIQEALETL-MEGRTTIVIAHRLSTIKK-AGQIIFLDKGQV 548
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
88-560 |
3.72e-38 |
|
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: 150.87 E-value: 3.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 88 IYAIRSV---LWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFIldwkmtlltfi 164
Cdd:TIGR00957 1034 IQASRVLhqdLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILL----------- 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 165 TIPIFVLIMIPLG--------------RIMQKISTSTQSEI-ANFS-GLLG----RVLTEM-RLVKISNTErleldnAHK 223
Cdd:TIGR00957 1103 ATPIAAVIIPPLGllyffvqrfyvassRQLKRLESVSRSPVySHFNeTLLGvsviRAFEEQeRFIHQSDLK------VDE 1176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 224 NLNEIYKLGLKQAKIAAVVQPISGIVMLltiaiilgFGAL--EIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKK 301
Cdd:TIGR00957 1177 NQKAYYPSIVANRWLAVRLECVGNCIVL--------FAALfaVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMET 1248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 302 AVGASSRIYEIMQEPIEPTEALEDSE--NVLIDDGVLSFEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTI 377
Cdd:TIGR00957 1249 NIVAVERLKEYSETEKEAPWQIQETAppSGWPPRGRVEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSL 1328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 378 FNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNI-LYGinrHVSDEELINYAKLANCHDFIM 456
Cdd:TIGR00957 1329 TLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS---QYSDEEVWWALELAHLKTFVS 1405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 457 QFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKK 536
Cdd:TIGR00957 1406 ALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMD 1485
|
490 500
....*....|....*....|....
gi 616431502 537 AGQIIFLDKGQVTGKGTHSELMAS 560
Cdd:TIGR00957 1486 YTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
351-501 |
1.05e-37 |
|
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: 136.24 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNSMMSG-TIRDNI 429
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 430 -----LYGINRHVSDEELINYAKLANCHDFImqfdegyDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATA 501
Cdd:pfam00005 81 rlgllLKGLSKREKDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
336-559 |
1.39e-37 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 138.62 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKY-DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYV 414
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQS--NSMMSGTIRDNILYG-INRHVSDEELINYAK--LAnchdfimqfdegydtLVGERGLK------LSGGQRQRIDI 483
Cdd:COG1122 81 FQNpdDQLFAPTVEEDVAFGpENLGLPREEIRERVEeaLE---------------LVGLEHLAdrppheLSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 484 ARSFVKNPDILLLDEATANLDSESELKIQEALETL-MEGRTTIVIAHRLSTI-KKAGQIIFLDKGQVTGKGTHSELMA 559
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-527 |
3.80e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 138.25 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKST---IFNlieRMYEIE-----SGDIKYGLESVYD--IPL 404
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLN---RMNDLIpgarvEGEILLDGEDIYDpdVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 405 SKWRRKIGYVMQ-SNSM-MSgtIRDNILYGI------NRHVSDEELINYAKLANchdfimQFDEGYDTLvGERGLKLSGG 476
Cdd:COG1117 88 VELRRRVGMVFQkPNPFpKS--IYDNVAYGLrlhgikSKSELDEIVEESLRKAA------LWDEVKDRL-KKSALGLSGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 616431502 477 QRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEgRTTIVI 527
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVI 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
336-547 |
2.23e-36 |
|
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: 133.85 E-value: 2.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYD--IPLSKWRRKIGY 413
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 414 VMQSNSMMSG-TIRDNILYGinrhvsdeelinyaklanchdfimqfdegydtlvgerglkLSGGQRQRIDIARSFVKNPD 492
Cdd:cd03229 81 VFQDFALFPHlTVLENIALG----------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 493 ILLLDEATANLDSESELKIQEALETL--MEGRTTIVIAHRLSTIKK-AGQIIFLDKGQ 547
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-309 |
3.72e-36 |
|
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: 136.84 E-value: 3.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 39 PLFTGRIVD----KFSVSHINWNLIALFGgIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQ 114
Cdd:cd18550 19 PLLLREIIDdalpQGDLGLLVLLALGMVA-VAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 115 LMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANF 194
Cdd:cd18550 98 IQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 195 SGLLGRVLTE--MRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITA 272
Cdd:cd18550 178 NSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTI 257
|
250 260 270
....*....|....*....|....*....|....*..
gi 616431502 273 GTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18550 258 GTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
336-562 |
4.03e-36 |
|
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: 135.12 E-value: 4.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKY-DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYV 414
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSG-TIRDNI-----LYGINRHVSDE---ELINYAKLAnchdfIMQFDEGYDTlvgerglKLSGGQRQRIDIAR 485
Cdd:cd03295 81 IQQIGLFPHmTVEENIalvpkLLKWPKEKIREradELLALVGLD-----PAEFADRYPH-------ELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 486 SFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRL-STIKKAGQIIFLDKGQVTGKGTHSELMASHA 562
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
335-558 |
4.84e-36 |
|
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: 135.17 E-value: 4.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYV 414
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSG-TIRDNILYGINRHVS--------DEELINYA-KLANCHDFIMQFdegYDTLvgerglklSGGQRQRIDIA 484
Cdd:COG1120 81 PQEPPAPFGlTVRELVALGRYPHLGlfgrpsaeDREAVEEAlERTGLEHLADRP---VDEL--------SGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 485 RSFVKNPDILLLDEATANLDSESELKIQEALETL--MEGRTTIVIAH------RLSTikkagQIIFLDKGQVTGKGTHSE 556
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHdlnlaaRYAD-----RLVLLKDGRIVAQGPPEE 224
|
..
gi 616431502 557 LM 558
Cdd:COG1120 225 VL 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
332-560 |
5.39e-36 |
|
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: 134.72 E-value: 5.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 332 DDGVLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIP---LSKWR 408
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 409 RKIGYVMQSN----SMmsgTIRDNILYGINRH--VSDEELINYA--KLAnchdfimqfdegydtLVGERGLK------LS 474
Cdd:COG1127 82 RRIGMLFQGGalfdSL---TVFENVAFPLREHtdLSEAEIRELVleKLE---------------LVGLPGAAdkmpseLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 475 GGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKKAG-QIIFLDKGQVTGK 551
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIAdRVAVLADGKIIAE 223
|
....*....
gi 616431502 552 GTHSELMAS 560
Cdd:COG1127 224 GTPEELLAS 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
336-548 |
6.19e-36 |
|
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: 133.80 E-value: 6.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPlsKWRRKIGYVM 415
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP--PERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSMMSG-TIRDNILYGINRHVSDEELINyaklANCHDFIMQFDEgyDTLVGERGLKLSGGQRQRIDIARSFVKNPDIL 494
Cdd:cd03259 79 QDYALFPHlTVAENIAFGLKLRGVPKAEIR----ARVRELLELVGL--EGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 495 LLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLS-TIKKAGQIIFLDKGQV 548
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRI 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
335-550 |
6.35e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.02 E-value: 6.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKK----ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIP---LSKW 407
Cdd:COG1136 4 LLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 408 RR-KIGYVMQSNSMMSG-TIRDNILY-----GINRHVSDE---ELINYAKLANCHDFimqfdegydtLVGErglkLSGGQ 477
Cdd:COG1136 84 RRrHIGFVFQFFNLLPElTALENVALplllaGVSRKERRErarELLERVGLGDRLDH----------RPSQ----LSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 478 RQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKKAGQIIFLDKGQVTG 550
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
56-309 |
1.41e-35 |
|
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: 134.92 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 56 WNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLP 135
Cdd:cd18546 39 LLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 136 NLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTER 215
Cdd:cd18546 119 QLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRER 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 216 lELDNAHKNLNEIY-KLGLKQAKIAAVVQPisGIVML--LTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINL 292
Cdd:cd18546 199 -RNAERFAELSDDYrDARLRAQRLVAIYFP--GVELLgnLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQL 275
|
250
....*....|....*..
gi 616431502 293 STLVTDYKKAVGASSRI 309
Cdd:cd18546 276 SQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
38-309 |
1.60e-35 |
|
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: 134.97 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSVSHINWNLIALFG----GIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESG 113
Cdd:cd18778 18 PPWLIRELVDLVTIGSKSLGLLLGLAllllGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 114 QLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIAN 193
Cdd:cd18778 98 DLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 194 FSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQP-ISGIVMLLTIaIILGFGALEIATGAITA 272
Cdd:cd18778 178 LNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPlMEFLTSLGTV-LVLGFGGRLVLAGELTI 256
|
250 260 270
....*....|....*....|....*....|....*..
gi 616431502 273 GTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18778 257 GDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
336-548 |
4.16e-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: 131.46 E-value: 4.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYD----VKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKW---- 407
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 408 RRKIGYVMQSNSMMSG-TIRDNILYG--INRHVSDE------ELINYAKLAnchdfimqfdEGYDTLVGErglkLSGGQR 478
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPllLAGVPKKErreraeELLERVGLG----------DRLNHYPSE----LSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616431502 479 QRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETL--MEGRTTIVIAHRLSTIKKAGQIIFLDKGQV 548
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
38-309 |
1.34e-34 |
|
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: 132.54 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSVSHINWNLIALFGGIFVINALLSGLGL----YLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESG 113
Cdd:cd18541 18 IPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRflwrYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 114 QLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIAN 193
Cdd:cd18541 98 DLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 194 FSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAG 273
Cdd:cd18541 178 LSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLG 257
|
250 260 270
....*....|....*....|....*....|....*.
gi 616431502 274 TLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18541 258 DLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
335-560 |
2.48e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 2.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYD--VKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYG-----LESVYDIplskw 407
Cdd:PRK13635 5 IIRVEHISFRYPdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlsEETVWDV----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 408 RRKIGYVMQS--NSMMSGTIRDNILYGI-NRHVSDEELI---NYA-KLANCHDFIMQfdEGYdtlvgerglKLSGGQRQR 480
Cdd:PRK13635 80 RRQVGMVFQNpdNQFVGATVQDDVAFGLeNIGVPREEMVervDQAlRQVGMEDFLNR--EPH---------RLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 481 IDIARSFVKNPDILLLDEATANLDSESElkiQEALETLME-----GRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHS 555
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGR---REVLETVRQlkeqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
....*
gi 616431502 556 ELMAS 560
Cdd:PRK13635 226 EIFKS 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
336-560 |
3.28e-34 |
|
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: 129.54 E-value: 3.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYD---IPLSKWRRKIG 412
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 413 YVMQSNSMMSG-TIRDNILYGINRHVS-DEELINyaklanchDFIMQFDEgydtLVGERGLK------LSGGQRQRIDIA 484
Cdd:cd03261 81 MLFQSGALFDSlTVFENVAFPLREHTRlSEEEIR--------EIVLEKLE----AVGLRGAEdlypaeLSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 485 RSFVKNPDILLLDEATANLDSESELKIQEALETL--MEGRTTIVIAHRLSTIKKAG-QIIFLDKGQVTGKGTHSELMAS 560
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAIAdRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
20-301 |
3.80e-34 |
|
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: 131.03 E-value: 3.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 20 LIVAAITISslgslsgllVPLFTGRIVDKFsVSHINWNLIALFGGI----FVINALLSGLGLYLLSKIGEKIIYAIRSVL 95
Cdd:cd18549 12 VLIAALDLV---------FPLIVRYIIDDL-LPSKNLRLILIIGAIllalYILRTLLNYFVTYWGHVMGARIETDMRRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 96 WEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIP 175
Cdd:cd18549 82 FEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 176 LGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNlNEIYKLGLKQA-KIAAVVQPISGIVMLLTI 254
Cdd:cd18549 162 FNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEG-NDRFLESKKKAyKAMAYFFSGMNFFTNLLN 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 616431502 255 AIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKK 301
Cdd:cd18549 241 LVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQK 287
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
38-309 |
3.93e-34 |
|
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: 131.07 E-value: 3.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSVSHIN---WNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQ 114
Cdd:cd18543 18 IPLLTRRAIDGPIAHGDRsalWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 115 LMSRLTDDTKVINEFISQkLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANF 194
Cdd:cd18543 98 LLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 195 SGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGT 274
Cdd:cd18543 177 ATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGT 256
|
250 260 270
....*....|....*....|....*....|....*
gi 616431502 275 LIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18543 257 LVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
336-552 |
4.41e-34 |
|
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: 127.43 E-value: 4.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYD--VKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlesvyDIPLSKW----RR 409
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD-----GVPVSDLekalSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 410 KIGYVMQSNSMMSGTIRDNIlyginrhvsdeelinyaklanchdfimqfdegydtlvgerGLKLSGGQRQRIDIARSFVK 489
Cdd:cd03247 76 LISVLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616431502 490 NPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKG 552
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
339-552 |
5.54e-34 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 127.17 E-value: 5.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 339 EHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSN 418
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 419 smmsgtirdnilyginrhvsdeELINYAKLAnchdfimqfDEGYDTlvgerglkLSGGQRQRIDIARSFVKNPDILLLDE 498
Cdd:cd03214 83 ----------------------ELLGLAHLA---------DRPFNE--------LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 499 ATANLDSESELKIQEALETL--MEGRTTIVIAHRLS-TIKKAGQIIFLDKGQVTGKG 552
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
336-548 |
6.35e-34 |
|
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: 126.74 E-value: 6.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLsKWRRKIGYVM 415
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSMmsgtirdnilyginrhvsdeelinyaklanchdfimqfdegYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILL 495
Cdd:cd03230 80 EEPSL-----------------------------------------YENLTVRENLKLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 496 LDEATANLDSESELKIQEALETLMEGRTTIVIA-HRLSTIKK-AGQIIFLDKGQV 548
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
335-549 |
8.67e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 127.86 E-value: 8.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKY-DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIP---LSKWRRK 410
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 411 IGYVMQSNSMMSG-TIRDNILY-----GINRHVSDE------ELINYAKLANChdFIMQfdegydtlvgerglkLSGGQR 478
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALplrvtGKSRKEIRRrvrevlDLVGLSDKAKA--LPHE---------------LSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616431502 479 QRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIA-HRLSTIKKAGQ-IIFLDKGQVT 549
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLV 216
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
82-568 |
2.65e-33 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 136.31 E-value: 2.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 82 KIGEKIIYAIRSVLWEHIIQLKMPFFD--KNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLF----ILD 155
Cdd:PTZ00265 892 VIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFyfcpIVA 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 156 WKMTLLTFITIPIF-VLIMIPLGRIMQKISTSTQSEIANFSG----------LLGRVLTEMRLVKISNTERLELDNAHKN 224
Cdd:PTZ00265 972 AVLTGTYFIFMRVFaIRARLTANKDVEKKEINQPGTVFAYNSddeifkdpsfLIQEAFYNMNTVIIYGLEDYFCNLIEKA 1051
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 225 LNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVG 304
Cdd:PTZ00265 1052 IDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKL 1131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 305 ASSRIYEIMQEpiEPTEALEDSENVLID-----DGVLSFEHVDFKYDVKK---ILDDVSFQIPQGQVSAFVGPSGSGKST 376
Cdd:PTZ00265 1132 SFEKYYPLIIR--KSNIDVRDNGGIRIKnkndiKGKIEIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKST 1209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 377 IFNLIERMYEIE------------------------------------------------------SGDIKYGLESVYDI 402
Cdd:PTZ00265 1210 VMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDY 1289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 403 PLSKWRRKIGYVMQSNSMMSGTIRDNILYGiNRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRID 482
Cdd:PTZ00265 1290 NLKDLRNLFSIVSQEPMLFNMSIYENIKFG-KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIA 1368
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 483 IARSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKKAGQIIFLDKGQVTG-----KGTHS 555
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNPDRTGsfvqaHGTHE 1448
|
570
....*....|....
gi 616431502 556 ELMASH-AKYKNFV 568
Cdd:PTZ00265 1449 ELLSVQdGVYKKYV 1462
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
337-546 |
1.26e-32 |
|
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: 124.57 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 337 SFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKyglesVYDIPLSKWRRKIGYVMQ 416
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIR-----VFGKPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 417 SNSM---MSGTIRDNILYGINRHV--------SDEELINYA-------KLANchdfiMQFDEgydtlvgerglkLSGGQR 478
Cdd:cd03235 76 RRSIdrdFPISVRDVVLMGLYGHKglfrrlskADKAKVDEAlervglsELAD-----RQIGE------------LSGGQQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 479 QRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETL-MEGRTTIVIAHRLSTI-KKAGQIIFLDKG 546
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
82-316 |
1.61e-32 |
|
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: 127.18 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 82 KIGEKIIYAIRSVLWEHIIQLKMPFFD--KNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMT 159
Cdd:cd18578 78 IAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 160 LLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIA 239
Cdd:cd18578 158 LVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALIS 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 240 AVVQPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRIYEIMQEP 316
Cdd:cd18578 238 GLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRK 314
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
336-529 |
3.87e-32 |
|
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: 123.35 E-value: 3.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYD----VKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLEsvydiPLSKWRRKI 411
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 412 GYVMQSNSMMS-GTIRDNILYGIN-RHVSDEELINYAklancHDFIMQFdegydtlvgerGLK---------LSGGQRQR 480
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElQGVPKAEARERA-----EELLELV-----------GLSgfenayphqLSGGMRQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 616431502 481 IDIARSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAH 529
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTH 190
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
335-552 |
5.09e-32 |
|
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: 123.38 E-value: 5.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVK----KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIP---LSKW 407
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 408 RRKIGYVMQsNSMMS----GTIRDNILYGINRH--VSDEELINYAKLANchdfimqfdegyDTLVG--ERGLK-----LS 474
Cdd:cd03257 81 RKEIQMVFQ-DPMSSlnprMTIGEQIAEPLRIHgkLSKKEARKEAVLLL------------LVGVGlpEEVLNrypheLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 475 GGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGK 551
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
.
gi 616431502 552 G 552
Cdd:cd03257 228 G 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
99-559 |
5.35e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 132.02 E-value: 5.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 99 IIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDwkmTLLTFITIPIFVLIMIPL-- 176
Cdd:PLN03232 993 ILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVS---TISLWAIMPLLILFYAAYly 1069
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 177 ----GRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKIsnTERLELDNAHKNLNEI-YKLGLKQAK--IAAVVQPISGIV 249
Cdd:PLN03232 1070 yqstSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKA--YDRMAKINGKSMDNNIrFTLANTSSNrwLTIRLETLGGVM 1147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 250 MLLTIAI-ILGFGALEIATG-AITAGTLIAmifYVIQLSMPLINLSTLVTDYKKAVGASSRIYEIMQEPIEPTEALEDSE 327
Cdd:PLN03232 1148 IWLTATFaVLRNGNAENQAGfASTMGLLLS---YTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNR 1224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 328 NV--LIDDGVLSFEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIP 403
Cdd:PLN03232 1225 PVsgWPSRGSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG 1304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 404 LSKWRRKIGYVMQSNSMMSGTIRDNIlYGINRHvSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDI 483
Cdd:PLN03232 1305 LTDLRRVLSIIPQSPVLFSGTVRFNI-DPFSEH-NDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSL 1382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 484 ARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMA 559
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
335-531 |
1.56e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 122.97 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYE-IES----GDIKYGLESVYD--IPLSKW 407
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlIPGfrveGKVTFHGKNLYApdVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 408 RRKIGYVMQSNSMMSGTIRDNILYG--INRHVSD-EELINYAklanchdfIMQ---FDEGYDTLvGERGLKLSGGQRQRI 481
Cdd:PRK14243 90 RRRIGMVFQKPNPFPKSIYDNIAYGarINGYKGDmDELVERS--------LRQaalWDEVKDKL-KQSGLSLSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 616431502 482 DIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRL 531
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
38-309 |
2.05e-31 |
|
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: 123.28 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFsVSHINWNLIALFGGIF----VINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESG 113
Cdd:cd18548 18 LPTLMADIIDEG-IANGDLSYILRTGLLMlllaLLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 114 QLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIAN 193
Cdd:cd18548 97 SLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 194 FSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAG 273
Cdd:cd18548 177 LNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVG 256
|
250 260 270
....*....|....*....|....*....|....*.
gi 616431502 274 TLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18548 257 DLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
336-557 |
4.76e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 124.05 E-value: 4.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLskWRRKIGYVM 415
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP--EKRNVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNS----MmsgTIRDNILYGI-NRHVSDEE----------LINYAKLAnchdfimqfdegyDTLVGErglkLSGGQRQR 480
Cdd:COG3842 84 QDYAlfphL---TVAENVAFGLrMRGVPKAEirarvaelleLVGLEGLA-------------DRYPHQ----LSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 481 IDIARSFVKNPDILLLDEATANLDSE------SELK-IQEALETlmegrTTIVIAHRLS---TIkkAGQIIFLDKGQVTG 550
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKlreemrEELRrLQRELGI-----TFIYVTHDQEealAL--ADRIAVMNDGRIEQ 216
|
....*..
gi 616431502 551 KGTHSEL 557
Cdd:COG3842 217 VGTPEEI 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-560 |
5.76e-31 |
|
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: 126.56 E-value: 5.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVK-----KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIP---LSK 406
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 407 WRRKIGYVMQS-----NSMMsgTIRDNILYGINRH--VSDEELinyAKLAnchdfimqfdegyDTLVGERGLK------- 472
Cdd:COG1123 340 LRRRVQMVFQDpysslNPRM--TVGDIIAEPLRLHglLSRAER---RERV-------------AELLERVGLPpdladry 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 473 ---LSGGQRQRIDIARSFVKNPDILLLDEATANLDseseLKIQEA-LETLME-----GRTTIVIAHRLSTIKK-AGQIIF 542
Cdd:COG1123 402 pheLSGGQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQiLNLLRDlqrelGLTYLFISHDLAVVRYiADRVAV 477
|
250
....*....|....*...
gi 616431502 543 LDKGQVTGKGTHSELMAS 560
Cdd:COG1123 478 MYDGRIVEDGPTEEVFAN 495
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
335-560 |
7.93e-31 |
|
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: 120.57 E-value: 7.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIER-MYEIESGDI-----KYGLESVYDIplskwR 408
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVrlfgeRRGGEDVWEL-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 409 RKIGYVmqSNSMM-----SGTIRDNIL------YGINRHVSDEELinyaKLAncHDFIMQFdeGYDTLVGERGLKLSGGQ 477
Cdd:COG1119 78 KRIGLV--SPALQlrfprDETVLDVVLsgffdsIGLYREPTDEQR----ERA--RELLELL--GLAHLADRPFGTLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 478 RQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLM-EGRTTIV-IAHRLSTIKKA-GQIIFLDKGQVTGKGTH 554
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAaEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAGPK 227
|
....*.
gi 616431502 555 SELMAS 560
Cdd:COG1119 228 EEVLTS 233
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-309 |
8.01e-31 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 121.82 E-value: 8.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 18 VGLIVAAITISslgslsgllVPLFTGRIVDKFSVSHIN---WNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSV 94
Cdd:cd18540 10 LMLLVALLDAV---------FPLLTKYAIDHFITPGTLdglTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 95 LWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIP-IFVLIM 173
Cdd:cd18540 81 AFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPvLAVVSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 174 IPLGRIM--QKISTSTQSEI-ANFS-GLLGrvlteMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIV 249
Cdd:cd18540 161 YFQKKILkaYRKVRKINSRItGAFNeGITG-----AKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 250 MLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18540 236 GSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
38-309 |
2.04e-30 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 120.49 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVD---------KFSVSHINWNLIA--------LFGGIFVINALlsglglyllskigeKIIYAIRSVLWEHII 100
Cdd:cd18784 15 IPYYTGQVIDgivieksqdKFSRAIIIMGLLAiassvaagIRGGLFTLAMA--------------RLNIRIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 101 QLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIM 180
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 181 QKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGF 260
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 616431502 261 GALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18784 241 GGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
39-559 |
4.38e-30 |
|
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: 126.18 E-value: 4.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 39 PLFTGRIVDKFSVSHINWNLIALFGGI-----FVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESG 113
Cdd:TIGR01271 100 PLLLGRIIASYDPFNAPEREIAYYLALglcllFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 114 QLMSRLTDDTKVINEFIS-QKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIpiFVLIMIPLGRIMQKISTSTQSEIA 192
Cdd:TIGR01271 180 QLVSLLSNNLNKFDEGLAlAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLIL--LALFQACLGQKMMPYRDKRAGKIS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 193 NFSGLLGRVLTEMRLVKISNTErlelDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTiAIILGFgaLEIATGAITA 272
Cdd:TIGR01271 258 ERLAITSEIIENIQSVKAYCWE----EAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFS-GFFVVF--LSVVPYALIK 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 273 GTLIAMIF----YVIQLSMPLI-NLSTLVTDYKKAVGASSRI--------YEIMQEPIEPTEALEDSENVLIDDGVLS-F 338
Cdd:TIGR01271 331 GIILRRIFttisYCIVLRMTVTrQFPGAIQTWYDSLGAITKIqdflckeeYKTLEYNLTTTEVEMVNVTASWDEGIGElF 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 339 EHV-------------------DFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlesv 399
Cdd:TIGR01271 411 EKIkqnnkarkqpngddglffsNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS---- 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 400 ydiplskwrRKIGYVMQSNSMMSGTIRDNILYGIN----RHVSdeeLINYAKLancHDFIMQFDEGYDTLVGERGLKLSG 475
Cdd:TIGR01271 487 ---------GRISFSPQTSWIMPGTIKDNIIFGLSydeyRYTS---VIKACQL---EEDIALFPEKDKTVLGEGGITLSG 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 476 GQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEA-LETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTH 554
Cdd:TIGR01271 552 GQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTF 631
|
....*
gi 616431502 555 SELMA 559
Cdd:TIGR01271 632 SELQA 636
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
335-548 |
5.16e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 117.79 E-value: 5.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTI---FNLIErmyEIESGDIKYGLESVYDIP--LSKWRR 409
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLE---EPDSGTITVDGEDLTDSKkdINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 410 KIGYVMQS----NSMmsgTIRDNILYG--INRHVSDEELINYAK--LAnchdfimqfdegydtLVG--ERGLK----LSG 475
Cdd:COG1126 78 KVGMVFQQfnlfPHL---TVLENVTLApiKVKKMSKAEAEERAMelLE---------------RVGlaDKADAypaqLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 476 GQRQRIDIARSFVKNPDILLLDEATANLDSESelkIQEALETLM----EGRTTIVIAHRLSTIKK-AGQIIFLDKGQV 548
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPEL---VGEVLDVMRdlakEGMTMVVVTHEMGFAREvADRVVFMDGGRI 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
349-559 |
5.23e-30 |
|
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: 117.68 E-value: 5.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKST---IFNLIERMyeiESGDIKYGLESVYDIP---LSKWRRKIGYVMQS-NSMM 421
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLERP---TSGSVLVDGTDLTLLSgkeLRKARRRIGMIFQHfNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 422 SGTIRDNILY----------GINRHVsdEELINYAKLANCHDFimqfdegYDTlvgerglKLSGGQRQRIDIARSFVKNP 491
Cdd:cd03258 96 SRTVFENVALpleiagvpkaEIEERV--LELLELVGLEDKADA-------YPA-------QLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616431502 492 DILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMA 559
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
103-570 |
5.96e-30 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 126.05 E-value: 5.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 103 KMPFFDKNESGQLMSRLTDDTKVinefisqkLPNLLPsiVTLVGSLIMLFILDWKMtLLTFITIPIFVLIMIPLG----R 178
Cdd:PTZ00243 1045 TMSFFDTTPLGRILNRFSRDIDI--------LDNTLP--MSYLYLLQCLFSICSSI-LVTSASQPFVLVALVPCGylyyR 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 179 IMQKISTST-----QSEIAN---FSgLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAK----IAAVVQPIS 246
Cdd:PTZ00243 1114 LMQFYNSANreirrIKSVAKspvFT-LLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVanrwLGVRVEFLS 1192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 247 GIVmLLTIAII-------------LGFGALEIATGAITAGTL------IA-----------MIFY---VIQLSMPliNLS 293
Cdd:PTZ00243 1193 NIV-VTVIALIgvigtmlratsqeIGLVSLSLTMAMQTTATLnwlvrqVAtveadmnsverLLYYtdeVPHEDMP--ELD 1269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 294 TLVTDYKKAVG-ASSRIYEIMQEPIEPTEALEDSenvlIDDGVLSFEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPS 370
Cdd:PTZ00243 1270 EEVDALERRTGmAADVTGTVVIEPASPTSAAPHP----VQAGSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRT 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 371 GSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNI----------------LYGIN 434
Cdd:PTZ00243 1346 GSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVdpfleassaevwaaleLVGLR 1425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 435 RHVSDEElinyaklanchdfimqfdEGYDTLVGERGLKLSGGQRQRIDIARSFVK-NPDILLLDEATANLDSESELKIQE 513
Cdd:PTZ00243 1426 ERVASES------------------EGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQA 1487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 514 ALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSEL-MASHAKYKNFVVS 570
Cdd:PTZ00243 1488 TVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVEA 1545
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-563 |
1.65e-29 |
|
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: 122.32 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPSGSGKST----IFNLIERMYEIeSGDIKYGLESVYDIPLSKWR 408
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTlalaLMGLLPHGGRI-SGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 409 RKIGYVMQS--NSMMSGTIRDNILYGI-NRHVSDEELINYAKLAnchdfimqFDE-GYDTLVGERGLKLSGGQRQRIDIA 484
Cdd:COG1123 83 RRIGMVFQDpmTQLNPVTVGDQIAEALeNLGLSRAEARARVLEL--------LEAvGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 485 RSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTI-KKAGQIIFLDKGQVTGKGTHSELMASH 561
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
..
gi 616431502 562 AK 563
Cdd:COG1123 235 QA 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
332-527 |
2.47e-29 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 116.73 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 332 DDGVLSFEHVDFKYDVKK----ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlesvyDIPLSKW 407
Cdd:COG1116 4 AAPALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD-----GKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 408 RRKIGYVMQSNSMMs-gTIRDNILYGIN-RHVSDEElinYAKLAncHDFImqfdegydTLVgerGLK---------LSGG 476
Cdd:COG1116 79 GPDRGVVFQEPALLpwlTVLDNVALGLElRGVPKAE---RRERA--RELL--------ELV---GLAgfedayphqLSGG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 616431502 477 QRQRIDIARSFVKNPDILLLDEATANLDSESELKIQ-EALETLMEGRTTIVI 527
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQdELLRLWQETGKTVLF 194
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
336-548 |
5.74e-29 |
|
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: 114.16 E-value: 5.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYD--IPLSKWRRKIGY 413
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 414 VMQS-NSMMSGTIRDNILYGIN--RHVSDEELINYAklanchdfimqfdEGYDTLVG--ERGLK----LSGGQRQRIDIA 484
Cdd:cd03262 81 VFQQfNLFPHLTVLENITLAPIkvKGMSKAEAEERA-------------LELLEKVGlaDKADAypaqLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 485 RSFVKNPDILLLDEATANLDSESelkIQEALETLM----EGRTTIVIAHRLSTIKK-AGQIIFLDKGQV 548
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPEL---VGEVLDVMKdlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
336-559 |
9.91e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 115.22 E-value: 9.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYD--VKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIK-YGL-----ESVYDIplskw 407
Cdd:TIGR04520 1 IEVENVSFSYPesEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTvDGLdtldeENLWEI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 408 RRKIGYVMQS--NSMMSGTIRDNILYGI-NRHVSDEELI----NYAKLANCHDFIMQfdEGYdtlvgerglKLSGGQRQR 480
Cdd:TIGR04520 76 RKKVGMVFQNpdNQFVGATVEDDVAFGLeNLGVPREEMRkrvdEALKLVGMEDFRDR--EPH---------LLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 481 IDIARSFVKNPDILLLDEATANLDSESELKIQEALETLM--EGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELM 558
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIF 224
|
.
gi 616431502 559 A 559
Cdd:TIGR04520 225 S 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
335-559 |
1.11e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.21 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYD---VKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDI-----KYGLESVYDIplsk 406
Cdd:PRK13650 4 IIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdLLTEENVWDI---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 407 wRRKIGYVMQS--NSMMSGTIRDNILYGI-NRHVSDEELINyaklanchdfimQFDEGYDtLVGERGLK------LSGGQ 477
Cdd:PRK13650 80 -RHKIGMVFQNpdNQFVGATVEDDVAFGLeNKGIPHEEMKE------------RVNEALE-LVGMQDFKereparLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 478 RQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHS 555
Cdd:PRK13650 146 KQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPR 225
|
....
gi 616431502 556 ELMA 559
Cdd:PRK13650 226 ELFS 229
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
56-309 |
1.30e-28 |
|
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: 116.13 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 56 WNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLP 135
Cdd:cd18565 54 WLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGAN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 136 NLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTER 215
Cdd:cd18565 134 SIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAED 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 216 LELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEI------ATGAITAGTLIAMIFYVIQLSMPL 289
Cdd:cd18565 214 FERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVldgpplFTGTLTVGTLVTFLFYTQRLLWPL 293
|
250 260
....*....|....*....|
gi 616431502 290 INLSTLVTDYKKAVGASSRI 309
Cdd:cd18565 294 TRLGDLIDQYQRAMASAKRV 313
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
336-558 |
1.45e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 114.34 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVM 415
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSMMSG-TIRDNILYGINRHVS--------DEELINYAklanchdfiMQfDEGYDTLVGERGLKLSGGQRQRIDIARS 486
Cdd:PRK11231 83 QHHLTPEGiTVRELVAYGRSPWLSlwgrlsaeDNARVNQA---------ME-QTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 487 FVKNPDILLLDEATANLDseseLKIQEALETLM-----EGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELM 558
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLD----INHQVELMRLMrelntQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
336-552 |
1.71e-28 |
|
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: 112.67 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGqVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPlSKWRRKIGYVM 415
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSMMSG-TIRD-----NILYGINRHVSDEELINYAKLANCHDFimqfdegYDTLVGerglKLSGGQRQRIDIARSFVK 489
Cdd:cd03264 79 QEFGVYPNfTVREfldyiAWLKGIPSKEVKARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616431502 490 NPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKG 552
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
336-557 |
2.24e-28 |
|
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: 113.43 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKY-DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIK---YGLESVYDIPLSKWRRKI 411
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 412 GYVMQS-----------NSMMSGTIRDNILYGINRHVSDEELINYAKLANchdfimqfDEGYDTLVGERGLKLSGGQRQR 480
Cdd:cd03256 81 GMIFQQfnlierlsvleNVLSGRLGRRSTWRSLFGLFPKEEKQRALAALE--------RVGLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 481 IDIARSFVKNPDILLLDEATANLDSESELKIQEALETL--MEGRTTIVIAHRLSTIKKAGQ-IIFLDKGQVTGKGTHSEL 557
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADrIVGLKDGRIVFDGPPAEL 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
344-561 |
5.45e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 112.59 E-value: 5.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 344 KYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQS-----N 418
Cdd:COG1124 14 GGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDpyaslH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 419 SMMsgTIRDNI-----LYGINRHVSD-EELINYAKLanchdfimqfdegYDTLVGERGLKLSGGQRQRIDIARSFVKNPD 492
Cdd:COG1124 94 PRH--TVDRILaeplrIHGLPDREERiAELLEQVGL-------------PPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616431502 493 ILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMASH 561
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
333-557 |
7.52e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.92 E-value: 7.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 333 DGVLSFEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRK 410
Cdd:PRK13648 5 NSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 411 IGYVMQS--NSMMSGTIRDNILYGINRH-VSDEELinyaklancHDFIMQFDEGYDTL--VGERGLKLSGGQRQRIDIAR 485
Cdd:PRK13648 85 IGIVFQNpdNQFVGSIVKYDVAFGLENHaVPYDEM---------HRRVSEALKQVDMLerADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616431502 486 SFVKNPDILLLDEATANLDSESELKIQEALETLMEGR--TTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSEL 557
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
348-552 |
7.71e-28 |
|
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: 110.33 E-value: 7.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLI--ERMYEIESGDIKYGlesVYDIPLSKWRRKIGYVMQsnsmmsgti 425
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLIN---GRPLDKRSFRKIIGYVPQ--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 426 rDNILYGinrHVSDEELINYAklANChdfimqfdegydtlvgeRGLklSGGQRQRIDIARSFVKNPDILLLDEATANLDS 505
Cdd:cd03213 90 -DDILHP---TLTVRETLMFA--AKL-----------------RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 616431502 506 ESELKIQEALETLM-EGRTTIVIAHRLST--IKKAGQIIFLDKGQVTGKG 552
Cdd:cd03213 145 SSALQVMSLLRRLAdTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
332-557 |
1.03e-27 |
|
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: 112.64 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 332 DDGVLSFEHvdFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlesvydiplskwrRKI 411
Cdd:cd03291 36 DDNNLFFSN--LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS-------------GRI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 412 GYVMQSNSMMSGTIRDNILYGinrhVSDEELINYAKLANCH--DFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVK 489
Cdd:cd03291 101 SFSSQFSWIMPGTIKENIIFG----VSYDEYRYKSVVKACQleEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 490 NPDILLLDEATANLDSESELKIQEA-LETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSEL 557
Cdd:cd03291 177 DADLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
112-568 |
1.15e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 118.93 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 112 SGQLMSRLTDDTKVINEfISQKLPNLLPSIVTLVGSLIMLF----ILDWKMTLLTFITIPIFVLIMiplgRIMQKISTST 187
Cdd:PLN03232 397 SGKVTNMITTDANALQQ-IAEQLHGLWSAPFRIIVSMVLLYqqlgVASLFGSLILFLLIPLQTLIV----RKMRKLTKEG 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 188 QSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAA----VVQPISGIVMLLTIAIILGFGAL 263
Cdd:PLN03232 472 LQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAfnsfILNSIPVVVTLVSFGVFVLLGGD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 264 EIATGAITAGTLIAMIFYviqlsmPLINLSTLVTDYKKAVGASSRIYEIMQepiepTEALEDSENVLIDDGV--LSFEHV 341
Cdd:PLN03232 552 LTPARAFTSLSLFAVLRS------PLNMLPNLLSQVVNANVSLQRIEELLL-----SEERILAQNPPLQPGApaISIKNG 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 342 DFKYDVK---KILDDVSFQIPQGQVSAFVGPSGSGKSTifnLIERMYeiesGDIKYGLESVYDIplskwRRKIGYVMQSN 418
Cdd:PLN03232 621 YFSWDSKtskPTLSDINLEIPVGSLVAIVGGTGEGKTS---LISAML----GELSHAETSSVVI-----RGSVAYVPQVS 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 419 SMMSGTIRDNILYGinrhvSDEELINYAKLANC----HDfiMQFDEGYD-TLVGERGLKLSGGQRQRIDIARSFVKNPDI 493
Cdd:PLN03232 689 WIFNATVRENILFG-----SDFESERYWRAIDVtalqHD--LDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDI 761
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 494 LLLDEATANLDSESELKI-QEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHAKYKNFV 568
Cdd:PLN03232 762 YIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
334-559 |
1.27e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 118.69 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 334 GVLSFEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkygLESVYDIP---LSKWR 408
Cdd:PLN03130 1236 GSIKFEDVVLRYrpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRI---LIDGCDISkfgLMDLR 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 409 RKIGYVMQSNSMMSGTIRDNiLYGINRHvSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFV 488
Cdd:PLN03130 1313 KVLGIIPQAPVLFSGTVRFN-LDPFNEH-NDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616431502 489 KNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMA 559
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-557 |
1.40e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 111.54 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIE-----SGDIKYGLESVYDIPLSKWRRKIGYVMQ-SNSMMS 422
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 423 GTIRDNILYG--INRHV-SDEELINYAKLAncHDFIMQFDEGYDTLVGERGlKLSGGQRQRIDIARSFVKNPDILLLDEA 499
Cdd:PRK14247 97 LSIFENVALGlkLNRLVkSKKELQERVRWA--LEKAQLWDEVKDRLDAPAG-KLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 500 TANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQ-IIFLDKGQVTGKGTHSEL 557
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDyVAFLYKGQIVEWGPTREV 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
336-548 |
1.45e-27 |
|
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: 110.42 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKwrRKIGYVM 415
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSM---MsgTIRDNILYGINRHVSDEELIN-----YAKLAnchdfimqfdeGYDTLVGERGLKLSGGQRQRIDIARSF 487
Cdd:cd03301 79 QNYALyphM--TVYDNIAFGLKLRKVPKDEIDervreVAELL-----------QIEHLLDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 488 VKNPDILLLDEATANLDSE------SELK-IQEALetlmeGRTTIVIAH-RLSTIKKAGQIIFLDKGQV 548
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKlrvqmrAELKrLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
353-560 |
1.51e-27 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 114.05 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 353 DVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYD----IPLSKWRRKIGYVMQSNSMMSG-TIRD 427
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 428 NILYGINRHVSDEELINYAKLANCHdfimqfdeGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSES 507
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVIELL--------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 508 ELKIQEALETLME--GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMAS 560
Cdd:TIGR02142 167 KYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
333-557 |
1.59e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.20 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 333 DGVLSFEHVDFKY-DVKK-ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGD--------IKYGLESVYDI 402
Cdd:PRK13640 3 DNIVEFKHVSFTYpDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 403 plskwRRKIGYVMQS--NSMMSGTIRDNILYGI-NRHVSDEELINYAklancHDFIMQFdeGYDTLVGERGLKLSGGQRQ 479
Cdd:PRK13640 83 -----REKVGIVFQNpdNQFVGATVGDDVAFGLeNRAVPRPEMIKIV-----RDVLADV--GMLDYIDSEPANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 480 RIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSEL 557
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
343-557 |
1.75e-27 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 110.29 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 343 FKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIK-YGLESVYDIplSKWRRKIGYVMQSNSMM 421
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYiNGYSIRTDR--KAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 422 SG-TIRDNI-----LYGINRHVSDEELINYAKLANCHDFImqfdegyDTLVGErglkLSGGQRQRIDIARSFVKNPDILL 495
Cdd:cd03263 88 DElTVREHLrfyarLKGLPKSEIKEEVELLLRVLGLTDKA-------NKRART----LSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 496 LDEATANLDSESELKIQEALETLMEGRTTIVIAH------RLSTikkagQIIFLDKGQVTGKGTHSEL 557
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdeaeALCD-----RIAIMSDGKLRCIGSPQEL 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-536 |
2.16e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 111.28 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 339 EHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIES-----GDIKYGLESVYD--IPLSKWRRKI 411
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLNRLRRQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 412 GYVMQSNSMMSGTIRDNILYGInrhvsdeELINYAKLANCHDFI---MQFDEGYDTL---VGERGLKLSGGQRQRIDIAR 485
Cdd:PRK14258 91 SMVHPKPNLFPMSVYDNVAYGV-------KIVGWRPKLEIDDIVesaLKDADLWDEIkhkIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616431502 486 SFVKNPDILLLDEATANLDSESELKIQEALETL-MEGRTTIVI-AHRLSTIKK 536
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIvSHNLHQVSR 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
336-548 |
4.82e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.47 E-value: 4.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKwrRKIGYVM 415
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QS----NSMmsgTIRDNILYGI-NRHVSDEElINyAKLANCHDfIMQFDEGYDTLVGErglkLSGGQRQRIDIARSFVKN 490
Cdd:COG3839 82 QSyalyPHM---TVYENIAFPLkLRKVPKAE-ID-RRVREAAE-LLGLEDLLDRKPKQ----LSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 491 PDILLLDEATANLDSE------SELK-IQEALETlmegrTTIVIAHRLS---TIkkAGQIIFLDKGQV 548
Cdd:COG3839 152 PKVFLLDEPLSNLDAKlrvemrAEIKrLHRRLGT-----TTIYVTHDQVeamTL--ADRIAVMNDGRI 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
338-558 |
5.30e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.41 E-value: 5.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 338 FEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYD--IPLSKWRRKIGYVM 415
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QS-NSMMSGTIRDNILYGiNRHVSDeelinyAKLANCHDFIMQfdegydtLVGERGL---------KLSGGQRQRIDIAR 485
Cdd:PRK09493 84 QQfYLFPHLTALENVMFG-PLRVRG------ASKEEAEKQARE-------LLAKVGLaerahhypsELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 486 SFVKNPDILLLDEATANLDSESE---LKIQEALETlmEGRTTIVIAHRLSTIKKAG-QIIFLDKGQVTGKGTHSELM 558
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRhevLKVMQDLAE--EGMTMVIVTHEIGFAEKVAsRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
341-552 |
5.86e-27 |
|
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: 108.54 E-value: 5.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 341 VDFKYDVKKILDDVSFQIPqGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYG----LESVYDIPLSKWRRKIGYVMQ 416
Cdd:cd03297 4 VDIEKRLPDFTLKIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlFDSRKKINLPPQQRKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 417 SNSMMSG-TIRDNILYGINRHVSDEELINYAKLANchdfIMQFDEgydtLVGERGLKLSGGQRQRIDIARSFVKNPDILL 495
Cdd:cd03297 83 QYALFPHlNVRENLAFGLKRKRNREDRISVDELLD----LLGLDH----LLNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 496 LDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKG 552
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
335-548 |
6.33e-27 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 109.38 E-value: 6.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDV-KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkygleSVYDIPLSK------- 406
Cdd:COG3638 2 MLELRNLSKRYPGgTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEI-----LVDGQDVTAlrgralr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 407 -WRRKIGYVMQS----NSMmsgTIRDNILYG----------INRHVSDEELinyaklanchdfimqfDEGYDTL--VG-- 467
Cdd:COG3638 77 rLRRRIGMIFQQfnlvPRL---SVLTNVLAGrlgrtstwrsLLGLFPPEDR----------------ERALEALerVGla 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 468 ----ERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKK-AGQI 540
Cdd:COG3638 138 dkayQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRI 217
|
....*...
gi 616431502 541 IFLDKGQV 548
Cdd:COG3638 218 IGLRDGRV 225
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
341-559 |
8.32e-27 |
|
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: 109.61 E-value: 8.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 341 VDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNSM 420
Cdd:cd03288 27 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPIL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 421 MSGTIRDNIlyGINRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEAT 500
Cdd:cd03288 107 FSGSIRFNL--DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 501 ANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMA 559
Cdd:cd03288 185 ASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
331-573 |
2.07e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.54 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 331 IDDGVLSFEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIK-YGLESVYDiPLSKW 407
Cdd:PRK13632 3 NKSVMIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKiDGITISKE-NLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 408 RRKIGYVMQS--NSMMSGTIRDNILYGI-NRHVSDEEL----INYAKLANCHDFIMQfdegydtlvgeRGLKLSGGQRQR 480
Cdd:PRK13632 82 RKKIGIIFQNpdNQFIGATVEDDIAFGLeNKKVPPKKMkdiiDDLAKKVGMEDYLDK-----------EPQNLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 481 IDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGR--TTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELM 558
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
250
....*....|....*
gi 616431502 559 AShakyKNFVVSQKL 573
Cdd:PRK13632 231 NN----KEILEKAKI 241
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
335-531 |
3.64e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 107.55 E-value: 3.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIE-----SGDIKYGLESVYDiPLS---K 406
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYS-PRTdtvD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 407 WRRKIGYVMQSNSMMSGTIRDNILYGI------NRHVSDEELINYAKLANChdfimqFDEGYDTLvGERGLKLSGGQRQR 480
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVYGLrlkgikDKQVLDEAVEKSLKGASI------WDEVKDRL-HDSALGLSGGQQQR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 616431502 481 IDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRL 531
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
343-560 |
1.16e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 112.56 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 343 FKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkyglesvydiplskW-RRKIGYVMQSNSMM 421
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WaERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 422 SGTIRDNILYginrhvSDEEliNYAKLAN---CHDF---IMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILL 495
Cdd:PTZ00243 734 NATVRGNILF------FDEE--DAARLADavrVSQLeadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYL 805
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 496 LDEATANLDSE-SELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMAS 560
Cdd:PTZ00243 806 LDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRT 871
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
339-557 |
1.85e-25 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 104.37 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 339 EHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGD-IKYGLESVYDIplSKWRRKIGYVMQS 417
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVVREP--REVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 418 NSMMSG-TIRDNI-----LYGINRHVSDE---ELINYAKLAnchdfimqfdEGYDTLVGerglKLSGGQRQRIDIARSFV 488
Cdd:cd03265 82 LSVDDElTGWENLyiharLYGVPGAERREridELLDFVGLL----------EAADRLVK----TYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616431502 489 KNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSEL 557
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
118-530 |
3.05e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.90 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 118 RLTDDtkvINEFISQKLP---NLLPSIVTLVGSLIMLFILDWKMTLLTF---ITIPIFV------------LIMIPLGRI 179
Cdd:COG4178 129 RIAED---IRLFTETTLSlslGLLSSVVTLISFIGILWSLSGSLTFTLGgysITIPGYMvwaaliyaiigtLLTHLIGRP 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 180 MQKISTSTQSEIANF-SGLlgrvlteMRL------VKISNTERLELDNAHKNLNEI----YKLGLKQAKIAAVVQPISGI 248
Cdd:COG4178 206 LIRLNFEQQRREADFrFAL-------VRVrenaesIALYRGEAAERRRLRRRFDAVianwRRLIRRQRNLTFFTTGYGQL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 249 VMLLTIAIILG--FgaleiaTGAITAGTL--IAMIFYVIQLSmplinLSTLVTDYK-----KAVgaSSRIYEIMQEpIEP 319
Cdd:COG4178 279 AVIFPILVAAPryF------AGEITLGGLmqAASAFGQVQGA-----LSWFVDNYQslaewRAT--VDRLAGFEEA-LEA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 320 TEALEDSENVL--IDDGVLSFEHVDFK-YDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKY-G 395
Cdd:COG4178 345 ADALPEAASRIetSEDGALALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 396 LESVYDIPlskwrrkigyvmQSNSMMSGTIRDNILY-GINRHVSDEELINYAKLANCHDFIMQFDEGYDtlvgeRGLKLS 474
Cdd:COG4178 425 GARVLFLP------------QRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERLDEEAD-----WDQVLS 487
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 475 GGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHR 530
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
348-548 |
3.31e-25 |
|
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: 103.89 E-value: 3.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMyeIESGDIKYGLESVYDIPLSK--WRRKIGYVMQSNSMMSG-T 424
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR--VEGGGTTSGQILFNGQPRKPdqFQKCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 425 IRDNILYGIN----RHVSD---EELINYAKLANCHDfimqfdegydTLVGERGLK-LSGGQRQRIDIARSFVKNPDILLL 496
Cdd:cd03234 98 VRETLTYTAIlrlpRKSSDairKKRVEDVLLRDLAL----------TRIGGNLVKgISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 497 DEATANLDSESELKIQEAL-ETLMEGRTTIVIAH--RLSTIKKAGQIIFLDKGQV 548
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLsQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
338-557 |
5.53e-25 |
|
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: 103.57 E-value: 5.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 338 FEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKwrRKIGYVMQS 417
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 418 NSMMSG-TIRDNILYGIN-RHVS---DEELINyAKLANCHDFiMQFDEGYDTLVGErglkLSGGQRQRIDIARSFVKNPD 492
Cdd:cd03296 83 YALFRHmTVFDNVAFGLRvKPRSerpPEAEIR-AKVHELLKL-VQLDWLADRYPAQ----LSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616431502 493 ILLLDEATANLDSeselKIQEALETLME------GRTTIVIAHRLS-TIKKAGQIIFLDKGQVTGKGTHSEL 557
Cdd:cd03296 157 VLLLDEPFGALDA----KVRKELRRWLRrlhdelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
39-309 |
5.91e-25 |
|
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: 105.22 E-value: 5.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 39 PLFTGRIVDKFSVSHINWNLIAL---FGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQL 115
Cdd:cd18570 22 SFFFQILIDDIIPSGDINLLNIIsigLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 116 MSRLTDDTKvINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFS 195
Cdd:cd18570 102 ISRFNDANK-IREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 196 GLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGTL 275
Cdd:cd18570 181 SYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQL 260
|
250 260 270
....*....|....*....|....*....|....
gi 616431502 276 IAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18570 261 IAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
348-568 |
9.25e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 104.02 E-value: 9.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEI-----ESGDIKYGLESVYDI-PLSKWRRKIGYVMQSNSMM 421
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 422 SGTIRDNILYGINRH--VSDEEL--INYAKLANchdfIMQFDEGYDTLvGERGLKLSGGQRQRIDIARSFVKNPDILLLD 497
Cdd:PRK14271 114 PMSIMDNVLAGVRAHklVPRKEFrgVAQARLTE----VGLWDAVKDRL-SDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 498 EATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQ--IIFLDkGQVTGKGTHSELMAS--HAKYKNFV 568
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDraALFFD-GRLVEEGPTEQLFSSpkHAETARYV 262
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
351-548 |
1.12e-24 |
|
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: 102.10 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIP---LSKWRRKIGYVMQSNSMMSG-TIR 426
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKIGVVFQDFRLLPDrNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 427 DNILYG----------INRHVSDE-ELINYAKLAncHDFIMQfdegydtlvgerglkLSGGQRQRIDIARSFVKNPDILL 495
Cdd:cd03292 97 ENVAFAlevtgvppreIRKRVPAAlELVGLSHKH--RALPAE---------------LSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 496 LDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQ--IIFLDKGQV 548
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
339-549 |
1.22e-24 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 101.56 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 339 EHVDFKY-DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlesVYDIPLSKWRRKIGYVMQS 417
Cdd:cd03226 3 ENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN---GKPIKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 418 --NSMMSGTIRDNILYGinrhvsDEELINYAKLANChdfIMQfDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILL 495
Cdd:cd03226 80 vdYQLFTDSVREELLLG------LKELDAGNEQAET---VLK-DLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 496 LDEATANLDSESELKIQEALETLM-EGRTTIVIAHRLSTIKK-AGQIIFLDKGQVT 549
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
335-543 |
1.24e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.48 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYV 414
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSGTIRDNIL--YGINRHVSDEelinyAKLAnchDFIMQFdEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPD 492
Cdd:PRK10247 87 AQTPTLFGDTVYDNLIfpWQIRNQQPDP-----AIFL---DDLERF-ALPDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616431502 493 ILLLDEATANLDSESELKIQEALETLMEGRTTIVI--AHRLSTIKKAGQIIFL 543
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVITL 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
336-529 |
1.44e-24 |
|
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: 102.32 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKwrRKIGYVM 415
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSMMSG-TIRDNILYGINRHVSDEELINyAKLANCHDFImqfdeGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDIL 494
Cdd:cd03300 79 QNYALFPHlTVFENIAFGLRLKKLPKAEIK-ERVAEALDLV-----QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 616431502 495 LLDEATANLDSESELKIQEALETL--MEGRTTIVIAH 529
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTH 189
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
350-548 |
1.62e-24 |
|
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: 103.40 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 350 ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIEsGDIKYGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNI 429
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 430 -LYGinrHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESE 508
Cdd:cd03289 98 dPYG---KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 616431502 509 LKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQV 548
Cdd:cd03289 175 QVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
353-560 |
1.75e-24 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 105.18 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 353 DVSFQIPQGQVSAFVGPSGSGKSTIFNLI---ERmyeIESGDIKYGLESVYD----IPLSKWRRKIGYVMQSNSM---MS 422
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEVLQDsargIFLPPHRRRIGYVFQEARLfphLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 423 gtIRDNILYGINRHVSDEELInyaklanchdfimQFDE-----GYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLD 497
Cdd:COG4148 94 --VRGNLLYGRKRAPRAERRI-------------SFDEvvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616431502 498 EATANLDSESELKIQEALETLM-EGRTTIV-IAH------RLstikkAGQIIFLDKGQVTGKGTHSELMAS 560
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRdELDIPILyVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
353-562 |
2.48e-24 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 102.72 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 353 DVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIP---LSKWRRK-IGYVMQSNSMMSG-TIRD 427
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLPHrTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 428 NILYGIN-RHVSDEELINYA----KLANCHDFImqfdegyDTLVGErglkLSGGQRQRIDIARSFVKNPDILLLDEATAN 502
Cdd:cd03294 122 NVAFGLEvQGVPRAEREERAaealELVGLEGWE-------HKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616431502 503 LDSESELKIQEALETL--MEGRTTIVIAHRLS-TIKKAGQIIFLDKGQVTGKGTHSELMASHA 562
Cdd:cd03294 191 LDPLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNPA 253
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
336-553 |
5.99e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 103.23 E-value: 5.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKK----ILDDVSFQIPQGQVSAFVGPSGSGKST---IFNLIERMyeiESGDIKYGLESVYDIP---LS 405
Cdd:COG1135 2 IELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLERP---TSGSVLVDGVDLTALSereLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 406 KWRRKIGYVMQS-NSMMSGTIRDNILY-----GINRHVSDE---ELINyaklanchdfimqfdegydtLVGERGLK---- 472
Cdd:COG1135 79 AARRKIGMIFQHfNLLSSRTVAENVALpleiaGVPKAEIRKrvaELLE--------------------LVGLSDKAdayp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 473 --LSGGQRQRIDIARSFVKNPDILLLDEATANLDSES-----EL--KIQEALetlmeGRTTIVIAHRLSTIKK-AGQIIF 542
Cdd:COG1135 139 sqLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsilDLlkDINREL-----GLTIVLITHEMDVVRRiCDRVAV 213
|
250
....*....|.
gi 616431502 543 LDKGQVTGKGT 553
Cdd:COG1135 214 LENGRIVEQGP 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
345-557 |
7.35e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 103.57 E-value: 7.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 345 YDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKwrRKIGYVMQSNSMMSG- 423
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSYALYPHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 424 TIRDNILYGINRHVSDEELINyaKLANCHDFIMQFDEgydtLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANL 503
Cdd:PRK11000 91 SVAENMSFGLKLAGAKKEEIN--QRVNQVAEVLQLAH----LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 504 DseSELKIQEALET--LME--GRTTIVIAH-RLSTIKKAGQIIFLDKGQVTGKGTHSEL 557
Cdd:PRK11000 165 D--AALRVQMRIEIsrLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
99-548 |
1.37e-23 |
|
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: 106.15 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 99 IIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGR 178
Cdd:TIGR01271 968 VLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLR 1047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 179 IMQKIStstQSEIANFSGLLGRVLTEMR-------LVKISNTERLeldnAHKNLNeiyklgLKQAKIAAVVQPISGIVML 251
Cdd:TIGR01271 1048 TSQQLK---QLESEARSPIFSHLITSLKglwtiraFGRQSYFETL----FHKALN------LHTANWFLYLSTLRWFQMR 1114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 252 LTIAIILGFGA---LEIATGAITAG------TLIAMIFYVIQLSmplINLSTLVTDYKKAVGASSRIYEIMQEPIEPTE- 321
Cdd:TIGR01271 1115 IDIIFVFFFIAvtfIAIGTNQDGEGevgiilTLAMNILSTLQWA---VNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGg 1191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 322 --ALEDSENVLIDD----------GVLSFEHVDFKY--DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEI 387
Cdd:TIGR01271 1192 ggKYQLSTVLVIENphaqkcwpsgGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST 1271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 388 EsGDIKYGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNIlyGINRHVSDEELINYAKLANCHDFIMQFDEGYDTLVG 467
Cdd:TIGR01271 1272 E-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL--DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLV 1348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 468 ERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQ 547
Cdd:TIGR01271 1349 DGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSS 1428
|
.
gi 616431502 548 V 548
Cdd:TIGR01271 1429 V 1429
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
349-560 |
1.47e-23 |
|
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: 99.43 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSK-WRRKIGYVMQSNSMMSG-TIR 426
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEiARLGIGRTFQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 427 DNILYGINRHV-----------SDEELINYAklanchDFIMQF---DEGYDTLVGErglkLSGGQRQRIDIARSFVKNPD 492
Cdd:cd03219 94 ENVMVAAQARTgsglllararrEEREARERA------EELLERvglADLADRPAGE----LSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 493 ILLLDEATANLDSESELKIQEALETL-MEGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMAS 560
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
335-528 |
1.79e-23 |
|
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: 98.32 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSkWRRKIGYV 414
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-YRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSG-TIRDNI-----LYGinRHVSDEELinyaklancHDFIMQFD-EGY-DTLVGerglKLSGGQRQRIDIARS 486
Cdd:COG4133 81 GHADGLKPElTVRENLrfwaaLYG--LRADREAI---------DEALEAVGlAGLaDLPVR----QLSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 616431502 487 FVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIA 528
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
285-568 |
1.91e-23 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 105.41 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 285 LSMPLINLSTLVTDYKKAVGASSRIYEIM-QEPIEPtealEDSENVLIDDG---VLSFEHVDFKY--DVKKILDDVSFQI 358
Cdd:TIGR00957 586 LRFPLNILPMVISSIVQASVSLKRLRIFLsHEELEP----DSIERRTIKPGegnSITVHNATFTWarDLPPTLNGITFSI 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 359 PQGQVSAFVGPSGSGKSTIFN-LIERMYEIEsGDIKYglesvydiplskwRRKIGYVMQSNSMMSGTIRDNILYG--INR 435
Cdd:TIGR00957 662 PEGALVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVHM-------------KGSVAYVPQQAWIQNDSLRENILFGkaLNE 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 436 HVSDEELINYAKLANchdfIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEAL 515
Cdd:TIGR00957 728 KYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHV 803
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 516 ---ETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMASHAKYKNFV 568
Cdd:TIGR00957 804 igpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
91-309 |
5.03e-23 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 99.47 E-value: 5.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 91 IRSVLWEHIiqlkmPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFV 170
Cdd:cd18589 76 FAAVLRQEI-----AFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 171 LIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVM 250
Cdd:cd18589 151 LVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSG 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 251 LLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18589 231 LALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
344-568 |
6.59e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.90 E-value: 6.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 344 KYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYG-LESVYDIPLSK-------WRRKIGYVM 415
Cdd:PRK11264 12 KFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGdITIDTARSLSQqkglirqLRQHVGFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QS-NSMMSGTIRDNILYG--INRHVSDEELINYAKlanchdfimqfdegydTLVGERGL---------KLSGGQRQRIDI 483
Cdd:PRK11264 92 QNfNLFPHRTVLENIIEGpvIVKGEPKEEATARAR----------------ELLAKVGLagketsyprRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 484 ARSFVKNPDILLLDEATANLDSEselKIQEALETLM----EGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELM 558
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPE---LVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
250
....*....|..
gi 616431502 559 AS--HAKYKNFV 568
Cdd:PRK11264 233 ADpqQPRTRQFL 244
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
336-560 |
8.57e-23 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 97.23 E-value: 8.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRK-IGYV 414
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSG-TIRDNILYGIN-RHVSDEELINYAKlanchDFIMQFdeGYDTLVGERGLKLSGGQRQRIDIARSFVKNPD 492
Cdd:cd03218 81 PQEASIFRKlTVEENILAVLEiRGLSKKEREEKLE-----ELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616431502 493 ILLLDEATANLDSESELKIQEALETLMEGRTTIVIA-HR----LSTIKKAgQIIFldKGQVTGKGTHSELMAS 560
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNvretLSITDRA-YIIY--EGKVLAEGTPEEIAAN 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
346-560 |
1.10e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.81 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 346 DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIK------YGLESVYDIPLSKWRRKIGYVMQS-N 418
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKvdgkvlYFGKDIFQIDAIKLRKEVGMVFQQpN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 419 SMMSGTIRDNILYGINRHVSDEELINYAKLANCHDFIMQFDEGYDTLvGERGLKLSGGQRQRIDIARSFVKNPDILLLDE 498
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616431502 499 ATANLDSESELKIQEALETLMEGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMAS 560
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
355-562 |
1.21e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 96.75 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 355 SFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKwrRKIGYVMQSNSM-MSGTIRDNILYGI 433
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQENNLfPHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 434 --NRHVSDEE---LINYAKLANCHDFImqfdegyDTLVGErglkLSGGQRQRIDIARSFVKNPDILLLDEATANLDseSE 508
Cdd:COG3840 97 rpGLKLTAEQraqVEQALERVGLAGLL-------DRLPGQ----LSGGQRQRVALARCLVRKRPILLLDEPFSALD--PA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 509 LKiQEALETLME-----GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMASHA 562
Cdd:COG3840 164 LR-QEMLDLVDElcrerGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEP 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
329-552 |
1.32e-22 |
|
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: 96.02 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 329 VLIDDGVLSFEHVDFKYDVkkilddvsfQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSkwR 408
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDL---------TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--D 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 409 RKIGYVMQSNSMMSG-TIRDNILYGINR--HVSDEELINYAKLANchdfimqfDEGYDTLVGERGLKLSGGQRQRIDIAR 485
Cdd:cd03298 70 RPVSMLFQENNLFAHlTVEQNVGLGLSPglKLTAEDRQAIEVALA--------RVGLAGLEKRLPGELSGGERQRVALAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 486 SFVKNPDILLLDEATANLDSESELKIQEALETL--MEGRTTIVIAHRLSTIKKAGQ-IIFLDKGQVTGKG 552
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
339-558 |
1.36e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.08 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 339 EHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSN 418
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 419 SMMSG-TIRDNILYGinRH--------VSDEELINYA-------KLANCHdfimqFDEgydtlvgerglkLSGGQRQRID 482
Cdd:COG4604 85 HINSRlTVRELVAFG--RFpyskgrltAEDREIIDEAiayldleDLADRY-----LDE------------LSGGQRQRAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 483 IARSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHrlsTIKKAG----QIIFLDKGQVTGKGTHSE 556
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADelGKTVVIVLH---DINFAScyadHIVAMKDGRVVAQGTPEE 222
|
..
gi 616431502 557 LM 558
Cdd:COG4604 223 II 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
336-567 |
1.95e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKST---IFNLIE--RMYEIESGDIKYGLESVYDIP-LSKWRR 409
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSllrVLNLLEtpDSGQLNIAGHQFDFSQKPSEKaIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 410 KIGYVMQS-NSMMSGTIRDNIL------YGINRHVSDE---ELINYAKLAnchDFIMQFDegydtlvgergLKLSGGQRQ 479
Cdd:COG4161 83 KVGMVFQQyNLWPHLTVMENLIeapckvLGLSKEQAREkamKLLARLRLT---DKADRFP-----------LHLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 480 RIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLME-GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSEL 557
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDASHF 228
|
250
....*....|
gi 616431502 558 maSHAKYKNF 567
Cdd:COG4161 229 --TQPQTEAF 236
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
38-309 |
2.55e-22 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 97.41 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSvSHINWN-------LIALF-----------GGIFVInallsglglyllskIGEKIIYAIRSVLWEHI 99
Cdd:cd18590 15 IPYYTGRVIDILG-GEYQHNaftsaigLMCLFslgsslsaglrGGLFMC--------------TLSRLNLRLRHQLFSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 100 IQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRI 179
Cdd:cd18590 80 VQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 180 MQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILG 259
Cdd:cd18590 160 HQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLY 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 616431502 260 FGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18590 240 CGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-549 |
2.62e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlESVydiplskwrrKIGYV 414
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG-ETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSG--TIRDNILYGiNRHVSDEELINYakLANchdfiMQFDegydtlvGERGLK----LSGGQRQRIDIARSFV 488
Cdd:COG0488 384 DQHQEELDPdkTVLDELRDG-APGGTEQEVRGY--LGR-----FLFS-------GDDAFKpvgvLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 489 KNPDILLLDEATANLDSESelkiQEALETLM---EGrTTIVIAH-R--LSTIkkAGQIIFLDKGQVT 549
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIET----LEALEEALddfPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVR 508
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
326-557 |
2.91e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.00 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 326 SENVLIDDGVLSFEHVDFKYDVK-----KILDDVSFQIPQGQVSAFVGPSGSGKSTI---FN--LIERMYEIESGDI--- 392
Cdd:PRK13631 12 VPNPLSDDIILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLvthFNglIKSKYGTIQVGDIyig 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 393 -KYGLESVYDIPLSK-------WRRKIGYVMQ--SNSMMSGTIRDNILYG-INRHVSDEELinyAKLANCHDFIMQFDEG 461
Cdd:PRK13631 92 dKKNNHELITNPYSKkiknfkeLRRRVSMVFQfpEYQLFKDTIEKDIMFGpVALGVKKSEA---KKLAKFYLNKMGLDDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 462 YDtlvgERG-LKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQE-ALETLMEGRTTIVIAHRLSTI-KKAG 538
Cdd:PRK13631 169 YL----ERSpFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQlILDAKANNKTVFVITHTMEHVlEVAD 244
|
250
....*....|....*....
gi 616431502 539 QIIFLDKGQVTGKGTHSEL 557
Cdd:PRK13631 245 EVIVMDKGKILKTGTPYEI 263
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
338-549 |
2.95e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 338 FEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkyglesvydiplskWRRK---IGYV 414
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------------SIPKglrIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSG-TIRDNILYGINRHVSDEELIN--YAKLANCHDFIMQFDE---------GY-------------------- 462
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELRALEAELEelEAKLAEPDEDLERLAElqeefealgGWeaearaeeilsglgfpeedl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 463 DTLVGErglkLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESelkIqEALETLMEGR--TTIVIAH-R--LSTIkkA 537
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---I-EWLEEFLKNYpgTVLVVSHdRyfLDRV--A 216
|
250
....*....|..
gi 616431502 538 GQIIFLDKGQVT 549
Cdd:COG0488 217 TRILELDRGKLT 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
336-557 |
3.12e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 98.30 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIermyeiesgdikYGLES-----------VYDIPL 404
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII------------AGLETpdsgrivlngrDLFTNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 405 SKWRRKIGYVMQSNS----MmsgTIRDNILYGI-NRHVSDEElinyaKLANCHDFImqfdegydTLVGERGLK------L 473
Cdd:COG1118 71 PPRERRVGFVFQHYAlfphM---TVAENIAFGLrVRPPSKAE-----IRARVEELL--------ELVQLEGLAdrypsqL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 474 SGGQRQRIDIARSFVKNPDILLLDEATANLDSeselKIQEALET-LME-----GRTTIVIAH------RLstikkAGQII 541
Cdd:COG1118 135 SGGQRQRVALARALAVEPEVLLLDEPFGALDA----KVRKELRRwLRRlhdelGGTTVFVTHdqeealEL-----ADRVV 205
|
250
....*....|....*.
gi 616431502 542 FLDKGQVTGKGTHSEL 557
Cdd:COG1118 206 VMNQGRIEQVGTPDEV 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
345-529 |
3.76e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.06 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 345 YDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIE-----SGDIKYGLESVY--DIPLSKWRRKIGYVMQ- 416
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYspDVDPIEVRREVGMVFQy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 417 SNSMMSGTIRDNILYGI--NRHV-SDEELINYAKLANCHDFImqFDEGYDTLVGERGlKLSGGQRQRIDIARSFVKNPDI 493
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVklNGLVkSKKELDERVEWALKKAAL--WDEVKDRLNDYPS-NLSGGQRQRLVIARALAMKPKI 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 616431502 494 LLLDEATANLDSESELKIQEALETLMEGRTTIVIAH 529
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
351-556 |
4.14e-22 |
|
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: 95.48 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKwrRKIGYVMQSNSMMSG-TIRDNI 429
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 430 LYGI-----NRHVSDEELINYAKLAnchdfimqfdeGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLD 504
Cdd:cd03299 93 AYGLkkrkvDKKEIERKVLEIAEML-----------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 505 SESELKIQEALETLME--GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSE 556
Cdd:cd03299 162 VRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
336-559 |
4.31e-22 |
|
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: 94.81 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSK-WRRKIGYV 414
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSG-TIRDNILYGINRHVSDEELINYAKLanchdFIM--QFDEGYDTLVGErglkLSGGQRQRIDIARSFVKNP 491
Cdd:cd03224 81 PEGRRIFPElTVEENLLLGAYARRRAKRKARLERV-----YELfpRLKERRKQLAGT----LSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 492 DILLLDEATANLdseSEL---KIQEALETLMEGRTTIV-----------IAHRLstikkagqiIFLDKGQVTGKGTHSEL 557
Cdd:cd03224 152 KLLLLDEPSEGL---APKiveEIFEAIRELRDEGVTILlveqnarfaleIADRA---------YVLERGRVVLEGTAAEL 219
|
..
gi 616431502 558 MA 559
Cdd:cd03224 220 LA 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
336-555 |
6.17e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 95.08 E-value: 6.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKST---IFNLIE--RMYEIESGDIKYGLESVYDIP-LSKWRR 409
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLEmpRSGTLNIAGNHFDFSKTPSDKaIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 410 KIGYVMQS-NSMMSGTIRDNILYGINR--HVSDEELINYAK--LANCH--DFIMQFDegydtlvgergLKLSGGQRQRID 482
Cdd:PRK11124 83 NVGMVFQQyNLWPHLTVQQNLIEAPCRvlGLSKDQALARAEklLERLRlkPYADRFP-----------LHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 483 IARSFVKNPDILLLDEATANLDSESELKIQEALETLME-GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHS 555
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
348-556 |
6.97e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.88 E-value: 6.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYD--IPLSKWRRKIGYVMQ--SNSMMSG 423
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 424 TIRDNILYG-INRHVSDEELINYAKLANChdfIMQFDegYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATAN 502
Cdd:PRK13637 100 TIEKDIAFGpINLGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 503 LDSESELKIQEALETLME--GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSE 556
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
340-541 |
1.05e-21 |
|
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: 96.28 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 340 HVDFKYDVK--KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYE---IESGDIKYGLESVYDIPLSKWR----RK 410
Cdd:COG0444 8 KVYFPTRRGvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRkirgRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 411 IGYVMQsNSMMS----GTIRDNILYGINRH--VSDEELINYAK--LAnchdfimqfdegydtLVG----ERGLK-----L 473
Cdd:COG0444 88 IQMIFQ-DPMTSlnpvMTVGDQIAEPLRIHggLSKAEARERAIelLE---------------RVGlpdpERRLDrypheL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 474 SGGQRQRIDIARSFVKNPDILLLDEATANLD-SeselkIQ-EALETLME-----GRTTIVIAHRLSTIKK---------A 537
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDvT-----IQaQILNLLKDlqrelGLAILFITHDLGVVAEiadrvavmyA 226
|
....
gi 616431502 538 GQII 541
Cdd:COG0444 227 GRIV 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
335-560 |
2.19e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 94.39 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKY----DVKKiLDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRK 410
Cdd:PRK13642 4 ILEVENLVFKYekesDVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 411 IGYVMQS--NSMMSGTIRDNILYGI-NRHVSDEELINYAKLANCHDFIMQFDEgydtlvgERGLKLSGGQRQRIDIARSF 487
Cdd:PRK13642 83 IGMVFQNpdNQFVGATVEDDVAFGMeNQGIPREEMIKRVDEALLAVNMLDFKT-------REPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 488 VKNPDILLLDEATANLDSESELKIQEALETLMEGR--TTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMAS 560
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFAT 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
336-552 |
2.58e-21 |
|
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: 92.28 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYgLESVYDIPLSKWRRkIGYVM 415
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF-DGKSYQKNIEALRR-IGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSM---MSGtiRDNI-----LYGInRHVSDEELINYAKLANCHDfimqfdegydtlvgERGLKLSGGQRQRIDIARSF 487
Cdd:cd03268 79 EAPGFypnLTA--RENLrllarLLGI-RKKRIDEVLDVVGLKDSAK--------------KKVKGFSLGMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 488 VKNPDILLLDEATANLDSESELKIQEALETLM-EGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKG 552
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
38-309 |
3.48e-21 |
|
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: 94.11 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVD---KFSVSHINWNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQ 114
Cdd:cd18555 21 IPILTQYVIDnviVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 115 LMSRLTDDTkVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANF 194
Cdd:cd18555 101 LLFRANSNV-YIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 195 SGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGT 274
Cdd:cd18555 180 QSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGE 259
|
250 260 270
....*....|....*....|....*....|....*
gi 616431502 275 LIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18555 260 LIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
344-552 |
4.35e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 92.40 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 344 KYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDiPLSKWRRKIGYVMQSNSMMSG 423
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVFGQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 424 TIRDNILYGINRHVSDEELINYAK-LANCHDfIMQFDEGYDTLVgergLKLSGGQRQRIDIARSFVKNPDILLLDEATAN 502
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPARFKKrLDELSE-LLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616431502 503 LDSESELKIQEALETLMEGRTTIVI--AHRLSTIKK-AGQIIFLDKGQVTGKG 552
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
83-297 |
4.59e-21 |
|
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: 94.02 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 83 IGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLT 162
Cdd:cd18554 73 IANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 163 FITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVV 242
Cdd:cd18554 153 LVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKT 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 243 QPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMP---LINLSTLVT 297
Cdd:cd18554 233 FSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPlrrLVNSFTTLT 290
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
349-552 |
5.13e-21 |
|
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: 91.66 E-value: 5.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKY-GLESVYDiPLSKwRRKIGYVMQSNSMMSG-TIR 426
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVVKE-PAEA-RRRLGFVSDSTGLYDRlTAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 427 DNI-----LYGINRHVSDEELINYAKLanchdfiMQFDEgydtLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATA 501
Cdd:cd03266 97 ENLeyfagLYGLKGDELTARLEELADR-------LGMEE----LLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616431502 502 NLDSESELKIQEALETLMEGRTTIVIA-HRLSTIKK-AGQIIFLDKGQVTGKG 552
Cdd:cd03266 166 GLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
39-295 |
7.64e-21 |
|
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: 93.01 E-value: 7.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 39 PLFTGRIVDKfSVSHINWNLIALFGGIFVI----NALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQ 114
Cdd:cd18568 22 PLFTQIILDR-VLVHKNISLLNLILIGLLIvgifQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 115 LMSRLTDDTKVINeFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANF 194
Cdd:cd18568 101 IITRFQENQKIRR-FLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 195 SGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGT 274
Cdd:cd18568 180 QSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQ 259
|
250 260
....*....|....*....|....
gi 616431502 275 LIA---MIFYVIQlsmPLINLSTL 295
Cdd:cd18568 260 LVAfnmLFGSVIN---PLLALVGL 280
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
83-309 |
8.88e-21 |
|
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: 92.99 E-value: 8.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 83 IGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDtkvINEF-------ISQKlpnlLPSIVTLVGSLIMLFILD 155
Cdd:cd18574 69 VGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTAD---VQEFkssfkqcVSQG----LRSVTQTVGCVVSLYLIS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 156 WKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQ 235
Cdd:cd18574 142 PKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 236 AKIAAVVQPIS-----GIVMlltiaIILGFGALEIATGAITAGTLiaMIFYV----IQLSmpLINLSTLVTDYKKAVGAS 306
Cdd:cd18574 222 GLGIGIFQGLSnlalnGIVL-----GVLYYGGSLVSRGELTAGDL--MSFLVatqtIQRS--LAQLSVLFGQYVKGKSAG 292
|
...
gi 616431502 307 SRI 309
Cdd:cd18574 293 ARV 295
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
349-532 |
1.07e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 93.26 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIP---LSKWRRKIGYVMQ----S-NSM 420
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQdpyaSlNPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 421 MsgTIRDNILYG--INRHVSDEELINYAKlanchdfimqfdegydTLVGERGLK----------LSGGQRQRIDIARSFV 488
Cdd:COG4608 112 M--TVGDIIAEPlrIHGLASKAERRERVA----------------ELLELVGLRpehadrypheFSGGQRQRIGIARALA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 616431502 489 KNPDILLLDEATANLDseseLKIQEALETLME------GRTTIVIAHRLS 532
Cdd:COG4608 174 LNPKLIVCDEPVSALD----VSIQAQVLNLLEdlqdelGLTYLFISHDLS 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
367-559 |
2.49e-20 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 92.17 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 367 VGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPlsKWRRKIGYVMQSNSMMSG-TIRDNILYGIN-RHVSDEEL-- 442
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP--PHLRHINMVFQSYALFPHmTVEENVAFGLKmRKVPRAEIkp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 443 -INYA-KLANCHDFimqfdegydtlVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLME 520
Cdd:TIGR01187 80 rVLEAlRLVQLEEF-----------ADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 616431502 521 --GRTTIVIAHRLS-TIKKAGQIIFLDKGQVTGKGTHSELMA 559
Cdd:TIGR01187 149 qlGITFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
338-559 |
2.55e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 91.62 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 338 FEHVDFKYDVK-----KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLE----SVYDIPLSKWR 408
Cdd:PRK13634 5 FQKVEHRYQYKtpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitaGKKNKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 409 RKIGYVMQ--SNSMMSGTIRDNILYG-INRHVSDEELINYAKLanchdfiMQFDEGYDTLVGERG-LKLSGGQRQRIDIA 484
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETVEKDICFGpMNFGVSEEDAKQKARE-------MIELVGLPEELLARSpFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 485 RSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMA 559
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
350-549 |
2.76e-20 |
|
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: 89.80 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 350 ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLI---ERmyeIESGDIKyglesVYDIPLSKW---------RRKIGYVMQS 417
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVR-----LAGQDLFALdedararlrARHVGFVFQS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 418 ----NSMmsgTIRDNILYGinrhvsdeelinyAKLANCHDfimQFDEGYDTL----VGERgLK-----LSGGQRQRIDIA 484
Cdd:COG4181 99 fqllPTL---TALENVMLP-------------LELAGRRD---ARARARALLervgLGHR-LDhypaqLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 485 RSFVKNPDILLLDEATANLDSESELKIQEALETLMEGR-TTIVIA-HRLSTIKKAGQIIFLDKGQVT 549
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVLVtHDPALAARCDRVLRLRAGRLV 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
335-560 |
4.73e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.02 E-value: 4.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESvydIP--LSKWRRKIG 412
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEP---VPsrARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 413 YVMQSNSMMSG-TIRDNIL-----YGINRHVSDE---ELINYAKLANchdfimqfdeGYDTLVGErglkLSGGQRQRIDI 483
Cdd:PRK13537 84 VVPQFDNLDPDfTVRENLLvfgryFGLSAAAARAlvpPLLEFAKLEN----------KADAKVGE----LSGGMKRRLTL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 484 ARSFVKNPDILLLDEATANLDSESELKIQEALETLM-EGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMAS 560
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
82-309 |
5.85e-20 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 90.80 E-value: 5.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 82 KIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLL 161
Cdd:cd18558 85 LAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 162 TFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAV 241
Cdd:cd18558 165 ILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNI 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 242 VQPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18558 245 SMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
349-559 |
6.52e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 89.33 E-value: 6.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKY------GLeSVYDIplskWRRKIGYVMQSNSMMS 422
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFdgrditGL-PPHRI----ARLGIARTFQNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 423 G-TIRDNILYGINRHVSD-----------------------EELINYAKLANCHdfimqfdegyDTLVGErglkLSGGQR 478
Cdd:COG0411 93 ElTVLENVLVAAHARLGRgllaallrlprarreereareraEELLERVGLADRA----------DEPAGN----LSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 479 QRIDIARSFVKNPDILLLDEATANLdSESElkIQEALETLME-----GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKG 552
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGL-NPEE--TEELAELIRRlrderGITILLIEHDMDLVMGlADRIVVLDFGRVIAEG 235
|
....*..
gi 616431502 553 THSELMA 559
Cdd:COG0411 236 TPAEVRA 242
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
351-546 |
1.01e-19 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 88.16 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDI----KYGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIR 426
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 427 DNILYG--INRHvSDEELINYAKLANCHDFIMQFDEgydTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLD 504
Cdd:cd03290 97 ENITFGspFNKQ-RYKAVTDACSLQPDIDLLPFGDQ---TEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 616431502 505 SE-SELKIQEALETLM--EGRTTIVIAHRLSTIKKAGQIIFLDKG 546
Cdd:cd03290 173 IHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
331-548 |
1.39e-19 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 87.61 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 331 IDDGVLSFEHVDFKYDVkkilddvsfQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKygLESVYDIPLSKWRRK 410
Cdd:TIGR01277 3 LDKVRYEYEHLPMEFDL---------NVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIK--VNDQSHTGLAPYQRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 411 IGYVMQSNSMMSG-TIRDNILYGINRHVSdeelINYAKLANCHDFIMQFdeGYDTLVGERGLKLSGGQRQRIDIARSFVK 489
Cdd:TIGR01277 72 VSMLFQENNLFAHlTVRQNIGLGLHPGLK----LNAEQQEKVVDAAQQV--GIADYLDRLPEQLSGGQRQRVALARCLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 490 NPDILLLDEATANLDSeselKIQEALETLM------EGRTTIVIAHRLS-TIKKAGQIIFLDKGQV 548
Cdd:TIGR01277 146 PNPILLLDEPFSALDP----LLREEMLALVkqlcseRQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
351-563 |
3.82e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 89.09 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYG---LESVYDIPLSKWRRKIGYVMQS-NSMMSGTIR 426
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDgqdLTALSEKELRKARRQIGMIFQHfNLLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 427 DNI-----LYG-----INRHVsdEELINYAKLANCHDFimqfdegYDTlvgerglKLSGGQRQRIDIARSFVKNPDILLL 496
Cdd:PRK11153 101 DNValpleLAGtpkaeIKARV--TELLELVGLSDKADR-------YPA-------QLSGGQKQRVAIARALASNPKVLLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 497 DEATANLDSES-----EL--KIQEALetlmeGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMAsHAK 563
Cdd:PRK11153 165 DEATSALDPATtrsilELlkDINREL-----GLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEVFS-HPK 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
336-529 |
4.81e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.06 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlesvyDIPLSKWRRKIGYVM 415
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLD-----GKPVEGPGAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSMMS-GTIRDNILYGIN-RHVSDEElinyaKLANCHDFIMQFD-EGYDTlvgERGLKLSGGQRQRIDIARSFVKNPD 492
Cdd:PRK11248 77 QNEGLLPwRNVQDNVAFGLQlAGVEKMQ-----RLEIAHQMLKKVGlEGAEK---RYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 616431502 493 ILLLDEATANLDSESELKIQEALETLME--GRTTIVIAH 529
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH 187
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
336-529 |
5.17e-19 |
|
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: 83.65 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLesvydiplskwRRKIGYVM 415
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QsnsmmsgtirdnilyginrhvsdeelinyaklanchdfimqfdegydtlvgerglkLSGGQRQRIDIARSFVKNPDILL 495
Cdd:cd03221 70 Q--------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....
gi 616431502 496 LDEATANLDSESELKIQEALETLmeGRTTIVIAH 529
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSH 125
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
335-559 |
5.50e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.49 E-value: 5.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPL-SKWRRKIGY 413
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 414 VMQSNSMMSG-TIRDNIL--YGINRHVSDEELINYAKlanchDFIMQFDEGYdtLVGERGLKLSGGQRQRIDIARSFVKN 490
Cdd:PRK10895 83 LPQEASIFRRlSVYDNLMavLQIRDDLSAEQREDRAN-----ELMEEFHIEH--LRDSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616431502 491 PDILLLDEATANLDSESELKIQEALETLME-GRTTIVIAHRL-STIKKAGQIIFLDKGQVTGKGTHSELMA 559
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
350-553 |
5.56e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.41 E-value: 5.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 350 ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKY---GLESVYDIPLSKWR-RKIGYVMQSNSMMSG-T 424
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFngqPMSKLSSAAKAELRnQKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 425 IRDNILYGInrhvsdeeLINYAKLANCHD--FIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATAN 502
Cdd:PRK11629 104 ALENVAMPL--------LIGKKKPAEINSraLEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 616431502 503 LDSESELKIQEALETL--MEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGT 553
Cdd:PRK11629 176 LDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
335-565 |
1.20e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 86.70 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlesvyDIPLSKW-RRKIGY 413
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD-----GEPLDPEdRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 414 V---------MqsnsmmsgTIRDNILY-----GINRHVSDEELINYAKlanchdfimQFDegydtlVGERGLK----LSG 475
Cdd:COG4152 76 LpeerglypkM--------KVGEQLVYlarlkGLSKAEAKRRADEWLE---------RLG------LGDRANKkveeLSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 476 GQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLME-GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGT 553
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
250
....*....|..
gi 616431502 554 HSELMASHAKYK 565
Cdd:COG4152 213 VDEIRRQFGRNT 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
336-550 |
1.44e-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: 82.86 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESV-YDIPLSKWRRKIGYV 414
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVsFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQsnsmmsgtirdnilyginrhvsdeelinyaklanchdfimqfdegydtlvgerglkLSGGQRQRIDIARSFVKNPDIL 494
Cdd:cd03216 81 YQ--------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 495 LLDEATANL-DSESE--LKIQEALETlmEGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTG 550
Cdd:cd03216 105 ILDEPTAALtPAEVErlFKVIRRLRA--QGVAVIFISHRLDEVFEiADRVTVLRDGRVVG 162
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
348-548 |
1.53e-18 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 85.63 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSK---WRRKIGYVMQS-----NS 419
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDspsavNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 420 MMsgTIRDNILYGINRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGErglkLSGGQRQRIDIARSFVKNPDILLLDEA 499
Cdd:TIGR02769 104 RM--TVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ----LSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 616431502 500 TANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKK-AGQIIFLDKGQV 548
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQI 229
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
112-560 |
1.75e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 89.80 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 112 SGQLMSRLTDDTKVINEfISQKLPNLLPSIVTLVGSLIMLFildWKMTLLTFITIPIFVLiMIPLGRI----MQKISTST 187
Cdd:PLN03130 397 SGKITNLMTTDAEALQQ-ICQQLHTLWSAPFRIIIAMVLLY---QQLGVASLIGSLMLVL-MFPIQTFiiskMQKLTKEG 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 188 QSEIANFSGLLGRVLTEMRLVKI---SNTERLELDNAHKN-LNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGAL 263
Cdd:PLN03130 472 LQRTDKRIGLMNEVLAAMDTVKCyawENSFQSKVQTVRDDeLSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 264 EIATGAITAGTLIAMifyviqLSMPLINLSTLVTDYKKAVGASSRIYEIM--QE-------PIEPTEAledseNVLIDDG 334
Cdd:PLN03130 552 LTPARAFTSLSLFAV------LRFPLFMLPNLITQAVNANVSLKRLEELLlaEErvllpnpPLEPGLP-----AISIKNG 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFehvDFKYDvKKILDDVSFQIPQGQVSAFVGPSGSGK-STIFNLIERMYEIESGDIKYglesvydiplskwRRKIGY 413
Cdd:PLN03130 621 YFSW---DSKAE-RPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVI-------------RGTVAY 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 414 VMQSNSMMSGTIRDNILYGINRHVSD-EELINYAKLAncHDfiMQFDEGYD-TLVGERGLKLSGGQRQRIDIARSFVKNP 491
Cdd:PLN03130 684 VPQVSWIFNATVRDNILFGSPFDPERyERAIDVTALQ--HD--LDLLPGGDlTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 492 DILLLDEATANLDSESELKI-QEALETLMEGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGTHSELMAS 560
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
349-520 |
1.82e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.06 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDipLSKWRRKIGYVMQSNSM---MsgTI 425
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARDRKVGFVFQHYALfrhM--TV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 426 RDNILYGI---------NRHVSDE------ELINYAKLANchDFIMQfdegydtlvgerglkLSGGQRQRIDIARSFVKN 490
Cdd:PRK10851 92 FDNIAFGLtvlprrerpNAAAIKAkvtqllEMVQLAHLAD--RYPAQ---------------LSGGQKQRVALARALAVE 154
|
170 180 190
....*....|....*....|....*....|
gi 616431502 491 PDILLLDEATANLDSESELKIQEALETLME 520
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHE 184
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
343-552 |
2.00e-18 |
|
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: 84.51 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 343 FKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYglesvydiplskwRRKIGYVMQSNSMMS 422
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-------------RGRVSSLLGLGGGFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 423 G--TIRDNI-----LYGINRHVSDEELinyaklanchDFIMQFDE-G--YDTLVGErglkLSGGQRQRIDIARSFVKNPD 492
Cdd:cd03220 97 PelTGRENIylngrLLGLSRKEIDEKI----------DEIIEFSElGdfIDLPVKT----YSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616431502 493 ILLLDEATANLDSESELKIQEALETLMEGRTTIVIA-HRLSTIKK-AGQIIFLDKGQVTGKG 552
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
345-529 |
2.03e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.81 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 345 YDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkygleSVYDIPLSKW----RRKIGYVMQSNSM 420
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI-----TVLGVPVPARarlaRARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 421 -MSGTIRDNIL-YGINRHVSDEE-------LINYAKLANchdfimqfdeGYDTLVGErglkLSGGQRQRIDIARSFVKNP 491
Cdd:PRK13536 126 dLEFTVRENLLvFGRYFGMSTREieavipsLLEFARLES----------KADARVSD----LSGGMKRRLTLARALINDP 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 616431502 492 DILLLDEATANLDSESELKIQEALETLM-EGRTTIVIAH 529
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTH 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
336-548 |
2.14e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.65 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDV-----KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVY----DIPLSK 406
Cdd:PRK13641 3 IKFENVDYIYSPgtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 407 WRRKIGYVMQ--SNSMMSGTIRDNILYG-INRHVSDEELINYAKlanchDFIMQFdeGYDTLVGERG-LKLSGGQRQRID 482
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpKNFGFSEDEAKEKAL-----KWLKKV--GLSEDLISKSpFELSGGQMRRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 483 IARSFVKNPDILLLDEATANLDSESELKIQEA-LETLMEGRTTIVIAHRLSTIKK-AGQIIFLDKGQV 548
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
336-562 |
2.26e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.40 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDI---KYGLESVYDIPLSKWRRK-I 411
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidGVDIAKISDAELREVRRKkI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 412 GYVMQSNSMMSG-TIRDNILYGIN-RHVSDEELINYAKLANCHDFIMQFDEGYDTlvgerglKLSGGQRQRIDIARSFVK 489
Cdd:PRK10070 109 AMVFQSFALMPHmTVLDNTAFGMElAGINAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 490 NPDILLLDEATANLDSESELKIQEALETLM--EGRTTIVIAHRLSTIKKAG-QIIFLDKGQVTGKGTHSELMASHA 562
Cdd:PRK10070 182 NPDILLMDEAFSALDPLIRTEMQDELVKLQakHQRTIVFISHDLDEAMRIGdRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
345-557 |
2.82e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.81 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 345 YDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPlsKWRRKIGYVMQSNSMMSG- 423
Cdd:PRK11607 29 FDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSYALFPHm 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 424 TIRDNILYGINR-HVSDEELINYAK--LANCHdfiMQfdegydTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEAT 500
Cdd:PRK11607 107 TVEQNIAFGLKQdKLPKAEIASRVNemLGLVH---MQ------EFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 501 ANLDSESELKIQEALETLME--GRTTIVIAH-RLSTIKKAGQIIFLDKGQVTGKGTHSEL 557
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
348-567 |
3.69e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.22 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVY----DIPLSKWRRKIGYVMQ--SNSMM 421
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRPVRKRIGMVFQfpESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 422 SGTIRDNILYG-INRHVSDEELINYAklancHDFIMQFDEGYDTLvGERGLKLSGGQRQRIDIARSFVKNPDILLLDEAT 500
Cdd:PRK13646 100 EDTVEREIIFGpKNFKMNLDEVKNYA-----HRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 501 ANLDSESELKIQEALETLM--EGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMASHAKYKNF 567
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
333-533 |
3.80e-18 |
|
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: 87.68 E-value: 3.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 333 DGVLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlESVydiplskwrrKIG 412
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG-ETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 413 YVMQSNSMMSG--TIRDNILYGinrhvSDEELINYAKLaNCHDFIMQFD-EGYD--TLVGErglkLSGGQRQRIDIARSF 487
Cdd:TIGR03719 389 YVDQSRDALDPnkTVWEEISGG-----LDIIKLGKREI-PSRAYVGRFNfKGSDqqKKVGQ----LSGGERNRVHLAKTL 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 616431502 488 VKNPDILLLDEATANLDSESELKIQEALETLmeGRTTIVIAH------RLST 533
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
336-515 |
7.10e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 83.76 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKK----ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkygleSVYDIPLSKWRRKI 411
Cdd:COG4525 4 LTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI-----TLDGVPVTGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 412 GYVMQSNSMMSG-TIRDNILYG--------INRHVSDEELINYAKLANCHD-FIMQfdegydtlvgerglkLSGGQRQRI 481
Cdd:COG4525 79 GVVFQKDALLPWlNVLDNVAFGlrlrgvpkAERRARAEELLALVGLADFARrRIWQ---------------LSGGMRQRV 143
|
170 180 190
....*....|....*....|....*....|....
gi 616431502 482 DIARSFVKNPDILLLDEATANLDSESELKIQEAL 515
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELL 177
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
351-529 |
1.04e-17 |
|
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: 82.48 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLE---------SVYDIpLSKWRRKIGYVMQsnsmm 421
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlaqaSPREI-LALRRRTIGYVSQ----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 422 sgtirdnILYGINRhVSdeelinyaklanCHDFIMQ--FDEGYDTLVG-ERGLKL------------------SGGQRQR 480
Cdd:COG4778 101 -------FLRVIPR-VS------------ALDVVAEplLERGVDREEArARARELlarlnlperlwdlppatfSGGEQQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 616431502 481 IDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIV-IAH 529
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
335-557 |
1.28e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYD-----VKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKW-- 407
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 408 --RRKIGYVMQ--SNSMMSGTIRDNILYGI-NRHVSDEELINYAklANCHDFIMQFDEGYDtlvgERGLKLSGGQRQRID 482
Cdd:PRK13643 81 pvRKKVGVVFQfpESQLFEETVLKDVAFGPqNFGIPKEKAEKIA--AEKLEMVGLADEFWE----KSPFELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 483 IARSFVKNPDILLLDEATANLDSESELKIQEALETLME-GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSEL 557
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDV 231
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
334-546 |
2.04e-17 |
|
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: 80.75 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 334 GVLSFEHVDFKYDVKK----ILDDVSFQIPQGQVSAFVGPSGSGKSTIFN-LIERMyeiESGDIKyGLESVYDIPLSK-W 407
Cdd:cd03232 2 SVLTWKNLNYTVPVKGgkrqLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRK---TAGVIT-GEILINGRPLDKnF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 408 RRKIGYVMQSNSMMSG-TIRDNILYGinrhvsdeelinyAKLanchdfimqfdegydtlvgeRGLKLSggQRQRIDIARS 486
Cdd:cd03232 78 QRSTGYVEQQDVHSPNlTVREALRFS-------------ALL--------------------RGLSVE--QRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616431502 487 FVKNPDILLLDEATANLDSESELKIQEALETL-MEGRTTIVIAHRLS--TIKKAGQIIFLDKG 546
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
332-559 |
2.09e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.59 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 332 DDGVLSFEHVDFKY-DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESV-YDIP-LSKWR 408
Cdd:PRK13636 2 EDYILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdYSRKgLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 409 RKIGYVMQS--NSMMSGTIRDNILYG-INRHVSDEELINYAklanchDFIMQfDEGYDTLVGERGLKLSGGQRQRIDIAR 485
Cdd:PRK13636 82 ESVGMVFQDpdNQLFSASVYQDVSFGaVNLKLPEDEVRKRV------DNALK-RTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 486 SFVKNPDILLLDEATANLDSESELKIQEAL-ETLMEGRTTIVIA-HRLSTIK-KAGQIIFLDKGQVTGKGTHSELMA 559
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLvEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
344-560 |
2.10e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 344 KYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDI------------KYGLESVYDI-PLSKWRRK 410
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtinlvrdKDGQLKVADKnQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 411 IGYVMQSNSMMSG-TIRDNIL------YGINRHVSDEELINY-AKLAnchdfimqFDEGYDtlvGERGLKLSGGQRQRID 482
Cdd:PRK10619 94 LTMVFQHFNLWSHmTVLENVMeapiqvLGLSKQEARERAVKYlAKVG--------IDERAQ---GKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 483 IARSFVKNPDILLLDEATANLDSE---SELKIQEALETlmEGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELM 558
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAE--EGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
..
gi 616431502 559 AS 560
Cdd:PRK10619 241 GN 242
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
336-545 |
2.59e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 79.51 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKY-DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkyglesvyDIPlskWRRKIGYV 414
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMP---EGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSGTIRDNILYGINRhvsdeelinyaklanchdfimqfdegydtlvgerglKLSGGQRQRIDIARSFVKNPDIL 494
Cdd:cd03223 70 PQRPYLPLGTLREQLIYPWDD------------------------------------VLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 616431502 495 LLDEATANLDSESELKIQEALETlmEGRTTIVIAHRLSTIKKAGQIIFLDK 545
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
351-552 |
4.08e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkygleSVYDIPLSKWRRK--IGYVMQSNSM---MSGTI 425
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQKnlVAYVPQSEEVdwsFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 426 RDNILYGINRHVS--------DEELINYAkLANchdfiMQFDEGYDTLVGErglkLSGGQRQRIDIARSFVKNPDILLLD 497
Cdd:PRK15056 98 EDVVMMGRYGHMGwlrrakkrDRQIVTAA-LAR-----VDMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 498 EATANLDSESELKIQEALETLM-EGRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKG 552
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
323-535 |
4.17e-17 |
|
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: 84.80 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 323 LEDSENVLIDDGVLSFEHVDFKYDVKKIL-DDVSFQIPQGQVSAFVGPSGSGKSTIFNLIErmyeiesgdikyGLESVYD 401
Cdd:TIGR00954 439 VPGRGIVEYQDNGIKFENIPLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILG------------ELWPVYG 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 402 IPLSKWRR-KIGYVMQSNSMMSGTIRDNILYG------INRHVSDEELINYAKLANCHDfIMQFDEGYDTLVGERGLkLS 474
Cdd:TIGR00954 507 GRLTKPAKgKLFYVPQRPYMTLGTLRDQIIYPdssedmKRRGLSDKDLEQILDNVQLTH-ILEREGGWSAVQDWMDV-LS 584
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616431502 475 GGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLmeGRTTIVIAHRLSTIK 535
Cdd:TIGR00954 585 GGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWK 643
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
336-548 |
4.21e-17 |
|
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: 80.02 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPlskwRRKIGYVM 415
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSMMSG-TIRDNILY-----GINRHvsdeelinYAKlANCHDFIMQFD-EGYDTLVGErglKLSGGQRQRIDIARSFV 488
Cdd:cd03269 77 EERGLYPKmKVIDQLVYlaqlkGLKKE--------EAR-RRIDEWLERLElSEYANKRVE---ELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616431502 489 KNPDILLLDEATANLDSESELKIQEALETLME-GRTTIVIAHRLSTIKK-AGQIIFLDKGQV 548
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARaGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
335-560 |
4.46e-17 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 80.80 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESV-----YDIPlskwRR 409
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglppHRIA----RL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 410 KIGYVMQSNSMMSG-TIRDNILYGInRHVSDEELINyaklanchdfiMQFDEGYDT--LVGER----GLKLSGGQRQRID 482
Cdd:COG0410 79 GIGYVPEGRRIFPSlTVEENLLLGA-YARRDRAEVR-----------ADLERVYELfpRLKERrrqrAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 483 IARSFVKNPDILLLDEATANL-----DseselKIQEALETLMEGRTTIVI----AHRLSTIkkAGQIIFLDKGQVTGKGT 553
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLaplivE-----EIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGT 219
|
....*..
gi 616431502 554 HSELMAS 560
Cdd:COG0410 220 AAELLAD 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
326-510 |
6.89e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.69 E-value: 6.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 326 SENVLIDDGVLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLS 405
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 406 KwrRKIGYVMQSNSM---MsgTIRDNILYG----------INRHVSDeelinyaKLAnchdfIMQFDEgydtLVGERGLK 472
Cdd:PRK09452 85 N--RHVNTVFQSYALfphM--TVFENVAFGlrmqktpaaeITPRVME-------ALR-----MVQLEE----FAQRKPHQ 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 616431502 473 LSGGQRQRIDIARSFVKNPDILLLDEATANLDS------ESELK 510
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYklrkqmQNELK 188
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
349-557 |
7.62e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.29 E-value: 7.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKSTifnLIERMYEI---ESGDIKYGLES-------------VYDIPLSK------ 406
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTT---FIEHLNALllpDTGTIEWIFKDeknkkktkekekvLEKLVIQKtrfkki 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 407 -----WRRKIGYVMQ--SNSMMSGTIRDNILYG-INRHVSDEELINYAKlanchdfimqfdeGYDTLVG--ERGLK---- 472
Cdd:PRK13651 98 kkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGpVSMGVSKEEAKKRAA-------------KYIELVGldESYLQrspf 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 473 -LSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETL-MEGRTTIVIAHRL-STIKKAGQIIFLDKGQVT 549
Cdd:PRK13651 165 eLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKII 244
|
....*....
gi 616431502 550 GKG-THSEL 557
Cdd:PRK13651 245 KDGdTYDIL 253
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
339-560 |
1.01e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.42 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 339 EHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQsN 418
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ-N 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 419 SMMSGTIRDNILYGINRH----------VSDEELINYAKLANchdfimqfdeGYDTLVGERGLKLSGGQRQRIDIARSFV 488
Cdd:PRK10253 90 ATTPGDITVQELVARGRYphqplftrwrKEDEEAVTKAMQAT----------GITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 489 KNPDILLLDEATANLDSESELKIQEALETL--MEGRTTIVIAHRLS-TIKKAGQIIFLDKGQVTGKGTHSELMAS 560
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTA 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
345-543 |
1.30e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 345 YDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLesvydiplskwRRKIGYVMQSNSM---M 421
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdsL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 422 SGTIRDNILYG-------INRHVSDEELInyakLANCHDFImqfdeGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDIL 494
Cdd:NF040873 71 PLTVRDLVAMGrwarrglWRRLTRDDRAA----VDDALERV-----GLADLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 616431502 495 LLDEATANLDSESELKIQEAL-ETLMEGRTTIVIAHRLSTIKKAGQIIFL 543
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
346-562 |
1.44e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.46 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 346 DVKKILDDVSF----QIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYD----IPLSKWRRKIGYVMQS 417
Cdd:PRK11144 5 NFKQQLGDLCLtvnlTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgICLPPEKRRIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 418 NSMMSG-TIRDNILYGINRhvSDEElinyaklanchdfimQFDE-----GYDTLVGERGLKLSGGQRQRIDIARSFVKNP 491
Cdd:PRK11144 85 ARLFPHyKVRGNLRYGMAK--SMVA---------------QFDKivallGIEPLLDRYPGSLSGGEKQRVAIGRALLTAP 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616431502 492 DILLLDEATANLDSESELKIQEALETLM-EGRTTIV-IAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMASHA 562
Cdd:PRK11144 148 ELLLMDEPLASLDLPRKRELLPYLERLArEINIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
336-557 |
1.61e-16 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 79.11 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDI-PLSKWRRKIGYV 414
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLpPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSG-TIRDNILYGI------NRHVSDEElinYAKLANCHDFImqfdegydtlvGERGLKLSGGQRQRIDIARSF 487
Cdd:TIGR03410 81 PQGREIFPRlTVEENLLTGLaalprrSRKIPDEI---YELFPVLKEML-----------GRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616431502 488 VKNPDILLLDEATANLDSESELKIQEALETL--MEGRTTIVIAHRLSTIKKAGQ-IIFLDKGQVTGKGTHSEL 557
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARELADrYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
333-557 |
1.62e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.78 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 333 DGVLSFEHVDFKY-DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYgLESVYDIPLSKW-RRK 410
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKV-MGREVNAENEKWvRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 411 IGYVMQS--NSMMSGTIRDNILYG-INRHVSDEELINYAKLANchdfimqfdegydTLVGERGLK------LSGGQRQRI 481
Cdd:PRK13647 81 VGLVFQDpdDQVFSSTVWDDVAFGpVNMGLDKDEVERRVEEAL-------------KAVRMWDFRdkppyhLSYGQKKRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 482 DIARSFVKNPDILLLDEATANLDSESELKIQEALETL-MEGRTTIVIAHRLS-TIKKAGQIIFLDKGQVTGKGTHSEL 557
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
335-556 |
1.70e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.76 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKY-DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVY-----DIPLskWR 408
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPF--LR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 409 RKIGYVMQSNSM-MSGTIRDN-----ILYG-----INRHVSdEELINYAKLANCHDFIMQfdegydtlvgerglkLSGGQ 477
Cdd:PRK10908 79 RQIGMIFQDHHLlMDRTVYDNvaiplIIAGasgddIRRRVS-AALDKVGLLDKAKNFPIQ---------------LSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 478 RQRIDIARSFVKNPDILLLDEATANLD---SESELKIQEALETLmeGRTTIVIAHRLSTI-KKAGQIIFLDKGQVTGkGT 553
Cdd:PRK10908 143 QQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRV--GVTVLMATHDIGLIsRRSYRMLTLSDGHLHG-GV 219
|
...
gi 616431502 554 HSE 556
Cdd:PRK10908 220 GGE 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
355-562 |
2.10e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.86 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 355 SFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSkwRRKIGYVMQSNSMMSG-TIRDNILYGI 433
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 434 N-----RHVSDEELINYAKLANCHDFImqfdegyDTLVGErglkLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESE 508
Cdd:PRK10771 97 NpglklNAAQREKLHAIARQMGIEDLL-------ARLPGQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 509 LKIQEALETLMEGR--TTIVIAHRLS-TIKKAGQIIFLDKGQVTGKGTHSELMASHA 562
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
339-559 |
2.38e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.35 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 339 EHVDFKY---DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKY-GLESVYDIP-LSKWRRKIGY 413
Cdd:PRK13639 3 ETRDLKYsypDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKYDKKsLLEVRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 414 VMQS--NSMMSGTIRDNILYG-INRHVSDEELINYAKLAnCHDFIMqfdEGYDTLVGERglkLSGGQRQRIDIARSFVKN 490
Cdd:PRK13639 83 VFQNpdDQLFAPTVEEDVAFGpLNLGLSKEEVEKRVKEA-LKAVGM---EGFENKPPHH---LSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616431502 491 PDILLLDEATANLDSESELKIQEALETL-MEGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMA 559
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
52-529 |
2.48e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 82.15 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 52 SHINWNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFIS 131
Cdd:COG4615 44 GAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 132 QkLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLI-MIPLGRIMQKISTSTQSEIANFSGLlgRVLT----EMR 206
Cdd:COG4615 124 R-LPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGyRLLVRRARRHLRRAREAEDRLFKHF--RALLegfkELK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 207 LvkisNTER------LELDNAHKNLNEIYKLGLKQAKIAAVvqpISGIVMLLTIAIIL-GFGALEIATGAITAGTLIAMI 279
Cdd:COG4615 201 L----NRRRrraffdEDLQPTAERYRDLRIRADTIFALANN---WGNLLFFALIGLILfLLPALGWADPAVLSGFVLVLL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 280 FyviqLSMPLINLSTLVTDYKKAVGASSRIYEIMQEP--IEPTEALEDSENVLIDDGVLSFEHVDFKYDVKKilDDVSFQ 357
Cdd:COG4615 274 F----LRGPLSQLVGALPTLSRANVALRKIEELELALaaAEPAAADAAAPPAPADFQTLELRGVTYRYPGED--GDEGFT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 358 -------IPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRrkigyvmqsnSMMSgTI----- 425
Cdd:COG4615 348 lgpidltIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR----------QLFS-AVfsdfh 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 426 ---RdniLYGINRHVSDEELINYAKLanchdfiMQFDEgydtLVGERG-----LKLSGGQRQRIDIARSFVKNPDILLLD 497
Cdd:COG4615 417 lfdR---LLGLDGEADPARARELLER-------LELDH----KVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFD 482
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 616431502 498 EATANLDSE----------SELKIQealetlmeGRTTIVIAH 529
Cdd:COG4615 483 EWAADQDPEfrrvfytellPELKAR--------GKTVIAISH 516
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
348-548 |
2.86e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.97 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQsNSMM----SG 423
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQ-DPMMgtapSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 424 TIRDNIL--------YGINRHVSDEELINY-AKLAnchdfimQFDEGY----DTLVGerglKLSGGQRQridiARSFV-- 488
Cdd:COG1101 98 TIEENLAlayrrgkrRGLRRGLTKKRRELFrELLA-------TLGLGLenrlDTKVG----LLSGGQRQ----ALSLLma 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 489 --KNPDILLLDEATANLDSESELKIQEALETLMEGR--TTIVIAHRLS-TIKKAGQIIFLDKGQV 548
Cdd:COG1101 163 tlTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
321-547 |
2.97e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 82.85 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 321 EALEDSENVLIDDGVLSFEHVDFKYDVK------KILDDVSFQIPQGQVSAFVGPSGSGKSTIFN-LIERmyeIESGDIK 393
Cdd:TIGR00956 743 DDVNDEKDMEKESGEDIFHWRNLTYEVKikkekrVILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAER---VTTGVIT 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 394 YGLESVYDIPL-SKWRRKIGYVMQSN-SMMSGTIRDNILYG----INRHVSDEELINYAklanchDFIMQFDE--GY-DT 464
Cdd:TIGR00956 820 GGDRLVNGRPLdSSFQRSIGYVQQQDlHLPTSTVRESLRFSaylrQPKSVSKSEKMEYV------EEVIKLLEmeSYaDA 893
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 465 LVGERGLKLSGGQRQRIDIARSFVKNPDILL-LDEATANLDSESELKIQEALETLME-GRTTIVIAH-----------RL 531
Cdd:TIGR00956 894 VVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHqpsailfeefdRL 973
|
250
....*....|....*..
gi 616431502 532 STIKKAGQII-FLDKGQ 547
Cdd:TIGR00956 974 LLLQKGGQTVyFGDLGE 990
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
350-557 |
3.21e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 80.15 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 350 ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDipLSKWRRKIGYVMQSNSM---MSgtIR 426
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSIQQRDICMVFQSYALfphMS--LG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 427 DNILYGIN-RHVSDEELINYAKLANCHDFIMQFDEGY-DtlvgerglKLSGGQRQRIDIARSFVKNPDILLLDEATANLD 504
Cdd:PRK11432 97 ENVGYGLKmLGVPKEERKQRVKEALELVDLAGFEDRYvD--------QISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 505 SESELKIQEALETLME--GRTTIVIAHRLS-TIKKAGQIIFLDKGQVTGKGTHSEL 557
Cdd:PRK11432 169 ANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
336-548 |
3.37e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.57 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlesvyDIPLSKWRRKIGYVM 415
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSMMS-GTIRDNILYGINRHVSDEELINYAKLanchdfimqfdeGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDIL 494
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGLKGQWRDAALQALAAV------------GLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 495 LLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLS-TIKKAGQIIFLDKGQV 548
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
334-504 |
3.40e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.15 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 334 GVLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRK-IG 412
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 413 YVMQSNSMMSG-TIRDNIL-----YGINRHVSDEELinyaklanchdfimqfdegyDTLVGE---------RGLKLSGGQ 477
Cdd:COG1137 82 YLPQEASIFRKlTVEDNILavlelRKLSKKEREERL--------------------EELLEEfgithlrksKAYSLSGGE 141
|
170 180
....*....|....*....|....*..
gi 616431502 478 RQRIDIARSFVKNPDILLLDEATANLD 504
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
338-560 |
4.42e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.90 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 338 FEHVDFKYDVK-----KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlesVYDIP--------L 404
Cdd:PRK13645 9 LDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG---DYAIPanlkkikeV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 405 SKWRRKIGYVMQ--SNSMMSGTIRDNILYG-INRHVSDEELinYAKLANCHDFImQFDEGYdtlVGERGLKLSGGQRQRI 481
Cdd:PRK13645 86 KRLRKEIGLVFQfpEYQLFQETIEKDIAFGpVNLGENKQEA--YKKVPELLKLV-QLPEDY---VKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 482 DIARSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELM 558
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIF 239
|
..
gi 616431502 559 AS 560
Cdd:PRK13645 240 SN 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
348-557 |
5.85e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.31 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQS--NSMMSGTI 425
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNpdDQIFSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 426 RDNILYGINRHVSDEELINYAKLANCHDFimqfdeGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDS 505
Cdd:PRK13652 97 EQDIAFGPINLGLDEETVAHRVSSALHML------GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 506 ESELKIQEALETLME--GRTTIVIAHRLSTIKKAGQIIF-LDKGQVTGKGTHSEL 557
Cdd:PRK13652 171 QGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEMADYIYvMDKGRIVAYGTVEEI 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
315-534 |
8.38e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 80.06 E-value: 8.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 315 EPIEPT--EALEDSEN-VLIDDGVLSfehvdfkYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIermyeieSGD 391
Cdd:PRK10938 244 EPDEPSarHALPANEPrIVLNNGVVS-------YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-------TGD 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 392 IKYGL--------------ESVYDIplskwRRKIGYVmqSNSM-----MSGTIRDNIL------YGINRHVSDEElinyA 446
Cdd:PRK10938 310 HPQGYsndltlfgrrrgsgETIWDI-----KKHIGYV--SSSLhldyrVSTSVRNVILsgffdsIGIYQAVSDRQ----Q 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 447 KLAnchdfiMQFDE--GYDTLVGERGLK-LSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLM-EGR 522
Cdd:PRK10938 379 KLA------QQWLDilGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGE 452
|
250 260
....*....|....*....|....
gi 616431502 523 TTIV------------IAHRLSTI 534
Cdd:PRK10938 453 TQLLfvshhaedapacITHRLEFV 476
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
348-548 |
1.13e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.42 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkygleSVYDIPLSK--------WRRKIGYVMQ-SN 418
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV-----SWRGEPLAKlnraqrkaFRRDIQMVFQdSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 419 SMMS--GTIRDnILYGINRHVSD----------EELINYAKLAnchdfimqfdegyDTLVGERGLKLSGGQRQRIDIARS 486
Cdd:PRK10419 100 SAVNprKTVRE-IIREPLRHLLSldkaerlaraSEMLRAVDLD-------------DSVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 487 FVKNPDILLLDEATANLDSESELKIQEALETLMEGRTT--IVIAHRLSTIKKAGQ-IIFLDKGQV 548
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERFCQrVMVMDNGQI 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
347-557 |
1.36e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.09 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 347 VKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIerMYEIESGDIKYGLESVYDIPLSKW--RRKIGYVMQSNSMM-SG 423
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLNGMPIDAKemRAISAYVQQDDLFIpTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 424 TIRDNILYG----INRHVSD-------EELINYAKLANCHDfimqfdegydTLVGERGLK--LSGGQRQRIDIARSFVKN 490
Cdd:TIGR00955 115 TVREHLMFQahlrMPRRVTKkekrervDEVLQALGLRKCAN----------TRIGVPGRVkgLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 491 PDILLLDEATANLDSESELKIQEALETL-MEGRTTIVIAHRLST--IKKAGQIIFLDKGQVTGKGTHSEL 557
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
344-553 |
2.19e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.89 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 344 KYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkyglesvydiplsKWRRKI--------GYvm 415
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-------------EVNGRVsallelgaGF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 qsNSMMSGtiRDNI-----LYGINRHVSDE---ELINYAKLancHDFImqfdegyDTLVGerglKLSGGQRQRIDIARSF 487
Cdd:COG1134 100 --HPELTG--RENIylngrLLGLSRKEIDEkfdEIVEFAEL---GDFI-------DQPVK----TYSSGMRARLAFAVAT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 488 VKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIA-HRLSTIKK-AGQIIFLDKGQVTGKGT 553
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVsHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
333-560 |
2.90e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.98 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 333 DGVLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlesvyDIPLSKWR---- 408
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD-----AQPLESWSskaf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 409 -RKIGYVMQSNSMMSG-TIRDniLYGINRH----------VSDEELINYAKlanchdfimqfdegydTLVGERGL----- 471
Cdd:PRK10575 84 aRKVAYLPQQLPAAEGmTVRE--LVAIGRYpwhgalgrfgAADREKVEEAI----------------SLVGLKPLahrlv 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 472 -KLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAhRLSTIKKAGQ----IIFLDKG 546
Cdd:PRK10575 146 dSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAARycdyLVALRGG 224
|
250
....*....|....
gi 616431502 547 QVTGKGTHSELMAS 560
Cdd:PRK10575 225 EMIAQGTPAELMRG 238
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
336-557 |
3.86e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.94 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDV-----KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSK---- 406
Cdd:PRK13649 3 INLQNVSYTYQAgtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 407 WRRKIGYVMQ--SNSMMSGTIRDNILYGI-NRHVSDEELINYA--KLAnchdfIMQFDEgydTLVGERGLKLSGGQRQRI 481
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPqNFGVSQEEAEALAreKLA-----LVGISE---SLFEKNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 482 DIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIV-IAHRLSTIKK-AGQIIFLDKGQVTGKGTHSEL 557
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGKPKDI 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
336-559 |
4.66e-15 |
|
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: 77.92 E-value: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERM--YEIESGDIKYGL----ESVYDIPLSK--- 406
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHValceKCGYVERPSKvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 407 ----------------W----------RRKIGYVMQSNSMMSG--TIRDNILYGINR-HVSDEELINYAKlanchDFIMQ 457
Cdd:TIGR03269 81 pcpvcggtlepeevdfWnlsdklrrriRKRIAIMLQRTFALYGddTVLDNVLEALEEiGYEGKEAVGRAV-----DLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 458 FDEGYDTLVGERglKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLM--EGRTTIVIAHRLSTIK 535
Cdd:TIGR03269 156 VQLSHRITHIAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|....*
gi 616431502 536 K-AGQIIFLDKGQVTGKGTHSELMA 559
Cdd:TIGR03269 234 DlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
83-309 |
5.53e-15 |
|
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: 75.70 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 83 IGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNL--LPSIVTLvgsLIMLFILDWKMTL 160
Cdd:cd18566 69 IGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALldLPFVLIF---LGLIWYLGGKLVL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 161 LTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAA 240
Cdd:cd18566 146 VPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 241 VVQPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18566 226 VAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
335-558 |
7.43e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.81 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIermyeieSGDIK--YGLESVYDIPLSKWRR--- 409
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-------SGELSpdSGEVRLNGRPLADWSPael 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 410 -KIGYVM-QSNSM-MSGTIRDNILYGINRHVS----DEELINyAKLANChdfimqfdeGYDTLVGERGLKLSGGQRQRID 482
Cdd:PRK13548 75 aRRRAVLpQHSSLsFPFTVEEVVAMGRAPHGLsraeDDALVA-AALAQV---------DLAHLAGRDYPQLSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 483 IAR------SFVKNPDILLLDEATANLDseseLKIQEALETLM------EGRTTIVIAHRLS-TIKKAGQIIFLDKGQVT 549
Cdd:PRK13548 145 LARvlaqlwEPDGPPRWLLLDEPTSALD----LAHQHHVLRLArqlaheRGLAVIVVLHDLNlAARYADRIVLLHQGRLV 220
|
....*....
gi 616431502 550 GKGTHSELM 558
Cdd:PRK13548 221 ADGTPAEVL 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
336-544 |
1.05e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 73.28 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLI----ERMYEIeSGDIKYGLESVYDIPLSkwRRKI 411
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlSPAFSA-SGEVLLNGRRLTALPAE--QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 412 GYVMQS---NSMMSgtIRDNILYGI-------NRHVSDEELINYAKLAnchDFimqFDEGYDTlvgerglkLSGGQRQRI 481
Cdd:COG4136 79 GILFQDdllFPHLS--VGENLAFALpptigraQRRARVEQALEEAGLA---GF---ADRDPAT--------LSGGQRARV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616431502 482 DIARSFVKNPDILLLDEATANLDSE----------SELKiQEALETLMegrttivIAHRLSTIKKAGQIIFLD 544
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAAlraqfrefvfEQIR-QRGIPALL-------VTHDEEDAPAAGRVLDLG 207
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
38-295 |
1.06e-14 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 74.87 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSVSH--INWNLIALFGGIFVINallsglglyllskiGEKIIYAIRSVLW----------------EHI 99
Cdd:cd18583 15 VPRQLGIIVDSLSGGSgkSPWKEIGLYVLLRFLQ--------------SGGGLGLLRSWLWipveqysyralstaafNHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 100 IQLKMPFFDKNESGQLMSRLtDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFIL-DWKMTLLTFITIPIFVLIMIPLGR 178
Cdd:cd18583 81 MNLSMDFHDSKKSGEVLKAI-EQGSSINDLLEQILFQIVPMIIDLVIAIVYLYYLfDPYMGLIVAVVMVLYVWSTIKLTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 179 IMQKIststQSEIANFSGLLGRVLTEMRL----VKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTI 254
Cdd:cd18583 160 WRTKL----RRDMIDADREERSILTESLLnwetVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLILTLGL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 616431502 255 AIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTL 295
Cdd:cd18583 236 LAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATL 276
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
39-295 |
1.22e-14 |
|
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: 74.55 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 39 PLFTGRIVDKFSVSH---INWNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQL 115
Cdd:cd18782 22 PLLFQVIIDKVLVQQdlaTLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 116 MSRLtDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFS 195
Cdd:cd18782 102 STRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 196 GLLGRVLTEMRLVKISNTE---RLELDNAHKN-LNEIYKLGLKQAKIAAVVQPISgivmLLTIAIILGFGALEIATGAIT 271
Cdd:cd18782 181 SYLVESLTGIQTVKAQNAElkaRWRWQNRYARsLGEGFKLTVLGTTSGSLSQFLN----KLSSLLVLWVGAYLVLRGELT 256
|
250 260
....*....|....*....|....
gi 616431502 272 AGTLIAMIFYVIQLSMPLINLSTL 295
Cdd:cd18782 257 LGQLIAFRILSGYVTGPILRLSTL 280
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
348-542 |
2.31e-14 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 71.91 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIF----NLIERMYEIEsGDIKYGLESvYDIPLSKWRRKIGYVMQSNSMMSg 423
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLkalaNRTEGNVSVE-GDIHYNGIP-YKEFAEKYPGEIIYVSEEDVHFP- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 424 tirdnilyginrHVSDEELINYAKLANCHDFImqfdegydtlvgeRGLklSGGQRQRIDIARSFVKNPDILLLDEATANL 503
Cdd:cd03233 97 ------------TLTVRETLDFALRCKGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 616431502 504 DSESELKIQEALETL--MEGRTTIVIAHRLS----------TIKKAGQIIF 542
Cdd:cd03233 150 DSSTALEILKCIRTMadVLKTTTFVSLYQASdeiydlfdkvLVLYEGRQIY 200
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
346-516 |
2.38e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 74.49 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 346 DVKK-------ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKwrRKIGYVMQSN 418
Cdd:PRK11650 8 AVRKsydgktqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVFQNY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 419 SM---MSgtIRDNILYGI-NRHVSDEElIN--YAKLANchdfIMQFDEgydtLVGERGLKLSGGQRQRIDIARSFVKNPD 492
Cdd:PRK11650 86 ALyphMS--VRENMAYGLkIRGMPKAE-IEerVAEAAR----ILELEP----LLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180
....*....|....*....|....
gi 616431502 493 ILLLDEATANLDseSELKIQEALE 516
Cdd:PRK11650 155 VFLFDEPLSNLD--AKLRVQMRLE 176
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
349-548 |
2.62e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.92 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDI---PLSKWRRK-IGYVMQSNSMMSG- 423
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREhFGFIFQRYHLLSHl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 424 TIRDN-----ILYGINRHvsdeelinyAKLANCHDFIMQFdeGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDE 498
Cdd:PRK10535 102 TAAQNvevpaVYAGLERK---------QRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 616431502 499 ATANLDSESELKIQEALETLME-GRTTIVIAHRLSTIKKAGQIIFLDKGQV 548
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
327-566 |
3.29e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.20 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 327 ENVLIDDGVLSFEHVDFKYDVKKI-LDDVSFQIPQGQVSAFVGPSGSGKSTI---FNLI-----ERMYeIESGDIKyGLE 397
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEKLaLDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALlipseGKVY-VDGLDTS-DEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 398 SVYDIplskwRRKIGYVMQS--NSMMSGTIRDNILYGI-NRHVSDEEL---INYA-KLANCHDFimqfdEGYDTLVgerg 470
Cdd:PRK13633 79 NLWDI-----RNKAGMVFQNpdNQIVATIVEEDVAFGPeNLGIPPEEIrerVDESlKKVGMYEY-----RRHAPHL---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 471 lkLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESElkiQEALETLME-----GRTTIVIAHRLSTIKKAGQIIFLDK 545
Cdd:PRK13633 145 --LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR---REVVNTIKElnkkyGITIILITHYMEEAVEADRIIVMDS 219
|
250 260
....*....|....*....|.
gi 616431502 546 GQVTGKGTHSELMASHAKYKN 566
Cdd:PRK13633 220 GKVVMEGTPKEIFKEVEMMKK 240
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
344-569 |
3.71e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.58 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 344 KYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTifnLIERMYEI---ESGDIKY-GLesvydIPlskWRRKIGYVMQSNS 419
Cdd:COG4586 31 EYREVEAVDDISFTIEPGEIVGFIGPNGAGKST---TIKMLTGIlvpTSGEVRVlGY-----VP---FKRRKEFARRIGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 420 MMsG---------TIRD--NIL---YGINRHVSDEELINYAKLANCHDFImqfdegyDTLVgeRglKLSGGQRQRIDIAR 485
Cdd:COG4586 100 VF-GqrsqlwwdlPAIDsfRLLkaiYRIPDAEYKKRLDELVELLDLGELL-------DTPV--R--QLSLGQRMRCELAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 486 SFVKNPDILLLDEATANLDSESELKIQEALETLMEGR-TTIVIA-HRLSTIKK-AGQIIFLDKGQVTGKGTHSELMASHA 562
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFG 247
|
....*..
gi 616431502 563 KYKNFVV 569
Cdd:COG4586 248 PYKTIVL 254
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
97-305 |
3.91e-14 |
|
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: 73.32 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 97 EHIIQLKMPFFDKNESGQLMSRLTDdTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTF---ITIPIFVLIM 173
Cdd:cd18783 83 DRLLSLPIDFFERTPAGVLTKHMQQ-IERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLafsALIALIILAF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 174 IPlgrIMQKISTSTQSEIANFSGLLGRVLTEMRLVK---ISNTERLELDNAhknLNEIYKLGLKQAKIAAVVQPISG-IV 249
Cdd:cd18783 162 LP---PFRRRLQALYRAEGERQAFLVETVHGIRTVKslaLEPRQRREWDER---VARAIRARFAVGRLSNWPQTLTGpLE 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 250 MLLTIAIILgFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGA 305
Cdd:cd18783 236 KLMTVGVIW-VGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLS 290
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
40-294 |
4.99e-14 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 72.70 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 40 LFTGRIVDKFsVSHINW----NLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQL 115
Cdd:cd18561 17 WLLARALARI-FAGGPWedimPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 116 MSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFS 195
Cdd:cd18561 96 QTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 196 G-LLGRV--LTEMRLVKISNTERLELDNAHknlNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITA 272
Cdd:cd18561 176 AqFLDSLqgMTTLKAFGASKRRGNELAARA---EDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTL 252
|
250 260
....*....|....*....|..
gi 616431502 273 GTLIAMIFYVIQLSMPLINLST 294
Cdd:cd18561 253 SSLLLILFLSREFFRPLRDLGA 274
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
336-530 |
6.04e-14 |
|
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: 70.63 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIerM----YEIESGDIKYGLESVYDIPLS-KWRRK 410
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MghpkYEVTEGEILFKGEDITDLPPEeRARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 411 IGYVMQSNSMMSGTirdnilyginrhvsdeelinyaKLAnchDFIMQFDEGydtlvgerglkLSGGQRQRIDIARSFVKN 490
Cdd:cd03217 79 IFLAFQYPPEIPGV----------------------KNA---DFLRYVNEG-----------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 616431502 491 PDILLLDEATANLDSESELKIQEALETLM-EGRTTIVIAHR 530
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHY 163
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
351-531 |
7.24e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 7.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKY-GLESVYDIPLSKWRRKIGYVMQSNSMMSG-TIRDN 428
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRFRSPRDAQAAGIAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 429 ILygINRHVSDEELINYAKL-----ANCHDFIMQFDEgyDTLVGErglkLSGGQRQRIDIARSFVKNPDILLLDEATANL 503
Cdd:COG1129 100 IF--LGREPRRGGLIDWRAMrrrarELLARLGLDIDP--DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190
....*....|....*....|....*....|...
gi 616431502 504 dSESElkiQEALETLM-----EGRTTIVIAHRL 531
Cdd:COG1129 172 -TERE---VERLFRIIrrlkaQGVAIIYISHRL 200
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
335-567 |
7.56e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.36 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVyDIPLSKWRRKIGYV 414
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSG-TIRDNILYGInrHVSD-----EELINYAKLANCHDFIMqfdegydtlvgerGLkLSGGQRQRIDIARSFV 488
Cdd:PRK13540 80 GHRSGINPYlTLRENCLYDI--HFSPgavgiTELCRLFSLEHLIDYPC-------------GL-LSSGQKRQVALLRLWM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 489 KNPDILLLDEATANLDseselkiQEALETLMegrtTIVIAHRlstiKKAGQIIFLdkgqvtgkgTHSELMASHAKYKNF 567
Cdd:PRK13540 144 SKAKLWLLDEPLVALD-------ELSLLTII----TKIQEHR----AKGGAVLLT---------SHQDLPLNKADYEEY 198
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
39-309 |
8.38e-14 |
|
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: 72.15 E-value: 8.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 39 PLFTGRIVDKFSVSHINWNLIALFGGIFVINallsglglyllskIGEKIIYAIR----------------SVLWEHIIQL 102
Cdd:cd18588 22 PLFFQVIIDKVLVHRSLSTLDVLAIGLLVVA-------------LFEAVLSGLRtylfshttnridaelgARLFRHLLRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 103 KMPFFDKNESGQLMSRLTD-DTkvINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQ 181
Cdd:cd18588 89 PLSYFESRQVGDTVARVRElES--IRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 182 KISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFG 261
Cdd:cd18588 167 RRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 616431502 262 ALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18588 247 AYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
350-560 |
1.05e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.95 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 350 ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNSM-MSGTIRDN 428
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 429 ILYGINRHVSD------------EELINYAKLAnchdfimQF-DEGYDTlvgerglkLSGGQRQRIDIARSFVKNPDILL 495
Cdd:PRK09536 98 VEMGRTPHRSRfdtwtetdraavERAMERTGVA-------QFaDRPVTS--------LSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 496 LDEATANLDSESELKIQEALETLME-GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMAS 560
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTA 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
341-498 |
1.16e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.33 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 341 VDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLEsvyDIP------LSKWRRKIGYV 414
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE---NIPamsrsrLYTVRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSG-TIRDNILYGINRHVS-DEELInyaklancHDFIMQFDEGydtlVGERGL------KLSGGQRQRIDIARS 486
Cdd:PRK11831 90 FQSGALFTDmNVFDNVAYPLREHTQlPAPLL--------HSTVMMKLEA----VGLRGAaklmpsELSGGMARRAALARA 157
|
170
....*....|..
gi 616431502 487 FVKNPDILLLDE 498
Cdd:PRK11831 158 IALEPDLIMFDE 169
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
335-516 |
1.36e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.61 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlESVydiplskwrrKIGYV 414
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG-ETV----------KLAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSG--TIRDNIlyginrhvSD-EELINYAKL-----ANCHDFimQFdEGYD--TLVGErglkLSGGQRQRIDIA 484
Cdd:PRK11819 393 DQSRDALDPnkTVWEEI--------SGgLDIIKVGNReipsrAYVGRF--NF-KGGDqqKKVGV----LSGGERNRLHLA 457
|
170 180 190
....*....|....*....|....*....|..
gi 616431502 485 RSFVKNPDILLLDEATANLDSESELKIQEALE 516
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
348-549 |
4.00e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGdikyglESVYDIPLSKWRRKigyvmqsnsmmsGTIRD 427
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV------AGCVDVPDNQFGRE------------ASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 428 NIlyGINRHVSDE-ELINYAKLANCHDFIMQFDEgydtlvgerglkLSGGQRQRIDIARSFVKNPDILLLDEATANLDSE 506
Cdd:COG2401 105 AI--GRKGDFKDAvELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 616431502 507 S----ELKIQEALETLmeGRTTIVIAHRlSTIKKAGQ---IIFLDKGQVT 549
Cdd:COG2401 171 TakrvARNLQKLARRA--GITLVVATHH-YDVIDDLQpdlLIFVGYGGVP 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
335-553 |
4.71e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.63 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKY-DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGD-IKYGLESVYDIPLSKWRRKIG 412
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKvLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 413 YVMQS--NSMMSGTIRDNILYGinrhvsDEELinyaklanCHDFImQFDEGYDTLVGERGLK---------LSGGQRQRI 481
Cdd:PRK13644 81 IVFQNpeTQFVGRTVEEDLAFG------PENL--------CLPPI-EIRKRVDRALAEIGLEkyrhrspktLSGGQGQCV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616431502 482 DIARSFVKNPDILLLDEATANLDSESELKIQEALETLME-GRTTIVIAHRLSTIKKAGQIIFLDKGQVTGKGT 553
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
311-529 |
5.28e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 71.37 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 311 EIMQEPIEPTEALEDSENVLIDDGVLSFEHVDFKY-----DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMY 385
Cdd:TIGR03269 255 EVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 386 EIESGD--IKYGLESVyDI----PLSKWRRK--IGYVMQSNSMMS-GTIRDNILYGINRHVSDEelinYAKLANCHDFIM 456
Cdd:TIGR03269 335 EPTSGEvnVRVGDEWV-DMtkpgPDGRGRAKryIGILHQEYDLYPhRTVLDNLTEAIGLELPDE----LARMKAVITLKM 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 457 Q-FDEGYDTLVGER-GLKLSGGQRQRIDIARSFVKNPDILLLDEATANLD-------SESELKIQEALEtlmegRTTIVI 527
Cdd:TIGR03269 410 VgFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkvdvTHSILKAREEME-----QTFIIV 484
|
..
gi 616431502 528 AH 529
Cdd:TIGR03269 485 SH 486
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
58-300 |
5.56e-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: 69.80 E-value: 5.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 58 LIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLtDDTKVINEFISQKLPNL 137
Cdd:cd18567 44 LAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 138 LPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLE 217
Cdd:cd18567 123 LLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAER 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 218 LDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVT 297
Cdd:cd18567 203 EARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDKLF 282
|
...
gi 616431502 298 DYK 300
Cdd:cd18567 283 ELR 285
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
350-528 |
6.76e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.98 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 350 ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLEsvyDIPLSKWRRKIGYVMQSNSMMSG-TIRDN 428
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG---DIDDPDVAEACHYLGHRNAMKPAlTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 429 I-----LYGINRHVSDE--ELINYAKLANchdfiMQFdeGYdtlvgerglkLSGGQRQRIDIARSFVKNPDILLLDEATA 501
Cdd:PRK13539 94 LefwaaFLGGEELDIAAalEAVGLAPLAH-----LPF--GY----------LSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|
gi 616431502 502 NLDSESelkiQEALETLMEGRTT---IVIA 528
Cdd:PRK13539 157 ALDAAA----VALFAELIRAHLAqggIVIA 182
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
341-552 |
9.16e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 9.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 341 VDFKYDVKkildDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMyeIES-GDIKYGlesvyDIPLSKW--------RRKI 411
Cdd:PRK15134 296 VDHNVVVK----NISFTLRPGETLGLVGESGSGKSTTGLALLRL--INSqGEIWFD-----GQPLHNLnrrqllpvRHRI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 412 GYVMQS-NSMMSGtiRDNILYGInrhvsDEELINYAKLANCHdfimQFDEGYDTLVGERGL----------KLSGGQRQR 480
Cdd:PRK15134 365 QVVFQDpNSSLNP--RLNVLQII-----EEGLRVHQPTLSAA----QREQQVIAVMEEVGLdpetrhrypaEFSGGQRQR 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 481 IDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGR--TTIVIAHRLSTIKK-AGQIIFLDKGQVTGKG 552
Cdd:PRK15134 434 IAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
335-548 |
9.23e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.50 E-value: 9.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIF----NLI------ERMYEIESGDIKYGLESVYDIpl 404
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLItgdksaGSHIELLGRTVQREGRLARDI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 405 SKWRRKIGYVMQSNSMMSG-TIRDNILYGinrhvsdeELINYAKLANCHDFI--MQFDEGYDTL--VG------ERGLKL 473
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRlSVLENVLIG--------ALGSTPFWRTCFSWFtrEQKQRALQALtrVGmvhfahQRVSTL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 474 SGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETL--MEGRTTIVIAHRLS-TIKKAGQIIFLDKGQV 548
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
346-504 |
1.08e-12 |
|
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: 70.48 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 346 DVKKILDDVSFQIPQGQVSAFVGPSGSGKST----IFNLIERmyeieSGDIKYGLESVYDIP---LSKWRRKIGYVMQ-- 416
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIPS-----EGEIRFDGQDLDGLSrraLRPLRRRMQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 417 --S-NSMMsgTIRDNILYGInrHVSDEELiNYAklanchdfimQFDEGYDTLVGERGLK----------LSGGQRQRIDI 483
Cdd:COG4172 372 fgSlSPRM--TVGQIIAEGL--RVHGPGL-SAA----------ERRARVAEALEEVGLDpaarhrypheFSGGQRQRIAI 436
|
170 180
....*....|....*....|.
gi 616431502 484 ARSFVKNPDILLLDEATANLD 504
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALD 457
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
351-529 |
1.78e-12 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 67.11 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKygLESvYDIPLSKWRRKIgyVMQSNSMMSG-TIRDNI 429
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVI--LEG-KQITEPGPDRMV--VFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 430 LYGINRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGErglkLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESEL 509
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|..
gi 616431502 510 KIQEALETLME--GRTTIVIAH 529
Cdd:TIGR01184 152 NLQEELMQIWEehRVTVLMVTH 173
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
342-529 |
2.47e-12 |
|
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: 67.05 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 342 DFKYDVKKilddvsFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkyglesvyDIPLSKWRRKIGYVmqsNSMM 421
Cdd:cd03237 12 EFTLEVEG------GSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--------EIELDTVSYKPQYI---KADY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 422 SGTIRDnILYGI-NRHVSDEELINyaKLANchdfIMQFDEGYDTLVGErglkLSGGQRQRIDIARSFVKNPDILLLDEAT 500
Cdd:cd03237 75 EGTVRD-LLSSItKDFYTHPYFKT--EIAK----PLQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190
....*....|....*....|....*....|.
gi 616431502 501 ANLDSESELKIQEALETLMEG--RTTIVIAH 529
Cdd:cd03237 144 AYLDVEQRLMASKVIRRFAENneKTAFVVEH 174
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
348-529 |
2.48e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.01 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIerM----YEIESGDIKYGLESVYDIPLSKWRRK-IGYVMQ------ 416
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MghpkYEVTSGSILLDGEDILELSPDERARAgIFLAFQypveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 417 --SNSM----MSGTIRDNILYGINrhvSDEELINYAKLanchdfiMQFDEGYdtlvGERGL--KLSGGQRQRIDIARSFV 488
Cdd:COG0396 91 gvSVSNflrtALNARRGEELSARE---FLKLLKEKMKE-------LGLDEDF----LDRYVneGFSGGEKKRNEILQMLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 616431502 489 KNPDILLLDEATANLDSESeLKI-QEALETLM-EGRTTIVIAH 529
Cdd:COG0396 157 LEPKLAILDETDSGLDIDA-LRIvAEGVNKLRsPDRGILIITH 198
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
335-518 |
4.64e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKyglesvYDIPLskwrrKIGYV 414
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKL-----RIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQ------------SNSMM--SGTIRDNILYGINRhvsdeelINYAKLancHDFIMQfdegydtlvgerglKLSGGQRQR 480
Cdd:PRK09544 73 PQklyldttlpltvNRFLRlrPGTKKEDILPALKR-------VQAGHL---IDAPMQ--------------KLSGGETQR 128
|
170 180 190
....*....|....*....|....*....|....*...
gi 616431502 481 IDIARSFVKNPDILLLDEATANLDSESELKIQEALETL 518
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQL 166
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
352-534 |
4.87e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.17 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 352 DDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKiGYV--MQS----NSMmsgTI 425
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVrtFQHvrlfREM---TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 426 RDNILYGINRHV----------------SDEELINYAklANCHDFImqfdeGYDTLVGERGLKLSGGQRQRIDIARSFVK 489
Cdd:PRK11300 98 IENLLVAQHQQLktglfsgllktpafrrAESEALDRA--ATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 616431502 490 NPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTI 534
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLV 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
350-529 |
5.90e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 350 ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkygleSVYDIPLSKWR---------RKIGYVMQSnSM 420
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEV-----SLVGQPLHQMDeearaklraKHVGFVFQS-FM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 421 MSGTI--RDNI-LYGINRHVSDEELINYAKlanchDFIMQFDegydtlVGER----GLKLSGGQRQRIDIARSFVKNPDI 493
Cdd:PRK10584 99 LIPTLnaLENVeLPALLRGESSRQSRNGAK-----ALLEQLG------LGKRldhlPAQLSGGEQQRVALARAFNGRPDV 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 616431502 494 LLLDEATANLDSESELKIQEALETLME--GRTTIVIAH 529
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTH 205
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
38-303 |
1.02e-11 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 65.98 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSVSHINWN-----LIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNES 112
Cdd:cd18582 15 VPFLLKYAVDALSAPASALLavpllLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRVFRHLHSLSLRFHLSRKT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 113 GQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFIL-DWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEI 191
Cdd:cd18582 95 GALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLyGWSYALITLVTVALYVAFTIKVTEWRTKFRREMNEAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 192 ANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAIT 271
Cdd:cd18582 175 NEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGLTAIMLLAAQGVVAGTLT 254
|
250 260 270
....*....|....*....|....*....|..
gi 616431502 272 AGTLIAMIFYVIQLSMPLINLSTLVTDYKKAV 303
Cdd:cd18582 255 VGDFVLVNTYLLQLYQPLNFLGFVYREIRQSL 286
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
348-559 |
1.11e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.60 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERmyEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNSMMSG-TIR 426
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--RIQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 427 DNILY----GINRHVSDEELINYAK-------LANCHDfimqfdegydTLVGERGLK-LSGGQRQRIDIARSFVKNPDIL 494
Cdd:PLN03211 159 ETLVFcsllRLPKSLTKQEKILVAEsviselgLTKCEN----------TIIGNSFIRgISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 495 LLDEATANLDSESELKIQEALETLME-GRTTIVIAHRLST--IKKAGQIIFLDKGQVTGKGTHSELMA 559
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQkGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
336-541 |
1.28e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.95 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKY-----GLESVYDIPLSKWRRK 410
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgQLRDLYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 411 I----GYVMQsnsmmsgtirdNILYGINRHVS-----DEELI-----NYAKLANCHDFIMQFDEGYDTLVGERGLKLSGG 476
Cdd:PRK11701 87 LrtewGFVHQ-----------HPRDGLRMQVSaggniGERLMavgarHYGDIRATAGDWLERVEIDAARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 477 QRQRIDIARSFVKNPDILLLDEATANLDseseLKIQEALETLMEGRTT-------IV---------IAHRLsTIKKAGQI 540
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLD----VSVQARLLDLLRGLVRelglavvIVthdlavarlLAHRL-LVMKQGRV 230
|
.
gi 616431502 541 I 541
Cdd:PRK11701 231 V 231
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
345-532 |
1.37e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.76 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 345 YDVK----------KILDDVSFQIPQGQVSAFVGPSGSGKSTI---FNLIErmyEIESGDIKYGLESVYDIPLSKW---R 408
Cdd:PRK11308 15 YPVKrglfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIE---TPTGGELYYQGQDLLKADPEAQkllR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 409 RKIGYVMQsNSMMS-------GTIRDNILYgINRHVSDEEliNYAKLANchdfIMQfdegydtLVGergLK--------- 472
Cdd:PRK11308 92 QKIQIVFQ-NPYGSlnprkkvGQILEEPLL-INTSLSAAE--RREKALA----MMA-------KVG---LRpehydryph 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 473 -LSGGQRQRIDIARSFVKNPDILLLDEATANLDseseLKIQ-EALETLME-----GRTTIVIAHRLS 532
Cdd:PRK11308 154 mFSGGQRQRIAIARALMLDPDVVVADEPVSALD----VSVQaQVLNLMMDlqqelGLSYVFISHDLS 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
351-550 |
1.49e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.97 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVyDI--PLSKWRRKIGYV----MQSNSMmsgT 424
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIrsPRDAIALGIGMVhqhfMLVPNL---T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 425 IRDNILYGinRHVSDEELINYAKLAnchDFIMQFDEGY------DTLVGErglkLSGGQRQRIDIARSFVKNPDILLLDE 498
Cdd:COG3845 97 VAENIVLG--LEPTKGGRLDRKAAR---ARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616431502 499 ATANLDSeselkiQEAlETLM--------EGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTG 550
Cdd:COG3845 168 PTAVLTP------QEA-DELFeilrrlaaEGKSIIFITHKLREVMAiADRVTVLRRGKVVG 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
304-553 |
3.86e-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: 66.19 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 304 GASSRiYEIMQEPIEP-TEALEDSENVL-IDDGVLSFEH------VDFKYDVK-------KILDDVSFQIPQGQVSAFVG 368
Cdd:TIGR01257 885 GCSTR-EERALEKTEPlTEEMEDPEHPEgINDSFFERELpglvpgVCVKNLVKifepsgrPAVDRLNITFYENQITAFLG 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 369 PSGSGKSTIFNLIERMYEIESGDIKYGLESVyDIPLSKWRRKIGYVMQSNSMMSG-TIRDNIL-YGINRHVSDEElinya 446
Cdd:TIGR01257 964 HNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILfYAQLKGRSWEE----- 1037
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 447 klANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIV 526
Cdd:TIGR01257 1038 --AQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIM 1115
|
250 260
....*....|....*....|....*...
gi 616431502 527 IAHRLSTIKKAG-QIIFLDKGQVTGKGT 553
Cdd:TIGR01257 1116 STHHMDEADLLGdRIAIISQGRLYCSGT 1143
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
335-504 |
4.18e-11 |
|
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: 65.48 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFE--HVDFKYD--VKKILDDVSFQIPQGQVSAFVGPSGSGKS----TIFNLIERMYEIESGDIKYGLESVYDIPLSK 406
Cdd:COG4172 6 LLSVEdlSVAFGQGggTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 407 WRR----KIGYV----MQS-NSMMsgTIRDNILYGINRH--VSDE-------ELINyaklanchdfimqfdegydtLVG- 467
Cdd:COG4172 86 LRRirgnRIAMIfqepMTSlNPLH--TIGKQIAEVLRLHrgLSGAaararalELLE--------------------RVGi 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 616431502 468 ---ERGLK-----LSGGQRQRIDIARSFVKNPDILLLDEATANLD 504
Cdd:COG4172 144 pdpERRLDayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
354-558 |
9.71e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 9.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 354 VSFQIPQGQVSAFVGPSGSGKSTifnLIERMYEI--ESGDIKYGLESVYDIPLSKWRRKIGYVMQSNS-----------M 420
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLlpGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTppfampvfqylT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 421 MSgtirdniLYGINRHVSDEELINYAklanCHDFIMQfdegyDTLvgERGL-KLSGGQRQRIDIARSFVK-----NPD-- 492
Cdd:PRK03695 92 LH-------QPDKTRTEAVASALNEV----AEALGLD-----DKL--GRSVnQLSGGEWQRVRLAAVVLQvwpdiNPAgq 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616431502 493 ILLLDEATANLDseseLKIQEALETLME-----GRTTIVIAHRLS-TIKKAGQIIFLDKGQVTGKGTHSELM 558
Cdd:PRK03695 154 LLLLDEPMNSLD----VAQQAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
335-529 |
1.33e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYG--LEsvydiplskwrrkIG 412
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGtkLE-------------VA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 413 YVMQSNSMM--SGTIRDNI--------LYGINRHVsdeelinyakLANCHDFI------MqfdegydTLVGerglKLSGG 476
Cdd:PRK11147 386 YFDQHRAELdpEKTVMDNLaegkqevmVNGRPRHV----------LGYLQDFLfhpkraM-------TPVK----ALSGG 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 477 QRQRIDIARSFVKNPDILLLDEATANLDSES-ELkiqeaLETLMEGR--TTIVIAH 529
Cdd:PRK11147 445 ERNRLLLARLFLKPSNLLILDEPTNDLDVETlEL-----LEELLDSYqgTVLLVSH 495
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
349-566 |
3.01e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.03 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRK---IGYVMQS-----NSM 420
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDplaslNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 421 MsgTIRDNI---LYGINRHVSDEELINYAK--------LANC-----HDFimqfdegydtlvgerglklSGGQRQRIDIA 484
Cdd:PRK15079 115 M--TIGEIIaepLRTYHPKLSRQEVKDRVKammlkvglLPNLinrypHEF-------------------SGGQCQRIGIA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 485 RSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKKAGqiiflDKGQVTGKGTHSELMASHA 562
Cdd:PRK15079 174 RALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHIS-----DRVLVMYLGHAVELGTYDE 248
|
....
gi 616431502 563 KYKN 566
Cdd:PRK15079 249 VYHN 252
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
335-562 |
3.35e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.66 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSK-WRRKIGY 413
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 414 VMQSNSMMSG-TIRDNILYGinRHVSDEELINyAKLANCHDFIMQFDEGYdtlvGERGLKLSGGQRQRIDIARSFVKNPD 492
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMG--GFFAERDQFQ-ERIKWVYELFPRLHERR----IQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616431502 493 ILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLS--TIKKAGQIIFLDKGQVTGKGTHSELMASHA 562
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
312-534 |
4.19e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 312 IMQEPIE----PTEAlEDSENVLIDDGVLSFEHVDFKYDVKkilddvSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEI 387
Cdd:PRK13409 319 IRPEPIEfeerPPRD-ESERETLVEYPDLTKKLGDFSLEVE------GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKP 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 388 ESGDIKYGLESVYdiplskwrrKIGYVmQSNSmmSGTIRDnILYGINRHVSDeeliNYAKlancHDFI--MQFDEGYDTL 465
Cdd:PRK13409 392 DEGEVDPELKISY---------KPQYI-KPDY--DGTVED-LLRSITDDLGS----SYYK----SEIIkpLQLERLLDKN 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616431502 466 VGErglkLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGR--TTIVIAHRLSTI 534
Cdd:PRK13409 451 VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI 517
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
331-560 |
8.61e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 8.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 331 IDDGVLSFEHVDfkyDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMY-----EIESGDIKYGLESVYDIPLS 405
Cdd:PRK15134 8 IENLSVAFRQQQ---TVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 406 KWRR----KIGYVMQSnSMMSGTIRDNI---LY-------GINRHVSDEELI---------NYAKLANchDFIMQfdegy 462
Cdd:PRK15134 85 TLRGvrgnKIAMIFQE-PMVSLNPLHTLekqLYevlslhrGMRREAARGEILncldrvgirQAAKRLT--DYPHQ----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 463 dtlvgerglkLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKK-AGQ 539
Cdd:PRK15134 157 ----------LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADR 226
|
250 260
....*....|....*....|.
gi 616431502 540 IIFLDKGQVTGKGTHSELMAS 560
Cdd:PRK15134 227 VAVMQNGRCVEQNRAATLFSA 247
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
346-528 |
1.09e-09 |
|
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: 58.27 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 346 DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKY---GLESVYDIplskWRRKIGYVMQSNSMMS 422
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggPLDFQRDS----IARGLLYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 423 G-TIRDNILYGINRHvSDEelinyaklanchdfimQFDEGYDTlVGERGLK------LSGGQRQRIDIARSFVKNPDILL 495
Cdd:cd03231 87 TlSVLENLRFWHADH-SDE----------------QVEEALAR-VGLNGFEdrpvaqLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190
....*....|....*....|....*....|...
gi 616431502 496 LDEATANLDSESELKIQEALETLMEGRTTIVIA 528
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLT 181
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
335-527 |
1.33e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 57.83 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDfkydVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKY-GLESVYDIPLSKWRRKIGY 413
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 414 V----MQSNSMMSGTIRDNILygINRHvsdeelinyaklanchdfimqfdegydtlvgerglkLSGGQRQRIDIARSFVK 489
Cdd:cd03215 80 VpedrKREGLVLDLSVAENIA--LSSL------------------------------------LSGGNQQKVVLARWLAR 121
|
170 180 190
....*....|....*....|....*....|....*....
gi 616431502 490 NPDILLLDEATANLDSESELKIQEAL-ETLMEGRTTIVI 527
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIrELADAGKAVLLI 160
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
351-536 |
1.44e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKW---RRKIGYVMQsNSMMSGTIRD 427
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqalRRDIQFIFQ-DPYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 428 NILYGINRHVSDEELINYAKLANCHDFIMqfdegydtlvgER-GLK----------LSGGQRQRIDIARSFVKNPDILLL 496
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKAAAARVAWLL-----------ERvGLLpehawrypheFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 616431502 497 DEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKK 536
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVER 529
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
343-559 |
1.82e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.87 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 343 FKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDI----------KYGLESVydiplskwRRKIG 412
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldysKRGLLAL--------RQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 413 YVMQ--SNSMMSGTIRDNILYGI-NRHVSDEELINyaklanchdfimQFDEGYdTLVGERGLK------LSGGQRQRIDI 483
Cdd:PRK13638 81 TVFQdpEQQIFYTDIDSDIAFSLrNLGVPEAEITR------------RVDEAL-TLVDAQHFRhqpiqcLSHGQKKRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 484 ARSFVKNPDILLLDEATANLDSESELKIQEALETLM-EGRTTIVIAHRLSTIKKAGQIIF-LDKGQVTGKGTHSELMA 559
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEISDAVYvLRQGQILTHGAPGEVFA 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
312-534 |
2.46e-09 |
|
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: 59.80 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 312 IMQEPIE----PTEALEDSEnVLIDDGVLSFEHVDFKYDVKkilddvSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEI 387
Cdd:COG1245 320 IRDEPIEfevhAPRREKEEE-TLVEYPDLTKSYGGFSLEVE------GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 388 ESGDIKYGLESVYdiplskwrrKIGYVMQSnsmMSGTIRDNILYGINRHVSD----EELINYaklanchdfiMQFDEGYD 463
Cdd:COG1245 393 DEGEVDEDLKISY---------KPQYISPD---YDGTVEEFLRSANTDDFGSsyykTEIIKP----------LGLEKLLD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616431502 464 TLVGErglkLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGR--TTIVIAHRLSTI 534
Cdd:COG1245 451 KNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI 519
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
336-538 |
2.80e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkygleSVYDIPLSKWRRK----- 410
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI-----TINNINYNKLDHKlaaql 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 411 -IGYVMQSNSMMSG-TIRDNILYG--INRHVSDEELINYAKL---ANCHDFIMQFDEGYDTLVGErglkLSGGQRQRIDI 483
Cdd:PRK09700 81 gIGIIYQELSVIDElTVLENLYIGrhLTKKVCGVNIIDWREMrvrAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 484 ARSFVKNPDILLLDEATANL-DSESE--LKIQEALETlmEGRTTIVIAHRLSTIKKAG 538
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLtNKEVDylFLIMNQLRK--EGTAIVYISHKLAEIRRIC 212
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
336-543 |
3.17e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.24 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKK-------------ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYE---IEsGDIKYgleSV 399
Cdd:PLN03140 868 MSFDDVNYFVDMPAemkeqgvtedrlqLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggyIE-GDIRI---SG 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 400 YDIPLSKWRRKIGYVMQsNSMMSG--TIRDNILYG----INRHVSDEELINYAklanchDFIM---QFDEGYDTLVGERG 470
Cdd:PLN03140 944 FPKKQETFARISGYCEQ-NDIHSPqvTVRESLIYSaflrLPKEVSKEEKMMFV------DEVMelvELDNLKDAIVGLPG 1016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 471 LK-LSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALE-TLMEGRTTIVIAHRLST-----------IKKA 537
Cdd:PLN03140 1017 VTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSIdifeafdelllMKRG 1096
|
....*.
gi 616431502 538 GQIIFL 543
Cdd:PLN03140 1097 GQVIYS 1102
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
350-549 |
3.45e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 350 ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYG-------LE---------SVYDiplskwrrkigY 413
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarLQqdpprnvegTVYD-----------F 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 414 VMQSNSMMSGTIRD--NILYGINRHVSDEELINYAKLANC--HDFIMQFDEGYDTLVGERGL-------KLSGGQRQRID 482
Cdd:PRK11147 87 VAEGIEEQAEYLKRyhDISHLVETDPSEKNLNELAKLQEQldHHNLWQLENRINEVLAQLGLdpdaalsSLSGGWLRKAA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 483 IARSFVKNPDILLLDEATANLDSESelkIqEALET-LMEGRTTIV-IAHRLSTIKK-AGQIIFLDKGQVT 549
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIET---I-EWLEGfLKTFQGSIIfISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
349-557 |
4.01e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.21 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKS----TIFNLIERMYEIESGDIKYGLESVYDIPlSKWRRKI-----GYVMQsNS 419
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRIS-EKERRNLvgaevAMIFQ-DP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 420 MMS----GTIRDNILYGI------NRHVSDEELINYAKLANCHDFIMQFDEgYDTlvgerglKLSGGQRQRIDIARSFVK 489
Cdd:PRK11022 99 MTSlnpcYTVGFQIMEAIkvhqggNKKTRRQRAIDLLNQVGIPDPASRLDV-YPH-------QLSGGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616431502 490 NPDILLLDEATANLDSESELKIQEALETLM--EGRTTIVIAHRLSTIKKAGQ-IIFLDKGQVTGKGTHSEL 557
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVAEAAHkIIVMYAGQVVETGKAHDI 241
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
348-547 |
4.62e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.18 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNliermyeiesgdIKYGLESvyDIPLSKWRR---KIGYVMQSNSM-MSG 423
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLR------------IMAGVDK--DFNGEARPQpgiKVGYLPQEPQLdPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 424 TIRDNILYG-------------INRHVSDE------------ELINYAKLANCHDFIMQFDEGYDTL--------VGerg 470
Cdd:TIGR03719 84 TVRENVEEGvaeikdaldrfneISAKYAEPdadfdklaaeqaELQEIIDAADAWDLDSQLEIAMDALrcppwdadVT--- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 471 lKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLmEGrTTIVIAH-RLSTIKKAGQIIFLDKGQ 547
Cdd:TIGR03719 161 -KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTHdRYFLDNVAGWILELDRGR 235
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
349-536 |
5.39e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.65 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIES--GDIKYGLESVY--DIPLSKwRRKIGYVMQS---NSMM 421
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRfkDIRDSE-ALGIVIIHQElalIPYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 422 SgtIRDNILYG--------INR---HVSDEELINYAKLanchdfimqfDEGYDTLVGERGLklsgGQRQRIDIARSFVKN 490
Cdd:NF040905 94 S--IAENIFLGnerakrgvIDWnetNRRARELLAKVGL----------DESPDTLVTDIGV----GKQQLVEIAKALSKD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 616431502 491 PDILLLDEATANL-DSESelkiqEALETLM-----EGRTTIVIAHRLSTIKK 536
Cdd:NF040905 158 VKLLILDEPTAALnEEDS-----AALLDLLlelkaQGITSIIISHKLNEIRR 204
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
86-283 |
7.00e-09 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 57.10 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 86 KIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFIsqkLPNLLPSIVTLVGSLIMLFIL---DWKMTLLT 162
Cdd:cd18585 65 RLLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLY---LRVLSPPVVALLVILATILFLaffSPALALIL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 163 FITIpIFVLIMIPLgrIMQKISTSTQSEIANFSGLLGRVLTE----MRLVKISNTERLELDNAHKNLNEIYKLGLKQAKI 238
Cdd:cd18585 142 LAGL-LLAGVVIPL--LFYRLGKKIGQQLVQLRAELRTELVDglqgMAELLIFGALERQRQQLEQLSDALIKEQRRLARL 218
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 616431502 239 AAVVQPISGIVMLLTIAIILGFGALEIATGAItAGTLIAMIFYVI 283
Cdd:cd18585 219 SGLSQALMILLSGLTVWLVLWLGAPLVQNGAL-DGALLAMLVFAV 262
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
350-573 |
7.92e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 350 ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKwRRKIG-YVMQSNSMM--SGTIR 426
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-AHQLGiYLVPQEPLLfpNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 427 DNILYGINRHVSDEELINyAKLA--NCHdfiMQFDEGYDTL-VGErglklsggqRQRIDIARSFVKNPDILLLDEATANL 503
Cdd:PRK15439 105 ENILFGLPKRQASMQKMK-QLLAalGCQ---LDLDSSAGSLeVAD---------RQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 504 D-SESELKIQEALETLMEGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSEL--------MASHAKYKNFVVSQKL 573
Cdd:PRK15439 172 TpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLstddiiqaITPAAREKSLSASQKL 251
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
355-559 |
1.31e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 355 SFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNS--MMSG-------TI 425
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNtdMLSPgeddtgrTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 426 RDNILyginRHVSDEELinyaklanCHDFIMQFdeGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDS 505
Cdd:PRK10938 103 AEIIQ----DEVKDPAR--------CEQLAQQF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 506 ESELKIQEALETLMEGRTTIV-IAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMA 559
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
353-560 |
1.43e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.95 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 353 DVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDI----------KYGLES-----VYDIPLSKW--RRKIGYVM 415
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplhfgDYSYRSqrirmIFQDPSTSLnpRQRISQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QS----NSMMSGTIRDNILYGINRHVSdeelinyakLANCHdfimqfdegydtlVGERGLKLSGGQRQRIDIARSFVKNP 491
Cdd:PRK15112 111 DFplrlNTDLEPEQREKQIIETLRQVG---------LLPDH-------------ASYYPHMLAPGQKQRLGLARALILRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616431502 492 DILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMAS 560
Cdd:PRK15112 169 KVIIADEALASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLAS 240
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
349-547 |
3.01e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVyDIPLSKWRRKIGYVM---QSNSMMSGTI 425
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMvhqELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 426 RDNILYGinRHVSDEELINYAKLANchDFIMQFDE-GYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLd 504
Cdd:PRK10982 91 MDNMWLG--RYPTKGMFVDQDKMYR--DTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 616431502 505 SESEL----KIQEALETlmEGRTTIVIAHRLSTIKK-AGQIIFLDKGQ 547
Cdd:PRK10982 166 TEKEVnhlfTIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
38-277 |
4.01e-08 |
|
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: 54.79 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSV-SHINW--NLIALFGGIFVINALLSGLGLYLLSKIGEKI-IYAIRSVLWeHIIQLKMPFFDKNESG 113
Cdd:cd18569 21 IPVFSRIFIDDILVgGLPDWlrPLLLGMALTALLQGLLTWLQQYYLLRLETKLaLSSSSRFFW-HVLRLPVEFFSQRYAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 114 QLMSRL-TDDTkvINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIA 192
Cdd:cd18569 100 DIASRVqSNDR--VANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 193 NFSGLLGRVLTEMRLVKISNTERlelD--------NAhKNLNEIYKLGLKQAKIAAVVQPISGivmlLTIAIILGFGALE 264
Cdd:cd18569 178 KLTGTTMSGLQMIETLKASGAES---DffsrwagyQA-KVLNAQQELGRTNQLLGALPTLLSA----LTNAAILGLGGLL 249
|
250
....*....|...
gi 616431502 265 IATGAITAGTLIA 277
Cdd:cd18569 250 VMDGALTIGMLVA 262
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
336-534 |
4.23e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYdiplskwrrkigYVM 415
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR------------FAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSMMSG--------------TIRDNILYGI--NRH-VSDEELINYAKLANCHDFIMQFDEgyDTLVGErglkLSGGQR 478
Cdd:PRK11288 73 TTAALAAGvaiiyqelhlvpemTVAENLYLGQlpHKGgIVNRRLLNYEAREQLEHLGVDIDP--DTPLKY----LSIGQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 616431502 479 QRIDIARSFVKNPDILLLDEATANLDS-ESE--LKIQEALETlmEGRTTIVIAHRLSTI 534
Cdd:PRK11288 147 QMVEIAKALARNARVIAFDEPTSSLSArEIEqlFRVIRELRA--EGRVILYVSHRMEEI 203
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
351-564 |
4.87e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.67 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkyglesvyDIPLSKWRRKIGYVMqsNSMMSGTirDNI- 429
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--------DIKGSAALIAISSGL--NGQLTGI--ENIe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 430 ----LYGINRHVSDEELINYAKLANCHDFIMQFDEGYdtlvgerglklSGGQRQRIDIARSFVKNPDILLLDEATANLDS 505
Cdd:PRK13545 108 lkglMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616431502 506 ESELKIQEALETLME-GRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMASHAKY 564
Cdd:PRK13545 177 TFTKKCLDKMNEFKEqGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEF 237
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
349-535 |
6.79e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIES--GDIKYGLESV--YDIPLSKwRRKIGYVMQSNSMMSG- 423
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELqaSNIRDTE-RAGIAIIHQELALVKEl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 424 TIRDNILYG--INRHvsdeELINYAKL-ANCHDFI--MQFDEGYDTLVGErglkLSGGQRQRIDIARSFVKNPDILLLDE 498
Cdd:PRK13549 98 SVLENIFLGneITPG----GIMDYDAMyLRAQKLLaqLKLDINPATPVGN----LGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 616431502 499 ATANLdSESE----LKIQEALETlmEGRTTIVIAHRLSTIK 535
Cdd:PRK13549 170 PTASL-TESEtavlLDIIRDLKA--HGIACIYISHKLNEVK 207
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
350-528 |
7.34e-08 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 52.75 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 350 ILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSkWRRKIGYVMQSNSMMSG-TIRDN 428
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-PHENILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 429 iLYGINRHVSDEELinyaklaNCHDFImqfdegydTLVGERGLK------LSGGQRQRIDIARSFVKNPDILLLDEATAN 502
Cdd:TIGR01189 94 -LHFWAAIHGGAQR-------TIEDAL--------AAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*....
gi 616431502 503 LDSESelkiQEALETLME---GRTTIVIA 528
Cdd:TIGR01189 158 LDKAG----VALLAGLLRahlARGGIVLL 182
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
335-558 |
8.77e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLI---------ERMYEIeSGDIKYGLESVYDIPLS 405
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgggaPRGARV-TGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 406 KW-RRKIGYVMQSNSMMSGTIRDNILYGINRHVS--------DEELINYA-KLAnchdfimqfdeGYDTLVGERGLKLSG 475
Cdd:PRK13547 80 RLaRLRAVLPQAAQPAFAFSAREIVLLGRYPHARragalthrDGEIAWQAlALA-----------GATALVGRDVTTLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 476 GQRQRIDIARSFVK---------NPDILLLDEATANLDSESELKIQEALETLME----GRTTIVIAHRLSTiKKAGQIIF 542
Cdd:PRK13547 149 GELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwnlGVLAIVHDPNLAA-RHADRIAM 227
|
250
....*....|....*.
gi 616431502 543 LDKGQVTGKGTHSELM 558
Cdd:PRK13547 228 LADGAIVAHGAPADVL 243
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
349-534 |
1.21e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKY-GLESVYDIPLSKWRRKIGYVMQS-NSMMSGTIR 426
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlGKEVTFNGPKSSQEAGIGIIHQElNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 427 DNILYGiNRHVSDEELINYAKLANCHDFIMQ---FDEGYDTLVGErglkLSGGQRQRIDIARSFVKNPDILLLDEATANL 503
Cdd:PRK10762 98 ENIFLG-REFVNRFGRIDWKKMYAEADKLLArlnLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190
....*....|....*....|....*....|..
gi 616431502 504 -DSESELKIQEALETLMEGRTTIVIAHRLSTI 534
Cdd:PRK10762 173 tDTETESLFRVIRELKSQGRGIVYISHRLKEI 204
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
38-295 |
1.40e-07 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 53.38 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 38 VPLFTGRIVDKFSVSHIN-----WNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNES 112
Cdd:cd18560 15 APLFLGRAVNALTLAKVKdlesaVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWHLSKKT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 113 GQLMSRLTDDTKVINEFISQKLPNLLPSIVTL-VGSLIMLFILDWKMTLLTFITIPIFVL--IMIPLGRIMQKISTSTQ- 188
Cdd:cd18560 95 GEVVRIMDRGTESANTLLSYLVFYLVPTLLELiVVSVVFAFHFGAWLALIVFLSVLLYGVftIKVTEWRTKFRRAANKKd 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 189 ---SEIANFSgllgrvLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEI 265
Cdd:cd18560 175 neaHDIAVDS------LLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTLGLLLAGYRV 248
|
250 260 270
....*....|....*....|....*....|
gi 616431502 266 ATGAITAGTLIAMIFYVIQLSMPLINLSTL 295
Cdd:cd18560 249 VDGGLSVGDFVAVNTYIFQLFQPLNFLGTI 278
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
360-531 |
1.57e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 360 QGQVSAFVGPSGSGKSTIFNliermyeIESGDIK-----YGLESVYDIPLSKWR-------------------RKIGYVM 415
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVK-------ILSGELIpnlgdYEEEPSWDEVLKRFRgtelqnyfkklyngeikvvHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSNSMMSGTIRDnILYGINRHVSDEELINYAKLANCHDfimqfdegydtlvgeRGLK-LSGGQRQRIDIARSFVKNPDIL 494
Cdd:PRK13409 171 LIPKVFKGKVRE-LLKKVDERGKLDEVVERLGLENILD---------------RDISeLSGGELQRVAIAAALLRDADFY 234
|
170 180 190
....*....|....*....|....*....|....*..
gi 616431502 495 LLDEATANLDSESELKIQEALETLMEGRTTIVIAHRL 531
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
335-535 |
1.67e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.06 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYE--IESGDIKYGLESVYDIPLSKWRRK-I 411
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 412 GYVMQSNSMMSG-TIRDNILYGiNRHVSDEELINYAKLA-NCHDFI--MQFDEGYDTL-VGERGlklsGGQRQRIDIARS 486
Cdd:TIGR02633 81 VIIHQELTLVPElSVAENIFLG-NEITLPGGRMAYNAMYlRAKNLLreLQLDADNVTRpVGDYG----GGQQQLVEIAKA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 616431502 487 FVKNPDILLLDEATANL-DSESELKIQEALETLMEGRTTIVIAHRLSTIK 535
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVK 205
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
351-553 |
1.74e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 52.62 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFN-----LIERMYEIESGDIK-----YGLES---VYDIPLSKwrrkIGYVMQS 417
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypALARRLHLKKEQPGnhdriEGLEHidkVIVIDQSP----IGRTPRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 418 NSMM-SG---TIRD----------------NILYGiNRHVSD----------EELINYAKLANCHDFIMQFDEGYDTLvG 467
Cdd:cd03271 87 NPATyTGvfdEIRElfcevckgkrynretlEVRYK-GKSIADvldmtveealEFFENIPKIARKLQTLCDVGLGYIKL-G 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 468 ERGLKLSGGQRQRIDIARSFVK---NPDILLLDEATANLDSESELKIQEALETLME-GRTTIVIAHRLSTIKKAGQIIFL 543
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWIIDL 244
|
250
....*....|....*.
gi 616431502 544 -----DK-GQVTGKGT 553
Cdd:cd03271 245 gpeggDGgGQVVASGT 260
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
331-504 |
2.73e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.10 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 331 IDDGVLSFEHVDfkydVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVyDI--PLSKWR 408
Cdd:COG1129 252 PGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIrsPRDAIR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 409 RKIGYV----MQSNSMMSGTIRDNILYGINRHVSDEELINYAKL-ANCHDFIMQFD---EGYDTLVGErglkLSGGQRQR 480
Cdd:COG1129 327 AGIAYVpedrKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRErALAEEYIKRLRiktPSPEQPVGN----LSGGNQQK 402
|
170 180
....*....|....*....|....
gi 616431502 481 IDIARSFVKNPDILLLDEATANLD 504
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGID 426
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
471-556 |
3.12e-07 |
|
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: 50.65 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 471 LKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLME--GRTTIVIAHRLSTIKKAGQIIFLDKGQV 548
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEGEP 149
|
....*...
gi 616431502 549 TGKGTHSE 556
Cdd:cd03222 150 GVYGIASQ 157
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
351-573 |
4.46e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.09 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYdIPLSKWRRKIGYVMQSNS---MMSGtiRD 427
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISDVHQNMGYCPQFDAiddLLTG--RE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 428 NI-LYGINRHVSDEELinyAKLANCHDFIMQFDEGYDTLVGerglKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSE 506
Cdd:TIGR01257 2032 HLyLYARLRGVPAEEI---EKVANWSIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616431502 507 SELKIQEALETLM-EGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGThselmASHAKYK---NFVVSQKL 573
Cdd:TIGR01257 2105 ARRMLWNTIVSIIrEGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGT-----IQHLKSKfgdGYIVTMKI 2171
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
467-557 |
5.34e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 467 GERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLM-EGRTTIVIAHRLSTIKK-AGQIIFLD 544
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQYMEEAEQlAHELTVID 218
|
90
....*....|...
gi 616431502 545 KGQVTGKGTHSEL 557
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
97-294 |
6.61e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 51.39 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 97 EHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSiVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPL 176
Cdd:cd18779 83 EHLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALLDG-TLVLGYLALLFAQSPLLGLVVLGLAALQVALLLAT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 177 GRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAI 256
Cdd:cd18779 162 RRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLV 241
|
170 180 190
....*....|....*....|....*....|....*...
gi 616431502 257 ILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLST 294
Cdd:cd18779 242 LLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVG 279
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
83-302 |
7.30e-07 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC 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: 350015 [Multi-domain] Cd Length: 294 Bit Score: 51.29 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 83 IGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKvINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLT 162
Cdd:cd18571 69 ISSRINISIISDFLIKLMRLPISFFDTKMTGDILQRINDHSR-IESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 163 FITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVV 242
Cdd:cd18571 148 LIGSVLYILWILLFLKKRKKLDYKRFDLSSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQ 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 243 QPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKA 302
Cdd:cd18571 228 QIGALFINQLKNILITFLAAKLVIDGEITLGMMLAIQYIIGQLNSPIEQLIGFIQSLQDA 287
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
351-547 |
7.65e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.63 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNliERMYEIESGDIKYGLESVYDIPLskwrrkigyvmqsnsMMSGTIRDNIL 430
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLISFLPKFSRNKL---------------IFIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 431 YGInrhvsdeelinyaklanchdfimqfdeGYDTLvGERGLKLSGGQRQRIDIARSFVKNPD--ILLLDEATANLDSESE 508
Cdd:cd03238 74 VGL---------------------------GYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 616431502 509 LKIQEALETLM-EGRTTIVIAHRLSTIKKAGQIIFLDKGQ 547
Cdd:cd03238 126 NQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
344-534 |
8.84e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 344 KYDVKKIlDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIK-YGLESVYDIPLSKWRRKIGYVMQS---NS 419
Cdd:PRK09700 273 SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRlNGKDISPRSPLDAVKKGMAYITESrrdNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 420 MMSG-TIRDNIlyGINRHVSDEELINYAKLANCHDFIMQFDEGYDTL------VGERGLKLSGGQRQRIDIARSFVKNPD 492
Cdd:PRK09700 352 FFPNfSIAQNM--AISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLalkchsVNQNITELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 616431502 493 ILLLDEATANLDSESELKIQEALETLM-EGRTTIVIAHRLSTI 534
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEI 472
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
363-545 |
1.02e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.53 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 363 VSAFVGPSGSGKSTIfnliermyeIESgdIKYGLESvydiplSKWRRKIGYVMQSNSMMSGTIRDNIlYGINRHVSDEEL 442
Cdd:cd03240 24 LTLIVGQNGAGKTTI---------IEA--LKYALTG------ELPPNSKGGAHDPKLIREGEVRAQV-KLAFENANGKKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 443 I---NYAKLANCHdFIMQfDEGYDTLVGERGLkLSGGQRQ------RIDIARSFVKNPDILLLDEATANLDSESelkIQE 513
Cdd:cd03240 86 TitrSLAILENVI-FCHQ-GESNWPLLDMRGR-CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---IEE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 616431502 514 ALETLMEGRTT------IVIAHRLSTIKKAGQIIFLDK 545
Cdd:cd03240 160 SLAEIIEERKSqknfqlIVITHDEELVDAADHIYRVEK 197
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
351-566 |
1.16e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDI-KYGLESVYDIplskwrrkigyvmqsNSMMSGTIR--D 427
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSVIAI---------------SAGLSGQLTgiE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 428 NI-----LYGINRHVSDE---ELINYAKLAnchDFIMQFDEGYdtlvgerglklSGGQRQRIDIARSFVKNPDILLLDEA 499
Cdd:PRK13546 105 NIefkmlCMGFKRKEIKAmtpKIIEFSELG---EFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616431502 500 TANLDS----ESELKIQEALEtlmEGRTTIVIAHRLSTIKK-AGQIIFLDKGQVTGKGTHSELMASHAKYKN 566
Cdd:PRK13546 171 LSVGDQtfaqKCLDKIYEFKE---QNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKYEAFLN 239
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
89-184 |
1.38e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 50.22 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 89 YAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILdwkmtlltfitIPI 168
Cdd:cd18605 75 RRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQ-----------LPW 143
|
90
....*....|....*.
gi 616431502 169 FVLIMIPLGRIMQKIS 184
Cdd:cd18605 144 LLLLLLPLAFIYYRIQ 159
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
358-533 |
1.44e-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: 50.94 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 358 IPQ-GQVSAFVGPSGSGKSTIFNliermyeIESGDIK-----YGLESVYDIPLSKWR-------------------RKIG 412
Cdd:COG1245 95 VPKkGKVTGILGPNGIGKSTALK-------ILSGELKpnlgdYDEEPSWDEVLKRFRgtelqdyfkklangeikvaHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 413 YVMQSNSMMSGTIRDnILYGINRHVSDEELINYAKLANchdfimqfdegydtlVGERGLK-LSGGQRQRIDIARSFVKNP 491
Cdd:COG1245 168 YVDLIPKVFKGTVRE-LLEKVDERGKLDELAEKLGLEN---------------ILDRDISeLSGGELQRVAIAAALLRDA 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 616431502 492 DILLLDEATANLDSESELK----IQEALEtlmEGRTTIVIAHRLST 533
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNvarlIRELAE---EGKYVLVVEHDLAI 274
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
360-545 |
1.60e-06 |
|
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: 48.14 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 360 QGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYglesvydiplskwrrkigyvmqsnsmmsgtirdnilyginrhVSD 439
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY------------------------------------------IDG 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 440 EELINYAklanchdfimqFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLM 519
Cdd:smart00382 39 EDILEEV-----------LDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180 190
....*....|....*....|....*....|...
gi 616431502 520 -------EGRTTIVIAHRLSTIKKAGQIIFLDK 545
Cdd:smart00382 108 llllkseKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
348-507 |
1.76e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNliermyeiesgdIKYGLESVYD---IPLSKWrrKIGYVMQSNSM-MSG 423
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLR------------IMAGVDKEFEgeaRPAPGI--KVGYLPQEPQLdPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 424 TIRDNI-------------------LYGINRHVSDEELINYAKL------ANCHDFIMQFDEGYDTL--------VGerg 470
Cdd:PRK11819 86 TVRENVeegvaevkaaldrfneiyaAYAEPDADFDALAAEQGELqeiidaADAWDLDSQLEIAMDALrcppwdakVT--- 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 616431502 471 lKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSES 507
Cdd:PRK11819 163 -KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
352-504 |
1.91e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 352 DDVSFQIPQGQVSAFVGPSGSGKST-----------------IFNliermYEIESGDIKYglesvydiplskwRRKIGYV 414
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTtmkmltgllpasegeawLFG-----QPVDAGDIAT-------------RRRVGYM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSG-TIRDNI-----LYginrHVSDEElINyaklANCHDFIMQFD-EGY-DTLVGErglkLSGGQRQRIDIARS 486
Cdd:NF033858 345 SQAFSLYGElTVRQNLelharLF----HLPAAE-IA----ARVAEMLERFDlADVaDALPDS----LPLGIRQRLSLAVA 411
|
170
....*....|....*...
gi 616431502 487 FVKNPDILLLDEATANLD 504
Cdd:NF033858 412 VIHKPELLILDEPTSGVD 429
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
84-305 |
2.01e-06 |
|
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: 49.74 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 84 GEKIIYAIRSVLWEHIIQLKMPFfDKNESGQLMSRLTD-DTkvINEFISQKlpnllpSIVTLVG------SLIMLFILDW 156
Cdd:cd18587 70 GKRADVILSSRLFERVLGLRLEA-RPASVGSFANNLREfES--VRDFFTSA------TLTALIDlpfvllFLAVIALIGG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 157 KMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQA 236
Cdd:cd18587 141 PLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSR 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616431502 237 KIAAVVQPISGIVM-LLTIAIILgFGALEIATGAITAGTLIAMifyVIqLS----MPLINLSTLVTDYKKAVGA 305
Cdd:cd18587 221 LLSSSATNFAQFVQqLVTVAIVI-VGVYLISDGELTMGGLIAC---VI-LSgralAPLGQIAGLLTRYQQARTA 289
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
335-500 |
2.29e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.51 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIkygleSVY--DIPLSKWRR--- 409
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV-----EVLggDMADARHRRavc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 410 -KIGYVMQ---SNSMMSGTIRDNI-----LYGINRhvsdeelinyaklANCHDFImqfdegyDTLVGERGL--------- 471
Cdd:NF033858 76 pRIAYMPQglgKNLYPTLSVFENLdffgrLFGQDA-------------AERRRRI-------DELLRATGLapfadrpag 135
|
170 180
....*....|....*....|....*....
gi 616431502 472 KLSGGQRQRIDIARSFVKNPDILLLDEAT 500
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
39-309 |
2.45e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 49.41 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 39 PLFTGRIVDKF-SVSHINWN----LIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESG 113
Cdd:cd18579 17 PLLLGLLISYLsSYPDEPLSegylLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRKALRLSSSARQETSTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 114 QLMSRLTDDTKVINEFISQkLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKIststQSEIAN 193
Cdd:cd18579 97 EIVNLMSVDVQRIEDFFLF-LHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKLISKL----RKKLMK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 194 FS----GLLGRVLTEMRLVKISNTErlelDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLT--IAIILGFGALEIAT 267
Cdd:cd18579 172 ATdervKLTNEILSGIKVIKLYAWE----KPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTpvLVSLATFATYVLLG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 616431502 268 GAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRI 309
Cdd:cd18579 248 NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
56-198 |
2.92e-06 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 49.33 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 56 WNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLP 135
Cdd:cd18584 37 LPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLP 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616431502 136 NLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLL 198
Cdd:cd18584 117 QLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKAAQAASRRQWAALSRLSGHF 179
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
335-555 |
2.97e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.02 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLI--ERMYEIESGDIKYGLESVYDI-PLSKWRRKI 411
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELsPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 412 GYVMQSNSMMSGTIRDNILY-GIN--RHVSDEELINYAKLAN-CHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSF 487
Cdd:PRK09580 81 FMAFQYPVEIPGVSNQFFLQtALNavRSYRGQEPLDRFDFQDlMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616431502 488 VKNPDILLLDEATANLDSESELKIQEALETLMEG-RTTIVIAH--RLSTIKKAGQIIFLDKGQVTGKGTHS 555
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFT 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
461-557 |
4.46e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 49.63 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 461 GYDTLvGERGLKLSGGQRQRIDIARSFVK---NPDILLLDEATANLDSESELKIQEALETLME-GRTTIVIAHRLSTIKK 536
Cdd:TIGR00630 819 GYIRL-GQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDkGNTVVVIEHNLDVIKT 897
|
90 100
....*....|....*....|....*..
gi 616431502 537 AGQIIFL-----DK-GQVTGKGTHSEL 557
Cdd:TIGR00630 898 ADYIIDLgpeggDGgGTVVASGTPEEV 924
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
336-560 |
5.59e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 336 LSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlESVydiplskwrrKIGYVM 415
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-ENA----------NIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 416 QSnsmmsgtirdnilyginrHVSDeelinYAKLANCHDFIMQF-DEGYDTLVgERGL----------------KLSGGQR 478
Cdd:PRK15064 389 QD------------------HAYD-----FENDLTLFDWMSQWrQEGDDEQA-VRGTlgrllfsqddikksvkVLSGGEK 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 479 QRIDIARSFVKNPDILLLDEATANLDSESELKIQEALEtLMEGrTTIVIAH-R--LSTIkkAGQII-FLDKGQVTGKGTH 554
Cdd:PRK15064 445 GRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE-KYEG-TLIFVSHdRefVSSL--ATRIIeITPDGVVDFSGTY 520
|
....*.
gi 616431502 555 SELMAS 560
Cdd:PRK15064 521 EEYLRS 526
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
348-563 |
7.56e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLI----ERMYEIESGDIKYGLESVYDIpLSKWRRKIGYVMQSNSMM-S 422
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDVHFpH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 423 GTIRDNILYGI------NRH--VSDEELINyaKLANCHDFIMQFDEGYDTLVGE---RGLklSGGQRQRIDIARSFVKNP 491
Cdd:TIGR00956 153 LTVGETLDFAArcktpqNRPdgVSREEYAK--HIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 492 DILLLDEATANLDSESELKIQEALETLmegrTTIVIAHRLSTIKKAGQ--------IIFLDKGQVTGKGThselmASHAK 563
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTS----ANILDTTPLVAIYQCSQdayelfdkVIVLYEGYQIYFGP-----ADKAK 299
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
335-504 |
2.16e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.33 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFK-YDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDI-PLSKWRRKIG 412
Cdd:COG3845 257 VLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLsPRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 413 YV----MQSNSMMSGTIRDNILygINRHVSDEE----LINYAKL-ANCHDFIMQFD---EGYDTLVGerglKLSGGQRQR 480
Cdd:COG3845 337 YIpedrLGRGLVPDMSVAENLI--LGRYRRPPFsrggFLDRKAIrAFAEELIEEFDvrtPGPDTPAR----SLSGGNQQK 410
|
170 180
....*....|....*....|....
gi 616431502 481 IDIARSFVKNPDILLLDEATANLD 504
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLD 434
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
325-553 |
2.30e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.16 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 325 DSENVLIDDGVlsfeHVDFKYDVKKI--LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlesvyDI 402
Cdd:PRK10261 8 DARDVLAVENL----NIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCD-----KM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 403 PLSKWRRKIGYVM-QSNSMMSG---------------------TIRDNILYGINRH--VSDEELINYAKLANCHDFIMQf 458
Cdd:PRK10261 79 LLRRRSRQVIELSeQSAAQMRHvrgadmamifqepmtslnpvfTVGEQIAESIRLHqgASREEAMVEAKRMLDQVRIPE- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 459 degYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRT--TIVIAHRLSTIKK 536
Cdd:PRK10261 158 ---AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAE 234
|
250
....*....|....*...
gi 616431502 537 -AGQIIFLDKGQVTGKGT 553
Cdd:PRK10261 235 iADRVLVMYQGEAVETGS 252
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
361-532 |
3.51e-05 |
|
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: 45.82 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 361 GQVSAFVGPSGSGKSTIFnliermyEIESGDI-----KYGLESVYDIPLSKWR-------------------RKIGYVMQ 416
Cdd:cd03236 26 GQVLGLVGPNGIGKSTAL-------KILAGKLkpnlgKFDDPPDWDEILDEFRgselqnyftkllegdvkviVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 417 SNSMMSGTIRDNILYGINRHVSDEeLINYAKLANchdfimqfdegydtlVGERGL-KLSGGQRQRIDIARSFVKNPDILL 495
Cdd:cd03236 99 IPKAVKGKVGELLKKKDERGKLDE-LVDQLELRH---------------VLDRNIdQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 616431502 496 LDEATANLDSESELKIQEALETLME-GRTTIVIAHRLS 532
Cdd:cd03236 163 FDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLA 200
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
97-188 |
6.92e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 45.16 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 97 EHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLImlfildwkmtlLTFITIPIFVLIMIPL 176
Cdd:cd18603 82 HNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLV-----------VISISTPIFLVVIIPL 150
|
90
....*....|....*..
gi 616431502 177 GRI---MQK--ISTSTQ 188
Cdd:cd18603 151 AILyffIQRfyVATSRQ 167
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
474-529 |
7.56e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 7.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 474 SGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALetLMEGRTTIVIAH 529
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
95-188 |
9.21e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 44.42 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 95 LWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLfildwkmtlltFITIPIFVLIMI 174
Cdd:cd18580 78 LLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVI-----------AIVSPYFLIVLP 146
|
90
....*....|....*....
gi 616431502 175 PLG---RIMQK--ISTSTQ 188
Cdd:cd18580 147 PLLvvyYLLQRyyLRTSRQ 165
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
96-176 |
1.18e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 44.39 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 96 WEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLImlfildwkmtlLTFITIPIFVLIMIP 175
Cdd:cd18606 75 LKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFI-----------LIIIYLPWFAIALPP 143
|
.
gi 616431502 176 L 176
Cdd:cd18606 144 L 144
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
351-560 |
1.21e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.79 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTI-FNLIermyeIESGDIKYgLESvydipLSKWRRkigyvmQSNSMMSGTIRDNI 429
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLaFDTI-----YAEGQRRY-VES-----LSAYAR------QFLGQMDKPDVDSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 430 ----------LYGINRHV-----SDEELINYAKL-------ANCHDFIMQFDEGYDTLVGERGlKLSGGQRQRIDIARSF 487
Cdd:cd03270 74 eglspaiaidQKTTSRNPrstvgTVTEIYDYLRLlfarvgiRERLGFLVDVGLGYLTLSRSAP-TLSGGEAQRIRLATQI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616431502 488 VKNPD--ILLLDEATANLDSESELKIQEALETLME-GRTTIVIAHRLSTIKKAGQIIflDKGqvTGKGTH-SELMAS 560
Cdd:cd03270 153 GSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVI--DIG--PGAGVHgGEIVAQ 225
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
348-403 |
1.38e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.86 E-value: 1.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 616431502 348 KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLI--ERMYEIESGDIKYGLESVYDIP 403
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLE 77
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
351-504 |
1.42e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.61 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKY------------GLES--VYdipLSKWRRKIGYV-- 414
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdghevvtrspqdGLANgiVY---ISEDRKRDGLVlg 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMSGTIRDNI--LYGINRHVSDEELINyaklanchDFIMQFD---EGYDTLVGErglkLSGGQRQRIDIARSFVK 489
Cdd:PRK10762 345 MSVKENMSLTALRYFsrAGGSLKHADEQQAVS--------DFIRLFNiktPSMEQAIGL----LSGGNQQKVAIARGLMT 412
|
170
....*....|....*
gi 616431502 490 NPDILLLDEATANLD 504
Cdd:PRK10762 413 RPKVLILDEPTRGVD 427
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
335-521 |
1.79e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDVKKIL-DDVSFQIPQGQVSAFVGPSGSGKSTIFNLIermyeieSGDIKyglesvydiPLSkwrrkiGY 413
Cdd:PLN03073 508 IISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLI-------SGELQ---------PSS------GT 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 414 VMQSNSMMSGTIRDNilyginrHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLK----------LSGGQRQRIDI 483
Cdd:PLN03073 566 VFRSAKVRMAVFSQH-------HVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSRVAF 638
|
170 180 190
....*....|....*....|....*....|....*...
gi 616431502 484 ARSFVKNPDILLLDEATANLDseselkiQEALETLMEG 521
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLD-------LDAVEALIQG 669
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
84-549 |
1.98e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.19 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 84 GEKIIYAIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINeFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTF 163
Cdd:PRK10522 76 GHHFVYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNIT-IAFVRLPELVQGIILTLGSAAYLAWLSPKMLLVTA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 164 ITIPI-----FVLIMiplgRIMQKISTSTQSEIA---NFSGLL-GRvlTEMRLvkisNTERLEL--DNAHKNLNEIYKLG 232
Cdd:PRK10522 155 IWMAVtiwggFVLVA----RVYKHMATLRETEDKlynDYQTVLeGR--KELTL----NRERAEYvfENEYEPDAQEYRHH 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 233 LKQAKI---AAVvqPISGIVMLLTIAII----LGFGALEIATGAITAGTLiamIFyviqLSMPLINlstlvtdykkAVGA 305
Cdd:PRK10522 225 IIRADTfhlSAV--NWSNIMMLGAIGLVfymaNSLGWADTNVAATYSLTL---LF----LRTPLLS----------AVGA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 306 -----SSRIY--EIMQEPIEPTEALEDSENVLIDDGVLSFEHVDFKYDVKKI-LDDVSFQIPQGQVSAFVGPSGSGKSTI 377
Cdd:PRK10522 286 lptllSAQVAfnKLNKLALAPYKAEFPRPQAFPDWQTLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 378 FNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNSMMSGtirdniLYGINRHVSDEELINY--AKLANCHDfi 455
Cdd:PRK10522 366 AMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQ------LLGPEGKPANPALVEKwlERLKMAHK-- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 456 MQFDEGYDTLvgergLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSE-SELKIQEALETLME-GRTTIVIAHRLST 533
Cdd:PRK10522 438 LELEDGRISN-----LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfRREFYQVLLPLLQEmGKTIFAISHDDHY 512
|
490
....*....|....*.
gi 616431502 534 IKKAGQIIFLDKGQVT 549
Cdd:PRK10522 513 FIHADRLLEMRNGQLS 528
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
316-534 |
3.05e-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: 43.66 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 316 PIEPTEaledsenvlIDDGVLSFEHVDfKYDV----KKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIE-SG 390
Cdd:TIGR02633 247 PHEPHE---------IGDVILEARNLT-CWDVinphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEG 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 391 DIKYGLESVyDI--PLSKWRRKIGYVMQSNSmmsgtiRDNIL--YGINRHVSDEELINYAklanchdFIMQFDEGYDTLV 466
Cdd:TIGR02633 317 NVFINGKPV-DIrnPAQAIRAGIAMVPEDRK------RHGIVpiLGVGKNITLSVLKSFC-------FKMRIDAAAELQI 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 467 GERGLK---------------LSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLM-EGRTTIVIAHR 530
Cdd:TIGR02633 383 IGSAIQrlkvktaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSE 462
|
....
gi 616431502 531 LSTI 534
Cdd:TIGR02633 463 LAEV 466
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
360-392 |
5.17e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 42.11 E-value: 5.17e-04
10 20 30
....*....|....*....|....*....|...
gi 616431502 360 QGQVSAFVGPSGSGKSTIFNLIERMYEIESGDI 392
Cdd:PRK00098 163 AGKVTVLAGQSGVGKSTLLNALAPDLELKTGEI 195
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
349-560 |
6.27e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 42.20 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 349 KILDDVSFQIPQGQVSAFVGPSGSGKS----TIFNLIERMYEIESGDIKYGlesvyDIPLSKW----RRKIgyVMQSNSM 420
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWN-----GIDLLKLspreRRKI--IGREIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 421 M----------SGTIRDNILYGI--------------NRHVSDEELINYAKLANcHDFIMQfdeGYDtlvgergLKLSGG 476
Cdd:COG4170 94 IfqepsscldpSAKIGDQLIEAIpswtfkgkwwqrfkWRKKRAIELLHRVGIKD-HKDIMN---SYP-------HELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 477 QRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGR-TTIV-IAHRLSTIKK-AGQIIFLDKGQVTGKGT 553
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQgTSILlISHDLESISQwADTITVLYCGQTVESGP 242
|
....*..
gi 616431502 554 HSELMAS 560
Cdd:COG4170 243 TEQILKS 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
351-564 |
1.08e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 351 LDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIK-YGLESVYDIPLSKWRRkiGYVMQSNSMMSGTIRDNI 429
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITlHGKKINNHNANEAINH--GFALVTEERRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 430 LYGINRHVS--DEELINYAKLANCHdfiMQFDE------------GYDTLVGErglkLSGGQRQRIDIARSFVKNPDILL 495
Cdd:PRK10982 342 DIGFNSLISniRNYKNKVGLLDNSR---MKSDTqwvidsmrvktpGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 496 LDEATANLDSESELKI-QEALETLMEGRTTIVIAHRL-STIKKAGQIIFLDKGQVTG-----KGTHSELMASHAKY 564
Cdd:PRK10982 415 LDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLVAGivdtkTTTQNEILRLASLH 490
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
346-520 |
1.21e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 40.56 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 346 DVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGlesvyDIPLSKWRrkigyvmqsnsmmsGTI 425
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ-----GEPIRRQR--------------DEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 426 RDNILY-----GINRHVSDEE-LINYAKLANC-HDFIMQfdegyDTL--VGERGLK------LSGGQRQRIDIARSFVKN 490
Cdd:PRK13538 73 HQDLLYlghqpGIKTELTALEnLRFYQRLHGPgDDEALW-----EALaqVGLAGFEdvpvrqLSAGQQRRVALARLWLTR 147
|
170 180 190
....*....|....*....|....*....|.
gi 616431502 491 PDILLLDEA-TAnLDSESelkiQEALETLME 520
Cdd:PRK13538 148 APLWILDEPfTA-IDKQG----VARLEALLA 173
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
99-203 |
1.28e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 41.05 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 99 IIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIM---IP 175
Cdd:cd18602 93 IVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQkfyRA 172
|
90 100
....*....|....*....|....*....
gi 616431502 176 LGRIMQKISTSTQSEI-ANFSGLLGRVLT 203
Cdd:cd18602 173 SSRELQRLDNITKSPVfSHFSETLGGLTT 201
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
471-541 |
1.78e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.27 E-value: 1.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616431502 471 LKLSGGQRQRIDIARSF----VKNPDILLLDEATANLDSESELKIQEAL-ETLMEGRTTIVIAHRLSTIKKAGQII 541
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAIlEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
360-381 |
1.99e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.69 E-value: 1.99e-03
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
352-531 |
2.88e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.09 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 352 DDVSFQIPQGQVSAFVGPSGSGKS-TIFNLIERMYE--IESGDIKYGLESVYDIP---LSKWR-RKIGYVMQS-----NS 419
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATFNGREILNLPekeLNKLRaEQISMIFQDpmtslNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 420 MMSgtIRDNIL------YGINRHVSDEE---LINYAKLANCHDFIMQFDEgydtlvgerglKLSGGQRQRIDIARSFVKN 490
Cdd:PRK09473 113 YMR--VGEQLMevlmlhKGMSKAEAFEEsvrMLDAVKMPEARKRMKMYPH-----------EFSGGMRQRVMIAMALLCR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 616431502 491 PDILLLDEATANLDSESELKIQEALETLM-EGRTTIV-IAHRL 531
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIImITHDL 222
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
470-529 |
4.27e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 4.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616431502 470 GLKLsggqrqRIDIARSFVKNPDILLLDEATANLDSESelkIQeALETLMEGR--TTIVIAH 529
Cdd:PRK15064 159 GWKL------RVLLAQALFSNPDILLLDEPTNNLDINT---IR-WLEDVLNERnsTMIIISH 210
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
335-544 |
4.37e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 335 VLSFEHVDFKYDvKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPlSKWRRKIGYV 414
Cdd:PRK13541 1 MLSLHQLQFNIE-QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-KPYCTYIGHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 415 MQSNSMMsgTIRDNILYGINRHVSDEEL---INYAKLancHDFImqfdegydtlvGERGLKLSGGQRQRIDIARSFVKNP 491
Cdd:PRK13541 79 LGLKLEM--TVFENLKFWSEIYNSAETLyaaIHYFKL---HDLL-----------DEKCYSLSSGMQKIVAIARLIACQS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 492 DILLLDEATANLDSESElKIQEALETLMEGRTTIVI--AHRLSTIKKAgQIIFLD 544
Cdd:PRK13541 143 DLWLLDEVETNLSKENR-DLLNNLIVMKANSGGIVLlsSHLESSIKSA-QILQLD 195
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
455-552 |
4.79e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.21 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 455 IMQFDEGYDTLVGERGLK-LSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIAHRLS- 532
Cdd:PLN03140 318 ILGLDICKDTIVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQp 397
|
90 100
....*....|....*....|...
gi 616431502 533 ---TIKKAGQIIFLDKGQVTGKG 552
Cdd:PLN03140 398 apeTFDLFDDIILLSEGQIVYQG 420
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
473-543 |
5.77e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 5.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616431502 473 LSGGQRQRIDIARSF---VKNPDILLLDEATANLDSESELKIQEALETLM-EGRTTIVIAHRLSTIKKAGQIIFL 543
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
461-551 |
6.78e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 461 GYDTLvGERGLKLSGGQRQRIDIARSFV---KNPDILLLDEATANLDSESELKIQEALETLM-EGRTTIVIAHRLSTIKK 536
Cdd:PRK00635 1689 GYLPL-GQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVsLGHSVIYIDHDPALLKQ 1767
|
90
....*....|....*
gi 616431502 537 AGQIIFLdkGQVTGK 551
Cdd:PRK00635 1768 ADYLIEM--GPGSGK 1780
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
472-518 |
9.91e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 35.67 E-value: 9.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616431502 472 KLSGGQRQ-------------RIDIARSFVKNPDILLLDEATANLDSESelkIQEALETL 518
Cdd:pfam13558 32 GLSGGEKQllaylplaaalaaQYGSAEGRPPAPRLVFLDEAFAKLDEEN---IRTALELL 88
|
|
| |
