|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
117-697 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 607.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 117 WKLFWQFLRPHLLALGVAIVLALGAALVNVQIPLLLGQLVEIVAkytrdhVGSFMTESRKLSTHLLILYGVQGLLTFGYL 196
Cdd:COG1132 9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL------AGGDLSALLLLLLLLLGLALLRALLSYLQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 197 VLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTR 276
Cdd:COG1132 83 YLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 277 LTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGR 356
Cdd:COG1132 163 LALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 357 GIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFEYMALSP 436
Cdd:COG1132 243 LSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 437 CIPLSGGCcIPKEHLRGSVTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML 516
Cdd:COG1132 323 EIPDPPGA-VPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 517 DGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLS 596
Cdd:COG1132 400 DGVDIRDLTLESLRRQI-GVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 597 GGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTH 676
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTH 558
|
570 580
....*....|....*....|.
gi 109068902 677 EELLKKGGLYAELIRRQALDA 697
Cdd:COG1132 559 EELLARGGLYARLYRLQFGEE 579
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
134-428 |
5.32e-167 |
|
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: 481.27 E-value: 5.32e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 134 AIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHVGSFMTESRKLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDMRRA 213
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNVISRSLKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 214 LFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGT 293
Cdd:cd18574 81 LFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 294 LMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMV 373
Cdd:cd18574 161 LYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGLSNLALNGIV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 374 LGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18574 241 LGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
117-690 |
2.67e-160 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 479.60 E-value: 2.67e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 117 WKLFwQFLRPHLLALGVAIVLALGAALVNVQIPLLLGQLVEIVakytrdhVGSFMTESRKLSTHLLILYGVQGLLTFG-- 194
Cdd:TIGR00958 150 FRLL-GLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTL-------GGDKGPPALASAIFFMCLLSIASSVSAGlr 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 195 ---YLVLLSHIGERMavdmRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLS 271
Cdd:TIGR00958 222 ggsFNYTMARINLRI----REDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFML 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 272 MLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACR--C 349
Cdd:TIGR00958 298 WLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLqlN 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 350 RAEELGRgiALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARVF 429
Cdd:TIGR00958 378 KRKALAY--AGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVF 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 430 EYMALSPCIPLSGGccIPKEHLRGSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDP 509
Cdd:TIGR00958 456 EYLDRKPNIPLTGT--LAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQP 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 510 TAGVVMLDGRDLRTLDPSWLRGQVVgFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVG 589
Cdd:TIGR00958 534 TGGQVLLDGVPLVQYDHHYLHRQVA-LVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVG 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 590 ERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEalDRASAGRTVLVIAHRLSTVRGAHRIIVMADGR 669
Cdd:TIGR00958 613 EKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGS 690
|
570 580
....*....|....*....|.
gi 109068902 670 VWEAGTHEELLKKGGLYAELI 690
Cdd:TIGR00958 691 VVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
121-693 |
5.24e-160 |
|
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: 474.19 E-value: 5.24e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 121 WQFLRPHLLALGVAIVLALGAALVNVQIPLLLGQLVeivakytrDHvGSFMTESRKLSTHLLILYGVQGLL---TFGYLV 197
Cdd:TIGR02204 10 WPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMI--------DH-GFSKDSSGLLNRYFAFLLVVALVLalgTAARFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 198 LLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRL 277
Cdd:TIGR02204 81 LVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 278 TLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEAC------RCRA 351
Cdd:TIGR02204 161 TSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAyeaarqRIRT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 352 EELGRGIALFQGLSNIAfncmvlGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFEY 431
Cdd:TIGR02204 241 RALLTAIVIVLVFGAIV------GVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIEL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 432 MALSPCIPLSGGCCIPKEHLRGSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTA 511
Cdd:TIGR02204 315 LQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 512 GVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGER 591
Cdd:TIGR02204 395 GRILLDGVDLRQLDPAELR-ARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGER 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 592 GTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVW 671
Cdd:TIGR02204 474 GVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIV 553
|
570 580
....*....|....*....|..
gi 109068902 672 EAGTHEELLKKGGLYAELIRRQ 693
Cdd:TIGR02204 554 AQGTHAELIAKGGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
103-694 |
5.78e-155 |
|
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: 465.85 E-value: 5.78e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 103 PASSTPRVVGSRFNWKLFWQFLRPHLLALGVAIVLALGAALVNVQIPLLLGQLVEIVAkytrdhVGSFMTESRKLSTHLL 182
Cdd:COG2274 130 PTPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVL------PNQDLSTLWVLAIGLL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 183 ILYGVQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRlttdVQEFKSSFKLVISQGLRSCTQ 262
Cdd:COG2274 204 LALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASR----FRDVESIREFLTGSLLTALLD 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 263 VAGCLVSLSML---STRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEER 339
Cdd:COG2274 280 LLFVLIFLIVLffySPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 340 YgAELEACRCRAEELGRGIALFQGLSNIAFNCMV-LGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQV 418
Cdd:COG2274 360 W-ENLLAKYLNARFKLRRLSNLLSTLSGLLQQLAtVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRF 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 419 VRGLSAGARVFEYMALsPCIPLSGGCCIPKEHLRGSVTFQNVCFSYPcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT 498
Cdd:COG2274 439 QDAKIALERLDDILDL-PPEREEGRSKLSLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKST 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 499 VASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFIT 578
Cdd:COG2274 517 LLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQI-GVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIE 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 579 SFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRG 658
Cdd:COG2274 596 ALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRL 675
|
570 580 590
....*....|....*....|....*....|....*.
gi 109068902 659 AHRIIVMADGRVWEAGTHEELLKKGGLYAELIRRQA 694
Cdd:COG2274 676 ADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
455-693 |
4.98e-141 |
|
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: 412.70 E-value: 4.98e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVv 534
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPT 614
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 615 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
117-693 |
2.14e-132 |
|
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: 402.94 E-value: 2.14e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 117 WKLFWQFLRPHLLALGVAIVLALGAALVNVQIPLLLgqlveivaKYTRDHVGSFMTESRKLSTHLLI--LYGVQGLLTFG 194
Cdd:TIGR02203 2 FRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALL--------KPLLDDGFGGRDRSVLWWVPLVVigLAVLRGICSFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 195 YLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSS----FKLVISQGLrsctQVAGCLVSL 270
Cdd:TIGR02203 74 STYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAatdaFIVLVRETL----TVIGLFIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 271 SMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCR 350
Cdd:TIGR02203 150 LYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 351 AEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFE 430
Cdd:TIGR02203 230 AMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 431 YMAlSPCIPLSGGccIPKEHLRGSVTFQNVCFSYPCRpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPT 510
Cdd:TIGR02203 310 LLD-SPPEKDTGT--RAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 511 AGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLA-ASDEEVYAAAREANAHEFITSFPEGYNTIVG 589
Cdd:TIGR02203 386 SGQILLDGHDLADYTLASLRRQV-ALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 590 ERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGR 669
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
570 580
....*....|....*....|....
gi 109068902 670 VWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:TIGR02203 545 IVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
455-689 |
7.83e-121 |
|
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: 360.78 E-value: 7.83e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPGFeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVv 534
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPT 614
Cdd:cd03251 79 GLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 615 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAEL 689
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
101-694 |
2.31e-120 |
|
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: 373.00 E-value: 2.31e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 101 APPASSTPRVVGSRFNWKLFWQFLRPHLLALGVAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHVGSFMtesrkLSTH 180
Cdd:COG5265 5 RAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLV-----VPVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 181 LLILYGVQGLLT--FGYL--VLLSHIGERMavdMRR-AL--FSSLLRQDIAFFDANKTGQLvSRlttdvqefkssfklVI 253
Cdd:COG5265 80 LLLAYGLLRLLSvlFGELrdALFARVTQRA---VRRlALevFRHLHALSLRFHLERQTGGL-SR--------------DI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 254 SQGLRSctqvAGCLVSLSMLSTRLTLL--LMVA-----------------TPALMGVGTLMGSGLR-KLSRQCQEQIARA 313
Cdd:COG5265 142 ERGTKG----IEFLLRFLLFNILPTLLeiALVAgillvkydwwfalitlvTVVLYIAFTVVVTEWRtKFRREMNEADSEA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 314 MGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGD 393
Cdd:COG5265 218 NTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 394 LMsfLVASQTVQRSMA--NLSVLFGQVVRGLSAGARVFEYMALSPCI-------PLSGGccipkehlRGSVTFQNVCFSY 464
Cdd:COG5265 298 FV--LVNAYLIQLYIPlnFLGFVYREIRQALADMERMFDLLDQPPEVadapdapPLVVG--------GGEVRFENVSFGY 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 465 pcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLF 544
Cdd:COG5265 368 --DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLR-AAIGIVPQDTVLF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 545 GTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 624
Cdd:COG5265 445 NDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 625 LDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAELIRRQA 694
Cdd:COG5265 525 LDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
455-693 |
1.65e-116 |
|
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: 349.61 E-value: 1.65e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 534
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLR-RAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPT 614
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 615 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
118-684 |
3.29e-108 |
|
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: 340.20 E-value: 3.29e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 118 KLFWQFLRPHLLALGVAIVLALGAALVNVQIPLLLGQLVE--IVAKYTRDHVGSFMTesrklstHLLILYGVQGLLTFGY 195
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAglIIGGAPLSALLPLLG-------LLLAVLLLRALLAWLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 196 LVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLST 275
Cdd:COG4988 79 ERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 276 RLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARamgVADEALGNVR---TVRAFAMEQREEERYGAELEACRCRAE 352
Cdd:COG4988 159 LSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALAR---LSGHFLDRLRgltTLKLFGRAKAEAERIAEASEDFRKRTM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 353 ELGRgIALfqgLSN-----IAFNCMVLGTLFIGGSLVAGQqLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGAR 427
Cdd:COG4988 236 KVLR-VAF---LSSavlefFASLSIALVAVYIGFRLLGGS-LTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 428 VFEYMALSPCIPLSGGCCIPKEHlRGSVTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFY 507
Cdd:COG4988 311 IFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 508 DPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTI 587
Cdd:COG4988 388 PPYSGSILINGVDLSDLDPASWRRQI-AWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 588 VGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMAD 667
Cdd:COG4988 467 LGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDD 546
|
570
....*....|....*..
gi 109068902 668 GRVWEAGTHEELLKKGG 684
Cdd:COG4988 547 GRIVEQGTHEELLAKNG 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
116-693 |
1.18e-103 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 328.90 E-value: 1.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 116 NWKLF---WQFLRPHLLALGVAIV-LALGAALVNVQIPLLLGQLVEIVAKYTRDhvgsFMtesRKLSTHLLILYGVQGLL 191
Cdd:PRK11176 9 TWQTFrrlWPTIAPFKAGLIVAGVaLILNAASDTFMLSLLKPLLDDGFGKADRS----VL---KWMPLVVIGLMILRGIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 192 TFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLS 271
Cdd:PRK11176 82 SFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 272 MLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRA 351
Cdd:PRK11176 162 YYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 352 EEL--GRGIA--LFQGLSNIAFNCMvlgtLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGAR 427
Cdd:PRK11176 242 MKMvsASSISdpIIQLIASLALAFV----LYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 428 VFEYMALSPCIPlSGGCCIpkEHLRGSVTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFY 507
Cdd:PRK11176 318 LFAILDLEQEKD-EGKRVI--ERAKGDIEFRNVTFTYPGKEV-PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 508 DPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLAA-SDEEVYAAAREANAHEFITSFPEGYNT 586
Cdd:PRK11176 394 DIDEGEILLDGHDLRDYTLASLRNQV-ALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDT 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 587 IVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMA 666
Cdd:PRK11176 473 VIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVE 552
|
570 580
....*....|....*....|....*..
gi 109068902 667 DGRVWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:PRK11176 553 DGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
205-692 |
9.31e-103 |
|
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: 325.95 E-value: 9.31e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 205 RMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVA 284
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 285 tpaLMGVGTLMGSGLRKLSRQCQEQIARAMG----VADEALGNVRTVRAFAMEQREEERYgAELEACRCRAEE-LGRGIA 359
Cdd:COG4987 165 ---LLLAGLLLPLLAARLGRRAGRRLAAARAalraRLTDLLQGAAELAAYGALDRALARL-DAAEARLAAAQRrLARLSA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 360 LFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFEYMALSPCIP 439
Cdd:COG4987 241 LAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 440 LSGGCCIPKEHlrGSVTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGR 519
Cdd:COG4987 321 EPAEPAPAPGG--PSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGV 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 520 DLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQ 599
Cdd:COG4987 398 DLRDLDEDDLR-RRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 600 KQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEEL 679
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
490
....*....|...
gi 109068902 680 LKKGGLYAELIRR 692
Cdd:COG4987 557 LAQNGRYRQLYQR 569
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
453-684 |
1.18e-102 |
|
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: 313.78 E-value: 1.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 453 GSVTFQNVCFSYpcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQ 532
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 533 VvGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQ 612
Cdd:cd03254 79 I-GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 613 PTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGG 684
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
455-693 |
5.22e-96 |
|
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: 296.71 E-value: 5.22e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYpcRP-GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQV 533
Cdd:cd03252 1 ITFEHVRFRY--KPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 vGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQP 613
Cdd:cd03252 79 -GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 614 TVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
267-705 |
9.61e-96 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 308.04 E-value: 9.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 267 LVSLSM-LSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAmeqreeeRYGAELE 345
Cdd:PRK13657 147 LLPLALfMNWRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYN-------RIEAETQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 346 ACRCRAEELGRG-------IALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL-VASQTVQRsmanLSVLFGQ 417
Cdd:PRK13657 220 ALRDIADNLLAAqmpvlswWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVgFATLLIGR----LDQVVAF 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 418 VVRGLSAGARVFEYMALSPCIPLSG--GCCIPKEHLRGSVTFQNVCFSYP-CRPGfevLKDFTLTLPPGKIVALVGQSGG 494
Cdd:PRK13657 296 INQVFMAAPKLEEFFEVEDAVPDVRdpPGAIDLGRVKGAVEFDDVSFSYDnSRQG---VEDVSFEAKPGQTVAIVGPTGA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 495 GKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAH 574
Cdd:PRK13657 373 GKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR-RNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAH 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 575 EFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLS 654
Cdd:PRK13657 452 DFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLS 531
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 109068902 655 TVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAELIRRQALDAPRTVAPPP 705
Cdd:PRK13657 532 TVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGMLQEDERRKQP 582
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
450-670 |
1.33e-90 |
|
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: 282.44 E-value: 1.33e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 450 HLRGSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWL 529
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 530 RGQVVgFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARAL 609
Cdd:cd03248 87 HSKVS-LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109068902 610 IKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRV 670
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
120-691 |
3.16e-85 |
|
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: 283.76 E-value: 3.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 120 FWQFLRPHLLALGVAIVLALGAALVNVQIPLLLGQLVEIVAKYTRdhVGSFMTESRKLSTHLLILYGVQGLLTFGYLVLL 199
Cdd:TIGR03796 141 LLRALWRRLRGSRGALLYLLLAGLLLVLPGLVIPAFSQIFVDEIL--VQGRQDWLRPLLLGMGLTALLQGVLTWLQLYYL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 200 SHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTD--VQEFKSSfklvisqglrsctQVAGCLVSLSMLSTRL 277
Cdd:TIGR03796 219 RRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLNdqVAEFLSG-------------QLATTALDAVMLVFYA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 278 tLLLMVATPALMGVGTLMG----------SGLRK-LSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERY-GAELE 345
Cdd:TIGR03796 286 -LLMLLYDPVLTLIGIAFAainvlalqlvSRRRVdANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSRWaGYQAK 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 346 ACRCRaEELGRGIALFQGLSNI--AFNCMVLgtLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLsVLFGQVVRGLS 423
Cdd:TIGR03796 365 LLNAQ-QELGVLTQILGVLPTLltSLNSALI--LVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNL-VGFGGTLQELE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 424 AGARVFEYMALSPCIPL------SGGCCIPKEHLRGSVTFQNVCFSYPcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKT 497
Cdd:TIGR03796 441 GDLNRLDDVLRNPVDPLleepegSAATSEPPRRLSGYVELRNITFGYS-PLEPPLIENFSLTLQPGQRVALVGGSGSGKS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 498 TVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFI 577
Cdd:TIGR03796 520 TIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSV-AMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVI 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 578 TSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAsaGRTVLVIAHRLSTVR 657
Cdd:TIGR03796 599 TSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRR--GCTCIIVAHRLSTIR 676
|
570 580 590
....*....|....*....|....*....|....
gi 109068902 658 GAHRIIVMADGRVWEAGTHEELLKKGGLYAELIR 691
Cdd:TIGR03796 677 DCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
134-428 |
1.07e-84 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 269.04 E-value: 1.07e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 134 AIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHVGSfmtesrKLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDMRRA 213
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLN------ELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 214 LFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGT 293
Cdd:cd18557 75 LFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 294 LMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMV 373
Cdd:cd18557 155 IYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 374 LGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18557 235 LLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
455-669 |
2.89e-80 |
|
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: 253.07 E-value: 2.89e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVv 534
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVLFGTTIMENIrfgklaasdeevyaaareanahefitsfpegyntivgergttLSGGQKQRLAIARALIKQPT 614
Cdd:cd03228 79 AYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 615 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGR 669
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
116-693 |
3.35e-73 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 248.48 E-value: 3.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 116 NWKLFWQFLR-------PHLLALGVAIVLALGAALVNVQIPLLLgqlveivaKYTRDHVgsfmtesrkLSTHLLILYGVQ 188
Cdd:PRK10790 3 SFSQLWPTLKrllaygsPWRKPLGLAVLMLWVAAAAEVSGPLLI--------SYFIDNM---------VAKGNLPLGLVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 189 GLLTfGYLVL-----LSHIGE-----RMAVD----MRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVIS 254
Cdd:PRK10790 66 GLAA-AYVGLqllaaGLHYAQsllfnRAAVGvvqqLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 255 QGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFameq 334
Cdd:PRK10790 145 TVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQF---- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 335 REEERYGAELEACRcRAEELGR-------GIALFQGLSniAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL--------- 398
Cdd:PRK10790 221 RQQARFGERMGEAS-RSHYMARmqtlrldGFLLRPLLS--LFSALILCGLLMLFGFSASGTIEVGVLYAFIsylgrlnep 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 399 VASQTVQRSMANLSVLfgqvvrglsAGARVFEYMAlSP-------CIPLSGGccipkehlrgSVTFQNVCFSYpcRPGFE 471
Cdd:PRK10790 298 LIELTTQQSMLQQAVV---------AGERVFELMD-GPrqqygndDRPLQSG----------RIDIDNVSFAY--RDDNL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMEN 551
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR-QGVAMVQQDPVVLADTFLAN 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 552 IRFGKlAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESER 631
Cdd:PRK10790 435 VTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 632 VVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:PRK10790 514 AIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
190-707 |
4.89e-73 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 247.32 E-value: 4.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 190 LLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQefkssfKLVISQGLRSCT----QVAG 265
Cdd:PRK10789 51 LLRYVWRVLLFGASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVD------RVVFAAGEGVLTlvdsLVMG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 266 CLVSLSM---LSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGA 342
Cdd:PRK10789 125 CAVLIVMstqISWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 343 ELEACRCRAEELGRGIALFQ-------GLSNIafncmvlgtLFIGGS--LVAGQQLTGGDLMSFLVASQTVQRSMANLSV 413
Cdd:PRK10789 205 DAEDTGKKNMRVARIDARFDptiyiaiGMANL---------LAIGGGswMVVNGSLTLGQLTSFVMYLGLMIWPMLALAW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 414 LFGQVVRGLSAGARVFEYMALSPCIpLSGGCCIPKEhlRGSVTFQNVCFSYP--CRPgfeVLKDFTLTLPPGKIVALVGQ 491
Cdd:PRK10789 276 MFNIVERGSAAYSRIRAMLAEAPVV-KDGSEPVPEG--RGELDVNIRQFTYPqtDHP---ALENVNFTLKPGQMLGICGP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 492 SGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREA 571
Cdd:PRK10789 350 TGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRL-AVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 572 NAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAH 651
Cdd:PRK10789 429 SVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 652 RLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAELIRRQALDAPRTVAPPPKK 707
Cdd:PRK10789 509 RLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAALDDAPEIRE 564
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
205-693 |
4.07e-72 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 247.95 E-value: 4.07e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 205 RMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRlttdVQEFKSSFKLVISQGLRSCTQVAGCLVSLSML---STRLTLLL 281
Cdd:TIGR03797 206 RMDASLQAAVWDRLLRLPVSFFRQYSTGDLASR----AMGISQIRRILSGSTLTTLLSGIFALLNLGLMfyySWKLALVA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 282 MVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYgAELEACRCRAEELGRGIALF 361
Cdd:TIGR03797 282 VALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARW-AKLFSRQRKLELSAQRIENL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 362 QGLSNIAFNCMVLGTLF-IGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFEYMALSPCIPL 440
Cdd:TIGR03797 361 LTVFNAVLPVLTSAALFaAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPEVDE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 441 SGgccIPKEHLRGSVTFQNVCFSYPCRpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRD 520
Cdd:TIGR03797 441 AK---TDPGKLSGAIEVDRVTFRYRPD-GPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 521 LRTLDPSWLRGQVvGFISQEPVLFGTTIMENIrFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQK 600
Cdd:TIGR03797 517 LAGLDVQAVRRQL-GVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 601 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRtvLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELL 680
Cdd:TIGR03797 595 QRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELM 672
|
490
....*....|...
gi 109068902 681 KKGGLYAELIRRQ 693
Cdd:TIGR03797 673 AREGLFAQLARRQ 685
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
287-682 |
1.86e-70 |
|
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: 240.04 E-value: 1.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 287 ALMGVGTLMGSGL------RKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIAL 360
Cdd:COG4618 161 ALVGALVLVALALlnerltRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAGG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 361 FQGLS---NIAFNCMVLGTlfiGGSLVAGQQLTGGDLM--SFLVAsqtvqRSMANLSVLFG---QVVRGLSAGARVFEYM 432
Cdd:COG4618 241 FSALSkflRLLLQSAVLGL---GAYLVIQGEITPGAMIaaSILMG-----RALAPIEQAIGgwkQFVSARQAYRRLNELL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 433 ALSPCIPlsggcciPKEHL---RGSVTFQNVCFSYPC--RPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFY 507
Cdd:COG4618 313 AAVPAEP-------ERMPLprpKGRLSVENLTVVPPGskRP---ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVW 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 508 DPTAGVVMLDGRDLRTLDPSWLrGQVVGFISQEPVLFGTTIMENI-RFGKlaASDEEVYAAAREANAHEFITSFPEGYNT 586
Cdd:COG4618 383 PPTAGSVRLDGADLSQWDREEL-GRHIGYLPQDVELFDGTIAENIaRFGD--ADPEKVVAAAKLAGVHEMILRLPDGYDT 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 587 IVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRGAHRIIVM 665
Cdd:COG4618 460 RIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVL 539
|
410
....*....|....*..
gi 109068902 666 ADGRVWEAGTHEELLKK 682
Cdd:COG4618 540 RDGRVQAFGPRDEVLAR 556
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
453-670 |
1.71e-69 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 226.70 E-value: 1.71e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 453 GSVTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQ 532
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 533 VVGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQ 612
Cdd:cd03245 79 NIGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 613 PTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRV 670
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
134-428 |
2.39e-69 |
|
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: 228.94 E-value: 2.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 134 AIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHvGSFMTESRKLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDMRRA 213
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDI-EIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 214 LFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGT 293
Cdd:cd18573 80 LFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 294 LMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMV 373
Cdd:cd18573 160 FYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 374 LGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18573 240 LSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
136-665 |
6.05e-66 |
|
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: 227.17 E-value: 6.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 136 VLALGAALVNVQIPLLLGQ---LVEIVAKYTRDhvGSFMTESRKLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDMRR 212
Cdd:TIGR02857 4 ALALLALLGVLGALLIIAQawlLARVVDGLISA--GEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 213 ALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVG 292
Cdd:TIGR02857 82 RLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 293 TLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRgIALfqgLSNIAFNcm 372
Cdd:TIGR02857 162 ILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLR-IAF---LSSAVLE-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 373 VLGTL-------FIGGSLVAGQQLTGGDLMSFLVASQTVQrSMANLSVLFGQVVRGLSAGARVFEYMALSPcIPLSGGCC 445
Cdd:TIGR02857 236 LFATLsvalvavYIGFRLLAGDLDLATGLFVLLLAPEFYL-PLRQLGAQYHARADGVAAAEALFAVLDAAP-RPLAGKAP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 446 IPKEHLRgSVTFQNVCFSYPCRPgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLD 525
Cdd:TIGR02857 314 VTAAPAS-SLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 526 PSWLRGQVvGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAI 605
Cdd:TIGR02857 391 ADSWRDQI-AWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLAL 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 606 ARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVM 665
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
453-675 |
1.55e-65 |
|
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: 216.21 E-value: 1.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 453 GSVTFQNVCFSYpcRPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG 531
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 532 QVvGFISQEPVLFGTTIMENIR-FGKlaASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALI 610
Cdd:cd03244 79 RI-SIIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 611 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGT 675
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
177-682 |
5.43e-65 |
|
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: 224.92 E-value: 5.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 177 LSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDAnKTGQLVSRLTTdVQEFKSSfklvisQG 256
Cdd:TIGR01842 48 LTVLALGLYLFLGLLDALRSFVLVRIGEKLDGALNQPIFAASFSATLRRGSG-DGLQALRDLDQ-LRQFLTG------PG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 257 LrsctqVAGC--------LVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVR 328
Cdd:TIGR01842 120 L-----FAFFdapwmpiyLLVCFLLHPWIGILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADSALRNAEVIE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 329 AFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGdlmSFLVASQTVQRSM 408
Cdd:TIGR01842 195 AMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPG---MMIAGSILVGRAL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 409 ANLSVLFG---QVVRGLSAGARVFEYMALSPciplsggccIPKEHL-----RGSVTFQNVCFSYPcRPGFEVLKDFTLTL 480
Cdd:TIGR01842 272 APIDGAIGgwkQFSGARQAYKRLNELLANYP---------SRDPAMplpepEGHLSVENVTIVPP-GGKKPTLRGISFSL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 481 PPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLrGQVVGFISQEPVLFGTTIMENI-RFGKlAA 559
Cdd:TIGR01842 342 QAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETF-GKHIGYLPQDVELFPGTVAENIaRFGE-NA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 560 SDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR 639
Cdd:TIGR01842 420 DPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKA 499
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 109068902 640 ASA-GRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKK 682
Cdd:TIGR01842 500 LKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
177-690 |
7.83e-65 |
|
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: 228.47 E-value: 7.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 177 LSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTtDVQEFKSSFKLVISQG 256
Cdd:TIGR01193 198 ISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 257 LRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAME--- 333
Cdd:TIGR01193 277 FLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEaer 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 334 -QREEERYGAELE-ACRCRAEELGRGiaLFQGLSNIAFNCMVLgtlFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANL 411
Cdd:TIGR01193 357 ySKIDSEFGDYLNkSFKYQKADQGQQ--AIKAVTKLILNVVIL---WTGAYLVMRGKLTLGQLITFNALLSYFLTPLENI 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 412 SVLFGQVVRGLSAGARVFE-YMALSPCIplSGGCCIPKEHLRGSVTFQNVCFSYpcrpGF--EVLKDFTLTLPPGKIVAL 488
Cdd:TIGR01193 432 INLQPKLQAARVANNRLNEvYLVDSEFI--NKKKRTELNNLNGDIVINDVSYSY----GYgsNILSDISLTIKMNSKTTI 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 489 VGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFG-KLAASDEEVYAA 567
Cdd:TIGR01193 506 VGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR-QFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 568 AREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAgRTVL 647
Cdd:TIGR01193 585 CEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTII 663
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 109068902 648 VIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAELI 690
Cdd:TIGR01193 664 FVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
198-653 |
6.97e-61 |
|
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: 213.38 E-value: 6.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 198 LLSH-IGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFklvisqgLRSCTQVAGCLVsLSMLSTR 276
Cdd:TIGR02868 75 LVGHdAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLY-------VRVIVPAGVALV-VGAAAVA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 277 LTLLLMVATPALMGVGTLMGSGL-----RKLSRQCQEQIARAMG----VADEALGNVRTVRAF-AME--QREEERYGAEL 344
Cdd:TIGR02868 147 AIAVLSVPAALILAAGLLLAGFVaplvsLRAARAAEQALARLRGelaaQLTDALDGAAELVASgALPaaLAQVEEADREL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 345 EACRCRAeelGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSA 424
Cdd:TIGR02868 227 TRAERRA---AAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 425 GARVFEYMALSPCIPLSGGCCIPKEHLRG-SVTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL 503
Cdd:TIGR02868 304 AERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 504 ERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEG 583
Cdd:TIGR02868 382 AGLLDPLQGEVTLDGVPVSSLDQDEVR-RRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDG 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 584 YNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRL 653
Cdd:TIGR02868 461 LDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
134-428 |
9.20e-60 |
|
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: 203.16 E-value: 9.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 134 AIVLALGAALVNVQIPLLLGQLVEIVAkytrdHVGSFMTESRKLsTHLLILYGVQGLLTFGYLVLLSHIGERMAVDMRRA 213
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVV-----ADGSREAFYRAV-LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 214 LFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGT 293
Cdd:cd18572 75 LFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 294 LMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMV 373
Cdd:cd18572 155 VYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQ 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 374 LGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18572 235 VLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
134-428 |
8.93e-59 |
|
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: 200.40 E-value: 8.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 134 AIVLALGAALVNVQIPLLLGQLVEIVakytrdHVGSFMTESRKLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDMRRA 213
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAA------LGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 214 LFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGT 293
Cdd:cd18576 75 LYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 294 LMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMV 373
Cdd:cd18576 155 LFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 374 LGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18576 235 VAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
477-693 |
1.18e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 205.85 E-value: 1.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 477 TLTLPPGKIVALVGQSGGGKTTVASLLERFYdPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGK 556
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHL-SWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 557 LAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEA 636
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 637 LDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
131-428 |
1.40e-56 |
|
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: 195.00 E-value: 1.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 131 LGVAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHVGS--FMTESRKLSTHLLILYGVQGLLTFGYLVLLSHIGERMAV 208
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPdeFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 209 DMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQ-VAGCLVSLSMlSTRLTLLLMVATPA 287
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTfIAGFIIAFIY-SWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 288 LMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEacrcRAEELGRGIALFQGLSNI 367
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALE----KARKAGIKKGLVSGLGLG 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 368 AFNCMVLGT----LFIGGSLVAGQQLTGGD----LMSFLVASQTVQRSMANLSVLfgqvVRGLSAGARV 428
Cdd:cd18577 236 LLFFIIFAMyalaFWYGSRLVRDGEISPGDvltvFFAVLIGAFSLGQIAPNLQAF----AKARAAAAKI 300
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
337-693 |
1.29e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 200.05 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 337 EERYGAELEACRCRAEELGRGIALFQGLSN---IAFNCM-VLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLS 412
Cdd:PRK11160 219 EDRYRQQLEQTEQQWLAAQRRQANLTGLSQalmILANGLtVVLMLWLAAGGVGGNAQPGALIALFVFAALAAFEALMPVA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 413 VLF---GQVVrglSAGARVFEYMALSPCIPLSGGCCIPKEhlRGSVTFQNVCFSYPCRPgFEVLKDFTLTLPPGKIVALV 489
Cdd:PRK11160 299 GAFqhlGQVI---ASARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQP-QPVLKGLSLQIKAGEKVALL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 490 GQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAR 569
Cdd:PRK11160 373 GRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR-QAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQ 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 570 EANAHEFITSfPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVI 649
Cdd:PRK11160 452 QVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMI 530
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 109068902 650 AHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:PRK11160 531 THRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
133-428 |
8.58e-55 |
|
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: 189.77 E-value: 8.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 133 VAIVLALGAALVnvqIPLLLGQLVEIVAKytrdHVGSFMTESRKLSTH----LLILYGVQGLLTFGYLVLLSHIGERMAV 208
Cdd:cd18780 3 IALLVSSGTNLA---LPYFFGQVIDAVTN----HSGSGGEEALRALNQavliLLGVVLIGSIATFLRSWLFTLAGERVVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 209 DMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPAL 288
Cdd:cd18780 76 RLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 289 MGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIA 368
Cdd:cd18780 156 SIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAA 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 369 FNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18780 236 AQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
182-667 |
3.48e-50 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 190.24 E-value: 3.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 182 LILYG-VQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTgqlvSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:PTZ00265 103 LVLIGiFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQVNAGIGTKFITI 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 261 TQVAGCLVSLSMLS----TRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQR- 335
Cdd:PTZ00265 179 FTYASAFLGLYIWSlfknARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTi 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 336 ------EEERYGA-ELEACRCRAEELGrgiaLFQG--LSNIAFNcMVLGTLFIGGSLVAGQ---QLTGGDLMSFLVAsqt 403
Cdd:PTZ00265 259 lkkfnlSEKLYSKyILKANFMESLHIG----MINGfiLASYAFG-FWYGTRIIISDLSNQQpnnDFHGGSVISILLG--- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 404 VQRSMANLSVLFGQV---VRGLSAGARVFEYMALSPCIPLSG-GCCIPKEHlrgSVTFQNVCFSYPCRPGFEVLKDFTLT 479
Cdd:PTZ00265 331 VLISMFMLTIILPNIteyMKSLEATNSLYEIINRKPLVENNDdGKKLKDIK---KIQFKNVRFHYDTRKDVEIYKDLNFT 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 480 LPPGKIVALVGQSGGGKTTVASLLERFYDPTAG-VVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRF---- 554
Cdd:PTZ00265 408 LTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdIIINDSHNLKDINLKWWRSKI-GVVSQDPLLFSNSIKNNIKYslys 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 555 -----------------------------GKLAAS------------------------DEEVYAAAREANAHEFITSFP 581
Cdd:PTZ00265 487 lkdlealsnyynedgndsqenknkrnscrAKCAGDlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIHDFVSALP 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 582 EGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGA 659
Cdd:PTZ00265 567 DKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYA 646
|
....*...
gi 109068902 660 HRIIVMAD 667
Cdd:PTZ00265 647 NTIFVLSN 654
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
131-408 |
1.20e-49 |
|
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: 175.14 E-value: 1.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 131 LGVAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHVgsfmTESRKLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDM 210
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPET----QALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 211 RRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRS-CTQVAGCLVSLSmLSTRLTLLLMVATPALM 289
Cdd:pfam00664 77 RRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSlATIVGGIIVMFY-YGWKLTLVLLAVLPLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 290 GVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAF 369
Cdd:pfam00664 156 LVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIG 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 109068902 370 NCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSM 408
Cdd:pfam00664 236 YLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
131-428 |
1.47e-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: 175.30 E-value: 1.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 131 LGVAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHVGSFMTesrkLSthLLILYGVQGLLTFGYLVLLSHIGERMAVDM 210
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVP----LA--IIGLFLLRGLASYLQTYLMAYVGQRVVRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 211 RRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMG 290
Cdd:cd18552 75 RNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 291 VGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFN 370
Cdd:cd18552 155 PIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 371 CMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18552 235 IAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
455-682 |
4.14e-49 |
|
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: 172.13 E-value: 4.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 534
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELR-RKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPV--LFGTTIMENIRFG--KLAASDEEVYAAAREA----NAHEFITSFPegyntivgergTTLSGGQKQRLAIA 606
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEDVAFGpeNLGLPREEIRERVEEAlelvGLEHLADRPP-----------HELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 607 RALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELLKK 682
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
131-428 |
4.16e-49 |
|
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: 174.28 E-value: 4.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 131 LGVAIVLALGAALVNVQIPLLLGQLV-EIVAKYTRDHVGSFMTEsrklsthLLILYGVQGLLTFGYLVLLSHIGERMAVD 209
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIdDVIPAGDLSLLLWIALL-------LLLLALLRALLSYLRRYLAARLGQRVVFD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 210 MRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALM 289
Cdd:cd07346 74 LRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 290 GVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAF 369
Cdd:cd07346 154 LILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLT 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 370 NCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd07346 234 ALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
202-691 |
5.54e-49 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 186.39 E-value: 5.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 202 IGERMAVDMRRALFSSLLRQDIAFFD--ANKTGQLVSRLTTDVQEFKSS--------------FKLVISQGLRSCTQVAG 265
Cdd:PTZ00265 893 IGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGlvnnivifthfivlFLVSMVMSFYFCPIVAA 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 266 CLVSLSMLSTRLTLLL--MVATPALMGVGTLMGSGLRKLSRQcQEQIARAMGVADEALGNVRTVRAFAMEQreeerYGAE 343
Cdd:PTZ00265 973 VLTGTYFIFMRVFAIRarLTANKDVEKKEINQPGTVFAYNSD-DEIFKDPSFLIQEAFYNMNTVIIYGLED-----YFCN 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 344 L--EACRCRAEELGRGI---ALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQV 418
Cdd:PTZ00265 1047 LieKAIDYSNKGQKRKTlvnSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDS 1126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 419 VRGLSAGARVFEYMALSPCIPL--SGGCCIP-KEHLRGSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGG 495
Cdd:PTZ00265 1127 ENAKLSFEKYYPLIIRKSNIDVrdNGGIRIKnKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSG 1206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 496 KTTVASLLERFYD------------------------------------------------------PTAGVVMLDGRDL 521
Cdd:PTZ00265 1207 KSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDI 1286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 522 RTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQ 601
Cdd:PTZ00265 1287 CDYNLKDLR-NLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQ 1365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 602 RLAIARALIKQPTVLILDEATSALDAESERVVQEAL--DRASAGRTVLVIAHRLSTVRGAHRIIVMAD-----GRVWEAG 674
Cdd:PTZ00265 1366 RIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHG 1445
|
570
....*....|....*...
gi 109068902 675 THEELLK-KGGLYAELIR 691
Cdd:PTZ00265 1446 THEELLSvQDGVYKKYVK 1463
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
119-695 |
2.16e-48 |
|
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: 184.76 E-value: 2.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 119 LFWQFLRphllALGVAIVLALgaalvnvqIPLLLGQLVEIVAK------YTRDHVGSFMTESRKLSTHLLILYGV-QGLL 191
Cdd:TIGR00957 954 VYWDYMK----AIGLFITFLS--------IFLFVCNHVSALASnywlslWTDDPMVNGTQNNTSLRLSVYGALGIlQGFA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 192 TFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLs 271
Cdd:TIGR00957 1022 VFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVI- 1100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 272 MLSTRLTLLLMvatPALMGVGTLMGSGLRKLSRQCQ--EQIARAMGVA--DEALGNVRTVRAFAMEQR----EEERYGAE 343
Cdd:TIGR00957 1101 LLATPIAAVII---PPLGLLYFFVQRFYVASSRQLKrlESVSRSPVYShfNETLLGVSVIRAFEEQERfihqSDLKVDEN 1177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 344 LEAC----------RCRAEELGRGIALFQGL-SNIAFNCMVLGtlFIGGSLVAGQQLTGgdLMSFLVasqtvqRSMANLS 412
Cdd:TIGR00957 1178 QKAYypsivanrwlAVRLECVGNCIVLFAALfAVISRHSLSAG--LVGLSVSYSLQVTF--YLNWLV------RMSSEME 1247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 413 VlfgqvvrGLSAGARVFEYMALSPCIPLSGGCCIPKEHL--RGSVTFQNVCFSYpcRPGFE-VLKDFTLTLPPGKIVALV 489
Cdd:TIGR00957 1248 T-------NIVAVERLKEYSETEKEAPWQIQETAPPSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIV 1318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 490 GQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVgFISQEPVLFGTTIMENIR-FGKLaaSDEEVYAAA 568
Cdd:TIGR00957 1319 GRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKIT-IIPQDPVLFSGSLRMNLDpFSQY--SDEEVWWAL 1395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 569 REANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLV 648
Cdd:TIGR00957 1396 ELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLT 1475
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 109068902 649 IAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAELIRRQAL 695
Cdd:TIGR00957 1476 IAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
456-670 |
5.71e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 165.37 E-value: 5.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 456 TFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVg 535
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 536 FISQEPVLFGTTIMENIRFGKLAASDEevyaaAREANAHEFITSFpeGYNTIVGERGTT-LSGGQKQRLAIARALIKQPT 614
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLRERK-----FDRERALELLERL--GLPPDILDKPVErLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 615 VLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH-RLSTVRGAHRIIVMADGRV 670
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
458-670 |
1.77e-46 |
|
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: 162.77 E-value: 1.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYP--CRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvG 535
Cdd:cd03246 4 ENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHV-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 536 FISQEPVLFGTTIMENIrfgklaasdeevyaaareanahefitsfpegyntivgergttLSGGQKQRLAIARALIKQPTV 615
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 616 LILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLSTVRGAHRIIVMADGRV 670
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
131-428 |
8.43e-46 |
|
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: 164.91 E-value: 8.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 131 LGVAIVLALGAALVNVQIPLLLGQLVEIVakytrdhvgSFMTESRKLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDM 210
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDAL---------SAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 211 RRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMG 290
Cdd:cd18551 72 RRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 291 VGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFN 370
Cdd:cd18551 152 IILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQ 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 371 CMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18551 232 LALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
455-680 |
1.89e-45 |
|
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: 170.08 E-value: 1.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPG--FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLR-- 530
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 531 GQVVGFISQEPV--LF-----GTTIMENIRFGKLaASDEEVYAAAREANAH-----EFITSFPegyntivgergTTLSGG 598
Cdd:COG1123 341 RRRVQMVFQDPYssLNprmtvGDIIAEPLRLHGL-LSRAERRERVAELLERvglppDLADRYP-----------HELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 599 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGT 675
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
....*
gi 109068902 676 HEELL 680
Cdd:COG1123 489 TEEVF 493
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
457-669 |
5.28e-45 |
|
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: 159.94 E-value: 5.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 457 FQNVCFSYPcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPsWLRGQVVGF 536
Cdd:cd03225 2 LKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSL-KELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 537 ISQEP--VLFGTTIMENIRFG--KLAASDEEVYAAAREANAHEFITSFPEgyntivgERGTTLSGGQKQRLAIARALIKQ 612
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALELVGLEGLRD-------RSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 613 PTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHRIIVMADGR 669
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
455-694 |
1.04e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 160.23 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgqVV 534
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR--RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVLFGT-TIMENIRF-GKLAASDEEVyaaaREANAHEFITSF--PEGYNTIVGergtTLSGGQKQRLAIARALI 610
Cdd:COG1131 76 GYVPQEPALYPDlTVRENLRFfARLYGLPRKE----ARERIDELLELFglTDAADRKVG----TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 611 KQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEELLKKG--GLY 686
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARLleDVF 227
|
....*...
gi 109068902 687 AELIRRQA 694
Cdd:COG1131 228 LELTGEEA 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
455-670 |
1.05e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 159.82 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLERfydPTAGVVMLDGRDLRTLDP---S 527
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSErelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 528 WLRGQVVGFISQEPVLFGT-TIMENIRFGKLAASdeeVYAAAREANAHEFITSFpeGyntiVGERG----TTLSGGQKQR 602
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVALPLLLAG---VSRKERRERARELLERV--G----LGDRLdhrpSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 603 LAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRGAHRIIVMADGRV 670
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
457-679 |
1.29e-44 |
|
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: 159.65 E-value: 1.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 457 FQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD-----PTAGVVMLDGRDLRTLD--PSWL 529
Cdd:cd03260 3 LRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDvdVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 530 RGQVvGFISQEPVLFGTTIMENIRFG-KLAASDEEVYAAAREANAHEFITSFPEgyntiVGER--GTTLSGGQKQRLAIA 606
Cdd:cd03260 80 RRRV-GMVFQKPNPFPGSIYDNVAYGlRLHGIKLKEELDERVEEALRKAALWDE-----VKDRlhALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 607 RALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEEL 679
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
455-670 |
2.92e-44 |
|
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: 158.42 E-value: 2.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLERfydPTAGVVMLDGRDLRTLDPSWL- 529
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 530 --RGQVVGFISQEPVLFGT-TIMENIRFGKLAASDEevyAAAREANAHEFITSF--PEGYNTIVGErgttLSGGQKQRLA 604
Cdd:cd03255 78 afRRRHIGFVFQSFNLLPDlTALENVELPLLLAGVP---KKERRERAEELLERVglGDRLNHYPSE----LSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 605 IARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRGAHRIIVMADGRV 670
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
133-428 |
3.41e-44 |
|
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: 160.67 E-value: 3.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 133 VAIVLALGAALVNVQIPLLLGQLV-EIVAKYTRDHVGsfmtesrKLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDMR 211
Cdd:cd18542 3 LAILALLLATALNLLIPLLIRRIIdSVIGGGLRELLW-------LLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 212 RALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGV 291
Cdd:cd18542 76 NDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 292 GTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNC 371
Cdd:cd18542 156 SYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 372 MVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18542 236 QIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
133-426 |
1.12e-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: 159.19 E-value: 1.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 133 VAIVLALGAALVnvqIPLLLGQLVeivakytrDHvGSFMTESRKLSTHLLILYGVQGLLTFG-----YLVllSHIGERMA 207
Cdd:cd18575 3 IALLIAAAATLA---LGQGLRLLI--------DQ-GFAAGNTALLNRAFLLLLAVALVLALAsalrfYLV--SWLGERVV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 208 VDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPA 287
Cdd:cd18575 69 ADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 288 LMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEAC------RCRAEELGRGIALF 361
Cdd:cd18575 149 VVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAfaaalrRIRARALLTALVIF 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 362 QGLSNIAFncmvlgTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRglSAGA 426
Cdd:cd18575 229 LVFGAIVF------VLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQR--AAGA 285
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
453-675 |
1.63e-43 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 156.03 E-value: 1.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 453 GSVTFQNVCFSY-PCRPgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG 531
Cdd:cd03369 5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 532 QVvGFISQEPVLFGTTIMENI-RFGKLaaSDEEVYAAAReanahefitsfpegyntiVGERGTTLSGGQKQRLAIARALI 610
Cdd:cd03369 83 SL-TIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 611 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGT 675
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
455-669 |
2.53e-42 |
|
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: 152.24 E-value: 2.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRP--GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL--ErfYDPTAGVVMLDGRdlrtldpswlr 530
Cdd:cd03250 1 ISVEDASFTWDSGEqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 531 gqvVGFISQEPVLFGTTIMENIRFGKlaASDEEVYAAAREANA-HEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARAL 609
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENILFGK--PFDEERYEKVIKACAlEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 610 IKQPTVLILDEATSALDAES-----ERVVQEALdraSAGRTVLVIAHRLSTVRGAHRIIVMADGR 669
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
455-711 |
5.79e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 160.07 E-value: 5.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPgFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTA---GVVMLDGRDLRTLDPsWLRG 531
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSE-ALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 532 QVVGFISQEP--VLFGTTIMENIRFG--KLAASDEEVYAAAREANAHEFITSFPEGYNTivgergtTLSGGQKQRLAIAR 607
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 608 ALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEELLKKgg 684
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA-- 233
|
250 260
....*....|....*....|....*..
gi 109068902 685 lYAELIRRQALDAPRTVAPPPKKPEGP 711
Cdd:COG1123 234 -PQALAAVPRLGAARGRAAPAAAAAEP 259
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
463-674 |
6.40e-42 |
|
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: 152.27 E-value: 6.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 463 SYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWL--RGQVVGFISQ 539
Cdd:cd03257 10 SFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkiRRKEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 540 EPVL-------FGTTIMENIRFGKLAASDEEVYAAAREA-----NAHEFITSFPegyntivgergTTLSGGQKQRLAIAR 607
Cdd:cd03257 90 DPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYP-----------HELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 608 ALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAG 674
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
121-438 |
1.23e-41 |
|
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: 154.15 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 121 WQFLRPHLLALGVAIVLALGAALVNvqiPL---LLGQLVEIVAKYTRDHVgsfMTESRKLSTHLLILYGVQGLLTFGYLV 197
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVF---PVfaiLFSKLISVFSLPDDDEL---RSEANFWALMFLVLAIVAGIAYFLQGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 198 LLSHIGERMAVDMRRALFSSLLRQDIAFFD--ANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVsLSM-LS 274
Cdd:cd18578 75 LFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLI-IAFvYG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 275 TRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEEL 354
Cdd:cd18578 154 WKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 355 GRGIALFQGLSN-IAFNCMVLGtLFIGGSLVAGQQLTGGD----LMSFLVASQTVQRSMAnlsvLFGQVVRGLSAGARVF 429
Cdd:cd18578 234 ALISGLGFGLSQsLTFFAYALA-FWYGGRLVANGEYTFEQffivFMALIFGAQSAGQAFS----FAPDIAKAKAAAARIF 308
|
....*....
gi 109068902 430 EYMALSPCI 438
Cdd:cd18578 309 RLLDRKPEI 317
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
134-428 |
1.86e-41 |
|
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: 152.85 E-value: 1.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 134 AIVLALGAALVNVQIPLLLGQLVE-IVAKYTRDhvgsfmtesrKLSTHLLILygvqGLLTFGYLV-------LLSHIGER 205
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDgIVIEKSQD----------KFSRAIIIM----GLLAIASSVaagirggLFTLAMAR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 206 MAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVAT 285
Cdd:cd18784 67 LNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 286 PALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEacrcRAEELGRGIALFQG-- 363
Cdd:cd18784 147 PLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLK----DTYKLKIKEALAYGgy 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 364 --LSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18784 223 vwSNELTELALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
473-623 |
1.97e-41 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 147.79 E-value: 1.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 473 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQvVGFISQEPVLF-GTTIMEN 551
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE-IGYVFQDPQLFpRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 552 IRFGklaASDEEVYAAAREANAHEFITSFPEGY--NTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:pfam00005 80 LRLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
455-692 |
8.01e-41 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 149.81 E-value: 8.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 534
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-RRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVL-FGTTIMENI---------RFGKLAASDEE-VYAAAREANAHEFItsfpegyntivgERG-TTLSGGQKQR 602
Cdd:COG1120 78 AYVPQEPPApFGLTVRELValgryphlgLFGRPSAEDREaVEEALERTGLEHLA------------DRPvDELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 603 LAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHRIIVMADGRVWEAGTHEEL 679
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
250
....*....|...
gi 109068902 680 LKkgglyAELIRR 692
Cdd:COG1120 226 LT-----PELLEE 233
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
455-698 |
1.74e-40 |
|
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: 149.50 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGrdLRTLDPS--WLRG 531
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEEnlWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 532 QVVGFISQEP--VLFGTTIMENIRFG--KLAASDEE----VYAAAREANAHEFITSFPEgyntivgergtTLSGGQKQRL 603
Cdd:TIGR04520 77 KKVGMVFQNPdnQFVGATVEDDVAFGleNLGVPREEmrkrVDEALKLVGMEDFRDREPH-----------LLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 604 AIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLK 681
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRklNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
250
....*....|....*..
gi 109068902 682 KGglyaELIRRQALDAP 698
Cdd:TIGR04520 226 QV----ELLKEIGLDVP 238
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
456-691 |
4.81e-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: 147.31 E-value: 4.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 456 TFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRGQVvG 535
Cdd:COG4555 3 EVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQI-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 536 FISQEPVLF-GTTIMENIR-FGKLAASDEEVYAAAREANAHEFItsFPEGYNTIVGErgttLSGGQKQRLAIARALIKQP 613
Cdd:COG4555 78 VLPDERGLYdRLTVRENIRyFAELYGLFDEELKKRIEELIELLG--LEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 614 TVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEELLKKGG---LYAE 688
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIGeenLEDA 231
|
...
gi 109068902 689 LIR 691
Cdd:COG4555 232 FVA 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
455-682 |
1.12e-39 |
|
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: 146.19 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVA---SLLERfydPTAGVVMLDGRDLRTLDPSWLR 530
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIrciNGLER---PTSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 531 G--QVVGFISQEPVLFGT-TIMENIRFG-KLAASDEevyaAAREANAHEFITsfpegyntIVG--ERG----TTLSGGQK 600
Cdd:cd03258 79 KarRRIGMIFQHFNLLSSrTVFENVALPlEIAGVPK----AEIEERVLELLE--------LVGleDKAdaypAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 601 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHE 677
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
....*
gi 109068902 678 ELLKK 682
Cdd:cd03258 227 EVFAN 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
455-674 |
1.85e-39 |
|
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: 143.61 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlRGQVV 534
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA--LSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVLFGTTIMENIrfgklaasdeevyaaareanahefitsfpegyntivgerGTTLSGGQKQRLAIARALIKQPT 614
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 615 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAG 674
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
455-674 |
1.05e-38 |
|
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: 142.66 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPsWLRGqvV 534
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP-ERRN--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVLFGT-TIMENIRFG------KLAASDEEVYAAAREANAHEFITSFPEgyntivgergtTLSGGQKQRLAIAR 607
Cdd:cd03259 75 GMVFQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 608 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHRIIVMADGRVWEAG 674
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
458-670 |
4.00e-38 |
|
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: 139.46 E-value: 4.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRGQVvGFI 537
Cdd:cd03230 4 RNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRI-GYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 538 SQEPVLFGT-TIMENIRfgklaasdeevyaaareanahefitsfpegyntivgergttLSGGQKQRLAIARALIKQPTVL 616
Cdd:cd03230 79 PEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 617 ILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHRIIVMADGRV 670
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
455-670 |
4.00e-38 |
|
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: 141.07 E-value: 4.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYP-CRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlrgqv 533
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 VGFISQEPVLFG-TTIMENIRFGKLAASdeeVYAAAREANAHEFITsfpegyntIVGERGT------TLSGGQKQRLAIA 606
Cdd:cd03293 75 RGYVFQQDALLPwLTVLDNVALGLELQG---VPKAEARERAEELLE--------LVGLSGFenayphQLSGGMRQRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 607 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHRIIVMA--DGRV 670
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSarPGRI 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
455-680 |
4.22e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 144.84 E-value: 4.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVA---SLLERfydPTAGVVMLDGRDLRTLDPSWLR 530
Cdd:COG1135 2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 531 G--QVVGFISQEPVLFGT-TIMENIRFG-KLAasdeEVYAAAREANAHEFITsfpegyntIVG--ERGTT----LSGGQK 600
Cdd:COG1135 79 AarRKIGMIFQHFNLLSSrTVAENVALPlEIA----GVPKAEIRKRVAELLE--------LVGlsDKADAypsqLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 601 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHE 677
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVL 226
|
...
gi 109068902 678 ELL 680
Cdd:COG1135 227 DVF 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
187-684 |
5.68e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 152.44 E-value: 5.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 187 VQGLLTFG----------YLVLLS-HIGERMavdmRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQ 255
Cdd:PLN03232 955 VYALLGFGqvavtftnsfWLISSSlHAAKRL----HDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNM 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 256 GLRSCTQVAGCLVSLSMLSTR-----LTLLLMVATPALMGVGTlmGSGLRKLSRQCQEQIARAMGvadEALGNVRTVRAF 330
Cdd:PLN03232 1031 FMNQLWQLLSTFALIGTVSTIslwaiMPLLILFYAAYLYYQST--SREVRRLDSVTRSPIYAQFG---EALNGLSSIRAY 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 331 AMEQREEERYGAELEacrcraeelgrgialfqglSNIAFNcmvLGTLFIGGSLVAGQQLTGGdLMSFLVASQTVQRS--- 407
Cdd:PLN03232 1106 KAYDRMAKINGKSMD-------------------NNIRFT---LANTSSNRWLTIRLETLGG-VMIWLTATFAVLRNgna 1162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 408 ----------------MANLSVLFGQVVR-------GLSAGARVFEYMAL---SPCI-----PLSGGccipkeHLRGSVT 456
Cdd:PLN03232 1163 enqagfastmglllsyTLNITTLLSGVLRqaskaenSLNSVERVGNYIDLpseATAIiennrPVSGW------PSRGSIK 1236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 457 FQNVCFSYpcRPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVG 535
Cdd:PLN03232 1237 FEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLR-RVLS 1313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 536 FISQEPVLFGTTIMENIR-FGKlaASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPT 614
Cdd:PLN03232 1314 IIPQSPVLFSGTVRFNIDpFSE--HNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 615 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGG 684
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
458-681 |
8.39e-38 |
|
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: 141.09 E-value: 8.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYP-CRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGF 536
Cdd:COG1124 5 RNLSVSYGqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV-QM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 537 ISQEPVL-------FGTTIMENIRFGKLAASDEEVYAAAREAN-AHEFITSFPEgyntivgergtTLSGGQKQRLAIARA 608
Cdd:COG1124 84 VFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 609 LIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTVrgAH---RIIVMADGRVWEAGTHEEL 679
Cdd:COG1124 153 LILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVV--AHlcdRVAVMQNGRIVEELTVADL 226
|
..
gi 109068902 680 LK 681
Cdd:COG1124 227 LA 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
455-670 |
9.48e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.38 E-value: 9.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlrgqv 533
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 VGFISQEPVLFG-TTIMENIRFG-KLA-ASDEEVYAAAREANAH----EFITSFPegyntivgergTTLSGGQKQRLAIA 606
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGlELRgVPKAERRERARELLELvglaGFEDAYP-----------HQLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 607 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH------RLstvrgAHRIIVMAD--GRV 670
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRI 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
456-669 |
4.38e-37 |
|
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: 136.22 E-value: 4.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 456 TFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvG 535
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 536 FISQepvlfgttimenirfgklaasdeevyaaareanahefitsfpegyntivgergttLSGGQKQRLAIARALIKQPTV 615
Cdd:cd00267 77 YVPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 616 LILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTV-RGAHRIIVMADGR 669
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
458-681 |
6.06e-37 |
|
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: 140.96 E-value: 6.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDP---TAGVVMLDGRDLRTLDPS---WLR 530
Cdd:COG0444 5 RNLKVYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKelrKIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 531 GQVVGFISQEP---------VlfGTTIMENIRFGKLAaSDEEVYAAAREA-------NAHEFITSFP-Egyntivgergt 593
Cdd:COG0444 85 GREIQMIFQDPmtslnpvmtV--GDQIAEPLRIHGGL-SKAEARERAIELlervglpDPERRLDRYPhE----------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 594 tLSGGQKQRLAIARALIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTVRG-AHRIIVMA 666
Cdd:COG0444 151 -LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVAEiADRVAVMY 225
|
250
....*....|....*
gi 109068902 667 DGRVWEAGTHEELLK 681
Cdd:COG0444 226 AGRIVEEGPVEELFE 240
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
458-701 |
1.80e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.61 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYP--CRPGfevLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrTLDPSW-LRGQVv 534
Cdd:PRK13635 9 EHISFRYPdaATYA---LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-SEETVWdVRRQV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEP--VLFGTTIMENIRFGkLAASD-------EEVYAAAREANAHEFITSFPEgyntivgergtTLSGGQKQRLAI 605
Cdd:PRK13635 84 GMVFQNPdnQFVGATVQDDVAFG-LENIGvpreemvERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 606 ARALIKQPTVLILDEATSALDAESErvvQEALD-----RASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELL 680
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
250 260
....*....|....*....|.
gi 109068902 681 KKGglyaELIRRQALDAPRTV 701
Cdd:PRK13635 229 KSG----HMLQEIGLDVPFSV 245
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
131-428 |
2.20e-36 |
|
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: 138.69 E-value: 2.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 131 LGVAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHVGSFMTESRKLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDM 210
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 211 RRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMG 290
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 291 VGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGA---ELEACRCRAEELGrGIA--LFQGLS 365
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEineELYKASFKAQFYS-GLLmpIMNFIN 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109068902 366 NIAFncmvLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18547 240 NLGY----VLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
169-691 |
2.26e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 147.58 E-value: 2.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 169 SFMTESRKLSTHLLILY-GVQGLLTFG---------YLVLLSHIgeRMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRL 238
Cdd:PLN03130 939 SEWTDQGTPKTHGPLFYnLIYALLSFGqvlvtllnsYWLIMSSL--YAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRF 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 239 TTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQcqEQIARAMGVAD 318
Cdd:PLN03130 1017 AKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRL--DSITRSPVYAQ 1094
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 319 --EALGNVRTVRAFAMEQREEERYGAELEacrcraeelgrgialfqglSNIAFNCMVLGtlfiGGSLVAGQQLTGGDLMS 396
Cdd:PLN03130 1095 fgEALNGLSTIRAYKAYDRMAEINGRSMD-------------------NNIRFTLVNMS----SNRWLAIRLETLGGLMI 1151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 397 FLVASQTV--------QRSMA-----------NLSVLFGQVVR-------GLSAGARVFEYMALSPCIPL--SGGCCIPK 448
Cdd:PLN03130 1152 WLTASFAVmqngraenQAAFAstmglllsyalNITSLLTAVLRlaslaenSLNAVERVGTYIDLPSEAPLviENNRPPPG 1231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 449 EHLRGSVTFQNVCFSYpcRPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS 527
Cdd:PLN03130 1232 WPSSGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLM 1309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 528 WLRgQVVGFISQEPVLFGTTIMENIR-FGKlaASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIA 606
Cdd:PLN03130 1310 DLR-KVLGIIPQAPVLFSGTVRFNLDpFNE--HNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLA 1386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 607 RALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELL-KKGGL 685
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLsNEGSA 1466
|
....*.
gi 109068902 686 YAELIR 691
Cdd:PLN03130 1467 FSKMVQ 1472
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
451-691 |
6.98e-36 |
|
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: 136.19 E-value: 6.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 451 LRGSVTFQNVCFSYP--CRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSW 528
Cdd:cd03288 16 LGGEIKIHDLCVRYEnnLKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 529 LRGQVvGFISQEPVLFGTTIMENIRfGKLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARA 608
Cdd:cd03288 93 LRSRL-SIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 609 LIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELL-KKGGLYA 687
Cdd:cd03288 171 FVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFA 250
|
....
gi 109068902 688 ELIR 691
Cdd:cd03288 251 SLVR 254
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
455-670 |
8.48e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.57 E-value: 8.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--Q 532
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 533 VVGFISQEPVLFG-TTIMENIRFGKLAAS----------DEEVYAAAREANAhefitsfpegyntIVG------ERGTTL 595
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVLAGRLGRTstwrsllglfPPEDRERALEALE-------------RVGladkayQRADQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 596 SGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRG-AHRIIVMADGRV 670
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
459-670 |
2.25e-35 |
|
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: 132.77 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 459 NVCFSYpcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrtldPSWLRGQVVGFIS 538
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 539 QEP--VLFGTTIMENIRFGKLAASDEEVYAAA--REANAHEFITSFPegyntivgergTTLSGGQKQRLAIARALIKQPT 614
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAGNEQAETvlKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 615 VLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHR---LSTVrgAHRIIVMADGRV 670
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDyefLAKV--CDRVLLLANGAI 204
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
454-679 |
2.43e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 137.15 E-value: 2.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGqv 533
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-PPEKRN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 VGFISQEPVLFG-TTIMENIRFG-KLAAsdeeVYAAAREANAHEF-----ITSFpegyntivGERG-TTLSGGQKQRLAI 605
Cdd:COG3842 79 VGMVFQDYALFPhLTVAENVAFGlRMRG----VPKAEIRARVAELlelvgLEGL--------ADRYpHQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 606 ARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS---TVrgAHRIIVMADGRVWEAGTHEEL 679
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
455-678 |
4.37e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.48 E-value: 4.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRg 531
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 532 QVVGFISQE-PVLFGTTIMENIRFGKLAA--SDEEVYAAAREA----NAHEFITSFPEgyntivgergtTLSGGQKQRLA 604
Cdd:COG2884 79 RRIGVVFQDfRLLPDRTVYENVALPLRVTgkSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 605 IARALIKQPTVLILDEATSALDAE-SERVVqEALDRASA-GRTVLVIAHRLSTVRGA-HRIIVMADGRVWEAGTHEE 678
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRrGTTVLIATHDLELVDRMpKRVLELEDGRLVRDEARGV 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
455-669 |
4.65e-35 |
|
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: 131.16 E-value: 4.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWL-RGQV 533
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPpLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 VGFISQEPVLF-GTTIMENIRFGklaasdeevyaaareanahefitsfpegyntivgergttLSGGQKQRLAIARALIKQ 612
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 613 PTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHRIIVMADGR 669
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
181-690 |
6.04e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 143.19 E-value: 6.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 181 LLILYGVqgllTFGYLV---LLSHIGeRMAVDMRRALFSSLLRQDIAF-FDANK---TGQLVSRLTTDVQEFKSsfklvI 253
Cdd:PLN03232 345 FLIFFGV----TFGVLCesqYFQNVG-RVGFRLRSTLVAAIFHKSLRLtHEARKnfaSGKVTNMITTDANALQQ-----I 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 254 SQGLRSCTQVAGCL-VSLSMLSTRL-------TLLLMVATPalmgVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVR 325
Cdd:PLN03232 415 AEQLHGLWSAPFRIiVSMVLLYQQLgvaslfgSLILFLLIP----LQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMD 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 326 TVRAFAMEQREEERYGAeleacrCRAEELgrgiALF---QGLSniAFNCMVLGTLFIGGSLVAGQQ--LTGGDL-----M 395
Cdd:PLN03232 491 TVKCYAWEKSFESRIQG------IRNEEL----SWFrkaQLLS--AFNSFILNSIPVVVTLVSFGVfvLLGGDLtparaF 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 396 SFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFEYM-----ALSPCIPLSGGccIPkehlrgSVTFQNVCFSYPCRPGF 470
Cdd:PLN03232 559 TSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLlseerILAQNPPLQPG--AP------AISIKNGYFSWDSKTSK 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVAS--LLERFYDPTAGVVmldgrdlrtldpswLRGQVvGFISQEPVLFGTTI 548
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISamLGELSHAETSSVV--------------IRGSV-AYVPQVSWIFNATV 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 549 MENIRFGklAASDEEVYAAAREANA--HEfITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 626
Cdd:PLN03232 696 RENILFG--SDFESERYWRAIDVTAlqHD-LDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 627 AE-SERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAELI 690
Cdd:PLN03232 773 AHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
455-680 |
6.99e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 132.43 E-value: 6.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTV---ASLLERfydPTAGVVMLDGRDL--RTLDPSWL 529
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLtdSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 530 RGQVvGFISQEPVLFG-TTIMENIRFG-----KLaaSDEEVYAAAREANAH----EFITSFPEgyntivgergtTLSGGQ 599
Cdd:COG1126 76 RRKV-GMVFQQFNLFPhLTVLENVTLApikvkKM--SKAEAEERAMELLERvglaDKADAYPA-----------QLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 600 KQRLAIARALIKQPTVLILDEATSALDAEserVVQEALD--R--ASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAG 674
Cdd:COG1126 142 QQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEG 218
|
....*.
gi 109068902 675 THEELL 680
Cdd:COG1126 219 PPEEFF 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
455-681 |
1.39e-34 |
|
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: 131.64 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRG 531
Cdd:COG1127 6 IEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 532 QVvGFISQEPVLFGT-TIMENIRF-----GKLaaSDEEVYAAAREA----NAHEFITSFPegyntivGErgttLSGGQKQ 601
Cdd:COG1127 83 RI-GMLFQGGALFDSlTVFENVAFplrehTDL--SEAEIRELVLEKlelvGLPGAADKMP-------SE----LSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 602 RLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEE 678
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRelRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
...
gi 109068902 679 LLK 681
Cdd:COG1127 229 LLA 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
458-674 |
1.95e-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: 129.48 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFI 537
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA-RKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 538 SQepvlfgttIMENIRFGKLAasdeevyaaareanahefitsfpegyntivgERG-TTLSGGQKQRLAIARALIKQPTVL 616
Cdd:cd03214 79 PQ--------ALELLGLAHLA-------------------------------DRPfNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109068902 617 ILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHRIIVMADGRVWEAG 674
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
456-679 |
3.46e-34 |
|
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: 130.77 E-value: 3.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 456 TFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQV-- 533
Cdd:cd03256 2 EVENLSKTYP--NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 VGFISQEPVLFG-TTIMENIRFGKLAAS----------DEEVYAAAREA----NAHEFITSfpegyntivgeRGTTLSGG 598
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRLGRRstwrslfglfPKEEKQRALAAlervGLLDKAYQ-----------RADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 599 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGT 675
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGP 228
|
....
gi 109068902 676 HEEL 679
Cdd:cd03256 229 PAEL 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
469-681 |
2.03e-33 |
|
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: 128.32 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS--WLRGQVVGFisQEPVLFGT 546
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHeiARLGIGRTF--QIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 -TIMENIR--------FGKLAASDEEVYAAAREAnAHEFITSF--PEGYNTIVGErgttLSGGQKQRLAIARALIKQPTV 615
Cdd:cd03219 90 lTVLENVMvaaqartgSGLLLARARREEREARER-AEELLERVglADLADRPAGE----LSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 616 LILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELLK 681
Cdd:cd03219 165 LLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
455-680 |
2.64e-33 |
|
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: 128.19 E-value: 2.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 534
Cdd:cd03295 1 IEFENVTKRYG--GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR-RKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVLF-GTTIMENIrfgKLAASDEEVYAAAREANAHEFITSF---PEGYntivGER-GTTLSGGQKQRLAIARAL 609
Cdd:cd03295 78 GYVIQQIGLFpHMTVEENI---ALVPKLLKWPKEKIRERADELLALVgldPAEF----ADRyPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 610 IKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRL-STVRGAHRIIVMADGRVWEAGTHEELL 680
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRlqQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
455-681 |
6.53e-33 |
|
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: 126.85 E-value: 6.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--Q 532
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 533 VVGFISQEPVLFGT-TIMENIRFG---KLAASDEEVYAAARE----ANAHEFITSFPegyntivGErgttLSGGQKQRLA 604
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLEkleaVGLRGAEDLYP-------AE----LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 605 IARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELLK 681
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
457-698 |
6.82e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.80 E-value: 6.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 457 FQNVCFSYPcrPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvG 535
Cdd:PRK13632 10 VENVSFSYP--NSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKI-G 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 536 FISQEP--VLFGTTIMENIRFG---KLAASDE---EVYAAAREANAHEFITSFPEgyntivgergtTLSGGQKQRLAIAR 607
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGlenKKVPPKKmkdIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 608 ALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKggl 685
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN--- 232
|
250
....*....|...
gi 109068902 686 yAELIRRQALDAP 698
Cdd:PRK13632 233 -KEILEKAKIDSP 244
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
198-428 |
7.83e-33 |
|
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: 128.22 E-value: 7.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 198 LLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRL 277
Cdd:cd18590 59 LFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 278 TLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRG 357
Cdd:cd18590 139 TLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTV 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109068902 358 IALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18590 219 RAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
455-680 |
3.42e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.20 E-value: 3.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRtldpswLRGQVV 534
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR------RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVL---FGTTIMENIR---------FGKLAASD-EEVYAAAREANAHEFItsfpegyNTIVGErgttLSGGQKQ 601
Cdd:COG1121 78 GYVPQRAEVdwdFPITVRDVVLmgrygrrglFRRPSRADrEAVDEALERVGLEDLA-------DRPIGE----LSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 602 RLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVwEAGTHEEL 679
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLV-AHGPPEEV 225
|
.
gi 109068902 680 L 680
Cdd:COG1121 226 L 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
469-670 |
4.08e-32 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 123.79 E-value: 4.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSW--LRgQVVGFISQEPVLFG- 545
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLR-QKVGMVFQQFNLFPh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 546 TTIMENIRFGK---LAASDEEVYAAAREANAH----EFITSFPegyntivgergTTLSGGQKQRLAIARALIKQPTVLIL 618
Cdd:cd03262 91 LTVLENITLAPikvKGMSKAEAEERALELLEKvglaDKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 619 DEATSALDAEserVVQEALD----RASAGRTVLVIAHRLSTVRG-AHRIIVMADGRV 670
Cdd:cd03262 160 DEPTSALDPE---LVGEVLDvmkdLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
455-679 |
4.29e-32 |
|
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: 124.15 E-value: 4.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPgFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVV 534
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAAR-QSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVLFGT-TIMENIRF-----GKlaaSDEEVYAaarEANAHEFITSFPEGYNTIVGergtTLSGGQKQRLAIARA 608
Cdd:cd03263 78 GYCPQFDALFDElTVREHLRFyarlkGL---PKSEIKE---EVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 609 LIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEEL 679
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
458-680 |
7.21e-32 |
|
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: 130.57 E-value: 7.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYPCRPG--------FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFyDPTAGVVMLDGRDLRTLDPSWL 529
Cdd:COG4172 279 RDLKVWFPIKRGlfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 530 RG-----QVVgFisQEPvlFGT---------TIMENIRFGKLAASDEEVYAAAREANA-------------HEFitsfpe 582
Cdd:COG4172 358 RPlrrrmQVV-F--QDP--FGSlsprmtvgqIIAEGLRVHGPGLSAAERRARVAEALEevgldpaarhrypHEF------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 583 gyntivgergttlSGGQKQRLAIARALIKQPTVLILDEATSALDaeseRVVQ-EALD-----RASAGRTVLVIAHRLSTV 656
Cdd:COG4172 427 -------------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVV 489
|
250 260
....*....|....*....|....*
gi 109068902 657 RG-AHRIIVMADGRVWEAGTHEELL 680
Cdd:COG4172 490 RAlAHRVMVMKDGKVVEQGPTEQVF 514
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
131-428 |
8.27e-32 |
|
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: 125.29 E-value: 8.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 131 LGVAIVLALGAALVNVQIPLLLGQLVeivakytrDHVGSFmTESRKLSTHLLILYGV---QGLLTFGYLVLLSHIGERMA 207
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAI--------DGPIAH-GDRSALWPLVLLLLALgvaEAVLSFLRRYLAGRLSLGVE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 208 VDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTD---VQEFKSSFKLVISQGLrsctQVAGCLVSLSMLSTRLTLLLMVA 284
Cdd:cd18543 72 HDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDlslVQRFLAFGPFLLGNLL----TLVVGLVVMLVLSPPLALVALAS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 285 TPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEER--------YGAELEACRCRAeelgR 356
Cdd:cd18543 148 LPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRfeaaarrlRATRLRAARLRA----R 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 357 GIALFQGLSNIAfncmVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18543 224 FWPLLEALPELG----LAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
131-399 |
1.31e-31 |
|
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: 124.83 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 131 LGVAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDhvgsfMTESRKLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDM 210
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLT-----ASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 211 RRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMG 290
Cdd:cd18541 76 RNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 291 VGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFN 370
Cdd:cd18541 156 LVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIG 235
|
250 260
....*....|....*....|....*....
gi 109068902 371 CMVLGTLFIGGSLVAGQQLTGGDLMSFLV 399
Cdd:cd18541 236 LSFLIVLWYGGRLVIRGTITLGDLVAFNS 264
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
456-680 |
1.79e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 122.56 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 456 TFQNVCFSYPcrpgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqvVG 535
Cdd:COG3840 3 RLDDLTYRYG-----DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERP--VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 536 FISQEPVLFG-TTIMENIRFG-----KLAASD-EEVYAAAREANAHEFITSFPEgyntivgergtTLSGGQKQRLAIARA 608
Cdd:COG3840 75 MLFQENNLFPhLTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 609 LIKQPTVLILDEATSALD----AESERVVQEAldRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELL 680
Cdd:COG3840 144 LVRKRPILLLDEPFSALDpalrQEMLDLVDEL--CRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
454-681 |
3.59e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 125.26 E-value: 3.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASL---LERfydPTAGVVMLDGRDLRTLDPSWLR 530
Cdd:COG1118 2 SIEVRNISKRFG---SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 531 GqvVGFISQEPVLFG-TTIMENIRFG--KLAASDEEVYAAARE----ANAHEFITSFPegyntivgergTTLSGGQKQRL 603
Cdd:COG1118 76 R--VGFVFQHYALFPhMTVAENIAFGlrVRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 604 AIARALIKQPTVLILDEATSALDA----ESERVVQEALDRasAGRTVLVIAH------RLstvrgAHRIIVMADGRVWEA 673
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDE--LGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQV 215
|
....*...
gi 109068902 674 GTHEELLK 681
Cdd:COG1118 216 GTPDEVYD 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
473-680 |
8.92e-31 |
|
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: 121.98 E-value: 8.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 473 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWL---RGQVVGFISQEPVLF-GTTI 548
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelRRKKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 549 MENIRFG-KLAASDEEV-YAAAREA----NAHEFITSFPegyntivGErgttLSGGQKQRLAIARALIKQPTVLILDEAT 622
Cdd:cd03294 120 LENVAFGlEVQGVPRAErEERAAEAlelvGLEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109068902 623 SALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHRIIVMADGRVWEAGTHEELL 680
Cdd:cd03294 189 SALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
458-679 |
1.07e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 121.30 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGV-----VMLDGRDL--RTLDPSWLR 530
Cdd:COG1117 15 RNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 531 GQVvGFISQEPVLFGTTIMENIRFG-KL------AASDEEVYAAAREANAHEfitsfpEgyntiVGER----GTTLSGGQ 599
Cdd:COG1117 92 RRV-GMVFQKPNPFPKSIYDNVAYGlRLhgikskSELDEIVEESLRKAALWD------E-----VKDRlkksALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 600 KQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLS-TVRGAHRIIVMADGRVWEAGTHEE 678
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEFGPTEQ 239
|
.
gi 109068902 679 L 679
Cdd:COG1117 240 I 240
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
172-679 |
1.19e-30 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 129.51 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 172 TESRKLS--THLLILYGVQGLLTFGY---LVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFK 246
Cdd:PTZ00243 990 TRSFKLSaaTYLYVYLGIVLLGTFSVplrFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILD 1069
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 247 SSFKLVISQgLRSCTqvAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMG---SGLRKLSRQCQEQIARAMGVADEALGN 323
Cdd:PTZ00243 1070 NTLPMSYLY-LLQCL--FSICSSILVTSASQPFVLVALVPCGYLYYRLMQfynSANREIRRIKSVAKSPVFTLLEEALQG 1146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 324 VRTVRAFAMEQ---REEERYGAELEACRCRAEELGRGIAL-FQGLSNIAFNCMVLgTLFIGGSLVAGQQLTGGDLMSFLV 399
Cdd:PTZ00243 1147 SATITAYGKAHlvmQEALRRLDVVYSCSYLENVANRWLGVrVEFLSNIVVTVIAL-IGVIGTMLRATSQEIGLVSLSLTM 1225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 400 ASQT--------------------VQR-----------SMANLSVLFGQVVRGLSAGARVFEYMALSPCIPLSGGcciPK 448
Cdd:PTZ00243 1226 AMQTtatlnwlvrqvatveadmnsVERllyytdevpheDMPELDEEVDALERRTGMAADVTGTVVIEPASPTSAA---PH 1302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 449 EHLRGSVTFQNVCFSYpcRPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS 527
Cdd:PTZ00243 1303 PVQAGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLR 1380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 528 WLRGQVvGFISQEPVLFGTTIMENIR-FgkLAASDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIA 606
Cdd:PTZ00243 1381 ELRRQF-SMIPQDPVLFDGTVRQNVDpF--LEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMA 1457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 607 RALIKQPTVLIL-DEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEEL 679
Cdd:PTZ00243 1458 RALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
464-679 |
1.67e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 122.53 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 464 YPCRPGF-----EVLK---DFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG---- 531
Cdd:COG4608 17 FPVRGGLfgrtvGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 532 -QVVgFisQEP---------VlfGTTIMENIRFGKLAaSDEEVYAAAREA-------------NAHEFitsfpegyntiv 588
Cdd:COG4608 97 mQMV-F--QDPyaslnprmtV--GDIIAEPLRIHGLA-SKAERRERVAELlelvglrpehadrYPHEF------------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 589 gergttlSGGQKQRLAIARALIKQPTVLILDEATSALD----AEserVV------QEALdrasaGRTVLVIAHRLSTVRG 658
Cdd:COG4608 159 -------SGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQ---VLnlledlQDEL-----GLTYLFISHDLSVVRH 223
|
250 260
....*....|....*....|..
gi 109068902 659 -AHRIIVMADGRVWEAGTHEEL 679
Cdd:COG4608 224 iSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
472-682 |
2.19e-30 |
|
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: 119.75 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqvVGFISQEPVLF-GTTIME 550
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-KRD--ISYVPQNYALFpHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 551 NIRFG--KLAASDEEVYAAAREanahefITSFpEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE 628
Cdd:cd03299 91 NIAYGlkKRKVDKKEIERKVLE------IAEM-LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 629 SERVVQEALDRA--SAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELLKK 682
Cdd:cd03299 164 TKEKLREELKKIrkEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
133-428 |
2.83e-30 |
|
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: 120.97 E-value: 2.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 133 VAIVLALGAALVNVQIPLLLGQLV-EIVAKYTRDHV---GSFMtesrklsthlLILYGVQGLLTFGYLVLLSHIGERMAV 208
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIIdEGIANGDLSYIlrtGLLM----------LLLALLGLIAGILAGYFAAKASQGFGR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 209 DMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPAL 288
Cdd:cd18548 73 DLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 289 MGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIA 368
Cdd:cd18548 153 ALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLI 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109068902 369 FNCMVLGTLFIGGSLVAGQQLTGGDLMSFL-VASQTVQrSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18548 233 MNLAIVAILWFGGHLINAGSLQVGDLVAFInYLMQILM-SLMMLSMVFVMLPRASASAKRI 292
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
469-680 |
2.85e-30 |
|
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: 119.08 E-value: 2.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGQV-VGFISQEPVLFGT- 546
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGL-PPHERARAgIGYVPEGRRIFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 TIMENIRFG-------KLAASDEEVYAAareanahefitsFPegyntIVGER----GTTLSGGQKQRLAIARALIKQPTV 615
Cdd:cd03224 91 TVEENLLLGayarrraKRKARLERVYEL------------FP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 616 LILDEATSALdaeSERVVQEALDR----ASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELL 680
Cdd:cd03224 154 LLLDEPSEGL---APKIVEEIFEAirelRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
455-679 |
9.41e-30 |
|
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: 117.72 E-value: 9.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqvV 534
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-KRP--V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVLF-GTTIMENIRFG-KLAASD-----EEVYAAAREANAHEFITSFPEgyntivgergtTLSGGQKQRLAIAR 607
Cdd:cd03300 75 NTVFQNYALFpHLTVFENIAFGlRLKKLPkaeikERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 608 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS---TVrgAHRIIVMADGRVWEAGTHEEL 679
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEI 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
469-670 |
1.86e-29 |
|
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: 117.45 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWL--RGQVVGFisQEPVLFGT 546
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarLGIARTF--QNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 -TIMENI-----------------RFGKLAASDEEVYAAAREAnAHEFitsfpeGYNTIVGERGTTLSGGQKQRLAIARA 608
Cdd:COG0411 94 lTVLENVlvaaharlgrgllaallRLPRARREEREARERAEEL-LERV------GLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 609 LIKQPTVLILDEATSAL-DAESERVVQ--EALdRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRV 670
Cdd:COG0411 167 LATEPKLLLLDEPAAGLnPEETEELAEliRRL-RDERGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
468-670 |
2.27e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.43 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP--SWLRGqvVGFISQEPVLFG 545
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdAQAAG--IAIIHQELNLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 546 T-TIMENIRFGKLAAS-----DEEVYAAAREAnAHEFITSFPEgyNTIVGErgttLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:COG1129 93 NlSVAENIFLGREPRRgglidWRAMRRRAREL-LARLGLDIDP--DTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 620 EATSAL-DAESER---VVQEaLdrASAGRTVLVIAHRLSTVRG-AHRIIVMADGRV 670
Cdd:COG1129 166 EPTASLtEREVERlfrIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
131-428 |
2.42e-29 |
|
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: 118.77 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 131 LGVAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHVGSFMTESRKLSTH---------LLILYGVQGLLTFGYLVLLSH 201
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLGLAPLLGPDPLallllaaaaLVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 202 IGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLL 281
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 282 MVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAE----LEAcRCRAEELGrg 357
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFAREnrksLRA-GLRAARLQ-- 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109068902 358 iALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18564 238 -ALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
455-670 |
3.58e-29 |
|
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: 113.68 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVV 534
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQepvlfgttimenirfgklaasdeevyaaareanahefitsfpegyntivgergttLSGGQKQRLAIARALIKQPT 614
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 615 VLILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRV 670
Cdd:cd03216 103 LLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
453-679 |
7.32e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 118.25 E-value: 7.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 453 GSVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTvasLLeR----FYDPTAGVVMLDGRDLRTLDPSw 528
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKST---LL-RmiagLEDPTSGEILIGGRDVTDLPPK- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 529 LRGqvVGFISQEPVLFGT-TIMENIRFG----KLAAS--DEEVYAAAREANAHEFITSFPegyntivgergTTLSGGQKQ 601
Cdd:COG3839 74 DRN--IAMVFQSYALYPHmTVYENIAFPlklrKVPKAeiDRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 602 RLAIARALIKQPTVLILDEATSALDAESeRV--------VQEALdrasaGRTVLVIAH------RLstvrgAHRIIVMAD 667
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRL-----GTTTIYVTHdqveamTL-----ADRIAVMND 209
|
250
....*....|..
gi 109068902 668 GRVWEAGTHEEL 679
Cdd:COG3839 210 GRIQQVGTPEEL 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
469-680 |
7.93e-29 |
|
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: 115.08 E-value: 7.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGT-T 547
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 548 IMENIRFGKLAASDEEVYAAAREAnAHEFitsFPegyntIVGER----GTTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:COG0410 95 VEENLLLGAYARRDRAEVRADLER-VYEL---FP-----RLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 624 ALdaeSERVVQE---ALDR-ASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELL 680
Cdd:COG0410 166 GL---APLIVEEifeIIRRlNREGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELL 224
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
131-428 |
1.03e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 116.48 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 131 LGVAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHvgsfmTESRKLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDM 210
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSL-----GLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 211 RRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMG 290
Cdd:cd18778 76 RSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 291 VGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAelEACRCRAEELGrgiALFqgLSNIAFN 370
Cdd:cd18778 156 GAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEA--LSRRYRKAQLR---AMK--LWAIFHP 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 371 CMV----LGT---LFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18778 229 LMEfltsLGTvlvLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
457-670 |
1.04e-28 |
|
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: 114.17 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 457 FQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTldpSWLRgqvVGF 536
Cdd:cd03235 2 VEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKR---IGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 537 ISQEPVL---FGTTIMENIR---------FGKLAASDeevYAAAREAnaHEFItsfpeGYNTIVGERGTTLSGGQKQRLA 604
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLmglyghkglFRRLSKAD---KAKVDEA--LERV-----GLSELADRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 605 IARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRGAHRIIVMADGRV 670
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
455-675 |
1.80e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 117.21 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPC-RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLERfydPTAGVVMLDGRDLRTLDPSWLR 530
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 531 G--QVVGFISQE-PVLFGTTIMENIRFG-KLAASDEevyaAAREANAHEFITsfpegyntIVG--ERGTT----LSGGQK 600
Cdd:PRK11153 79 KarRQIGMIFQHfNLLSSRTVFDNVALPlELAGTPK----AEIKARVTELLE--------LVGlsDKADRypaqLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 601 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGT 675
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
195-398 |
3.62e-28 |
|
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: 114.88 E-value: 3.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 195 YLVLLSHIGERMavdmRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLS 274
Cdd:cd18589 60 YNITMSRIHSRL----QGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 275 TRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRC--RAE 352
Cdd:cd18589 136 PKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRlnKKE 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 109068902 353 ELGRGIALF-QGLSNIAfncMVLGTLFIGGSLVAGQQLTGGDLMSFL 398
Cdd:cd18589 216 AAAYAVSMWtSSFSGLA---LKVGILYYGGQLVTAGTVSSGDLVTFV 259
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
131-428 |
4.09e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 114.91 E-value: 4.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 131 LGVAIVLALGAALVNVQIPLLLGQLVeivakytrDHVgsFMTESRKLSTHLLILY-----GVQGLLTF-----GYLvlLS 200
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILI--------DDV--LIQLGPGGNTSLLLLLvlglaGAYVLSALlgilrGRL--LA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 201 HIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLL 280
Cdd:cd18563 69 RLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 281 LMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIAL 360
Cdd:cd18563 149 VLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWAT 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 361 FQGLSNIafnCMVLGTLFI---GGSLVAGQQLTGGDLMSFLV-ASQTVQRsMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18563 229 FFPLLTF---LTSLGTLIVwyfGGRQVLSGTMTLGTLVAFLSyLGMFYGP-LQWLSRLNNWITRALTSAERI 296
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
454-679 |
7.46e-28 |
|
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: 112.43 E-value: 7.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlRGQV 533
Cdd:cd03296 2 SIEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 VGFISQEPVLFG-TTIMENIRFG-KLAASDEEVYAAAREANAHEFI-----TSFPEGYNTivgergtTLSGGQKQRLAIA 606
Cdd:cd03296 76 VGFVFQHYALFRhMTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYPA-------QLSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 607 RALIKQPTVLILDEATSALDA----ESERVVQEALDRASAgRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEEL 679
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHV-TTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
455-701 |
8.84e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.58 E-value: 8.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPGFE--VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML------DGRDLRTLDP 526
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 527 swLRgQVVGFISQ--EPVLFGTTIMENIRFGKL--AASDEEVYAAAREANA-----HEFITSFPegyntivgergTTLSG 597
Cdd:PRK13634 83 --LR-KKVGIVFQfpEHQLFEETVEKDICFGPMnfGVSEEDAKQKAREMIElvglpEELLARSP-----------FELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 598 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAG 674
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQG 228
|
250 260
....*....|....*....|....*..
gi 109068902 675 THEELLKKGglyAELIRRQaLDAPRTV 701
Cdd:PRK13634 229 TPREIFADP---DELEAIG-LDLPETV 251
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
131-428 |
2.89e-27 |
|
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: 112.48 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 131 LGVAIVLALGAALVNVQIPLLLGQLV-EIVAKYTRDHVGSFMtesrkLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVD 209
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIdDYIVPGQGDLQGLLL-----LALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 210 MRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALM 289
Cdd:cd18544 76 LRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 290 GVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGA---ELEACRCRAEELGrgiALF----Q 362
Cdd:cd18544 156 LATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEinqEYRKANLKSIKLF---ALFrplvE 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 363 GLSNIAfncmVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18544 233 LLSSLA----LALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
454-696 |
3.40e-27 |
|
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: 118.51 E-value: 3.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYpCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswlrgqv 533
Cdd:TIGR00957 636 SITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 VGFISQEPVLFGTTIMENIRFGKlaASDEEVYAAAREANAH-EFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQ 612
Cdd:TIGR00957 701 VAYVPQQAWIQNDSLRENILFGK--ALNEKYYQQVLEACALlPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 613 PTVLILDEATSALDAESERVVQEAL---DRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAEL 689
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
....*..
gi 109068902 690 IRRQALD 696
Cdd:TIGR00957 859 LRTYAPD 865
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
475-674 |
4.41e-27 |
|
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: 109.50 E-value: 4.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 475 DFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlrGQVVGFISQEPVLFG-TTIMENIR 553
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRPVSMLFQENNLFAhLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 554 FG-----KLAASDEE-VYAAAREANAHEFITSFPEgyntivgergtTLSGGQKQRLAIARALIKQPTVLILDEATSALD- 626
Cdd:cd03298 93 LGlspglKLTAEDRQaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDp 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 109068902 627 AESERVVQEALD-RASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAG 674
Cdd:cd03298 162 ALRAEMLDLVLDlHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
458-705 |
4.71e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.63 E-value: 4.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSypcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPsWLRGQVVGFI 537
Cdd:PRK13548 6 RNLSVR---LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 538 SQEPVL-FGTTIMENIRFGKL------AASDEEVYAAAREANAHEFITSFpegYntivgergTTLSGGQKQRLAIARALI 610
Cdd:PRK13548 82 PQHSSLsFPFTVEEVVAMGRAphglsrAEDDALVAAALAQVDLAHLAGRD---Y--------PQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 611 ------KQPTVLILDEATSALD-AESERVVQEALDRA-SAGRTVLVIAHRLS-TVRGAHRIIVMADGRVWEAGTHEELLK 681
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAhERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
250 260
....*....|....*....|....
gi 109068902 682 kgglyAELIRRqALDAPRTVAPPP 705
Cdd:PRK13548 231 -----PETLRR-VYGADVLVQPHP 248
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
471-694 |
5.29e-27 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 110.16 E-value: 5.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL---ERfYDPTAGVVMLDGRDLRTLDPS--WLRGQVVGFisQEPV--- 542
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPDerARAGIFLAF--QYPVeip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 -----LFGTTIMENIRFGKLAASD--EEVYAAAREAN-AHEFITSfpeGYNtiVGergttLSGGQKQRLAIARALIKQPT 614
Cdd:COG0396 91 gvsvsNFLRTALNARRGEELSAREflKLLKEKMKELGlDEDFLDR---YVN--EG-----FSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 615 VLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAH--RLSTVRGAHRIIVMADGRVWEAGTHE---ELLKKGglYAE 688
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKElalELEEEG--YDW 238
|
....*.
gi 109068902 689 LIRRQA 694
Cdd:COG0396 239 LKEEAA 244
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
119-679 |
7.87e-27 |
|
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: 117.32 E-value: 7.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 119 LFWQFLRphllalgVAIVLALGAALVNVQiPLLLGQlveIVAKYTRDHvgsfmTESRKLSTHLLI----LYGVQGLLTFG 194
Cdd:TIGR01271 78 FFWRFVF-------YGILLYFGEATKAVQ-PLLLGR---IIASYDPFN-----APEREIAYYLALglclLFIVRTLLLHP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 195 YLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFklvisqGLRSCTQVA--GCLVSLSM 272
Cdd:TIGR01271 142 AIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGL------ALAHFVWIAplQVILLMGL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 273 LSTRLTLLLMVATPALMGVGtLMGSGLRKLSRQCQEQ----IARAMGVADEALGNVRTVRAF----AMEQREEERYGAEL 344
Cdd:TIGR01271 216 IWELLEVNGFCGLGFLILLA-LFQACLGQKMMPYRDKragkISERLAITSEIIENIQSVKAYcweeAMEKIIKNIRQDEL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 345 EACR----CR--------------------AEELGRGIALFQGLSNIAFnCMVLgtlfiggSLVAGQQLTGG-------- 392
Cdd:TIGR01271 295 KLTRkiayLRyfyssafffsgffvvflsvvPYALIKGIILRRIFTTISY-CIVL-------RMTVTRQFPGAiqtwydsl 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 393 ----DLMSFLVASQ--TVQRSMANLSVLFGQVVRGLSAG-ARVFEYMAlspciplsggcciPKEHLRG------SVTFQN 459
Cdd:TIGR01271 367 gaitKIQDFLCKEEykTLEYNLTTTEVEMVNVTASWDEGiGELFEKIK-------------QNNKARKqpngddGLFFSN 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 460 vcFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswlrgqvVGFISQ 539
Cdd:TIGR01271 434 --FSLYVTP---VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQ 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 540 EPVLFGTTIMENIRFGklAASDEEVYAAAREA-NAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLIL 618
Cdd:TIGR01271 495 TSWIMPGTIKDNIIFG--LSYDEYRYTSVIKAcQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLL 572
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 619 DEATSALDAESER-VVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEEL 679
Cdd:TIGR01271 573 DSPFTHLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
455-680 |
8.09e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.46 E-value: 8.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDlrTLDPSWLRG--Q 532
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGirK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 533 VVGFISQEP--VLFGTTIMENIRFG--KLAASDEEVYAAAREANAHEFITSFPEgyntivgERGTTLSGGQKQRLAIARA 608
Cdd:PRK13644 78 LVGIVFQNPetQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRALAEIGLEKYRH-------RSPKTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109068902 609 LIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELL 680
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
454-670 |
9.42e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 108.02 E-value: 9.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYPCRPG---FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL--ERFYDPTAGVVMLDGRDLrtlDPSW 528
Cdd:cd03213 3 TLSFRNLTVTVKSSPSksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 529 LRGQVvGFISQEPVLFGT-TIMENIRFgklaasdeevyaAAREanahefitsfpegyntivgeRGttLSGGQKQRLAIAR 607
Cdd:cd03213 80 FRKII-GYVPQDDILHPTlTVRETLMF------------AAKL--------------------RG--LSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 608 ALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLST--VRGAHRIIVMADGRV 670
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRV 190
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
277-690 |
1.08e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 117.15 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 277 LTLLLMVATPalmgvgTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAeleacrCRAEELG- 355
Cdd:PLN03130 448 LMLVLMFPIQ------TFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQT------VRDDELSw 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 356 -RGIALFQGLSNIAFNCM-VLGTL-------FIGGSLVAGQQLTGGDLMS------FLVASQTVQRSMANLSVLFGQVVr 420
Cdd:PLN03130 516 fRKAQLLSAFNSFILNSIpVLVTVvsfgvftLLGGDLTPARAFTSLSLFAvlrfplFMLPNLITQAVNANVSLKRLEEL- 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 421 gLSAGARVfeymaLSPCIPLSGGccIPkehlrgSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVA 500
Cdd:PLN03130 595 -LLAEERV-----LLPNPPLEPG--LP------AISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLI 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 501 SLLERFYDPTAGVVMLdgrdlrtldpswLRGQVvGFISQEPVLFGTTIMENIRFGklAASDEEVYAAAREANA-HEFITS 579
Cdd:PLN03130 661 SAMLGELPPRSDASVV------------IRGTV-AYVPQVSWIFNATVRDNILFG--SPFDPERYERAIDVTAlQHDLDL 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 580 FPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESER-VVQEALDRASAGRT-VLVI--AHRLST 655
Cdd:PLN03130 726 LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRqVFDKCIKDELRGKTrVLVTnqLHFLSQ 805
|
410 420 430
....*....|....*....|....*....|....*
gi 109068902 656 VrgaHRIIVMADGRVWEAGTHEELLKKGGLYAELI 690
Cdd:PLN03130 806 V---DRIILVHEGMIKEEGTYEELSNNGPLFQKLM 837
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
130-428 |
1.32e-26 |
|
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: 110.25 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 130 ALGVAIVLALGAALVNVQIPLLLGQLVE--IVAKytrdHVGSFMTesrkLSTHLLILYGVQGLLTFGYLVLLSHIGERMA 207
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDeyIPNG----DLSGLLI----IALLFLALNLVNWVASRLRIYLMAKVGQRIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 208 VDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVqefkSSFKLVISQGL----RSCTQVAGCLVSLSMLSTRLTLLLMV 283
Cdd:cd18545 73 YDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDV----NSLSDLLSNGLinliPDLLTLVGIVIIMFSLNVRLALVTLA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 284 ATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEER--------YGAELEACRcraeelg 355
Cdd:cd18545 149 VLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIfdelnrenRKANMRAVR------- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 356 rgiaLFQGLSNIAFNCMVLGT---LFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18545 222 ----LNALFWPLVELISALGTalvYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
455-698 |
2.87e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 108.69 E-value: 2.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPGFeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 534
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR-KHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEP--VLFGTTIMENIRFG---KLAASDE---EVYAAAREANAHEFITSFPEgyntivgergtTLSGGQKQRLAIA 606
Cdd:PRK13648 86 GIVFQNPdnQFVGSIVKYDVAFGlenHAVPYDEmhrRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 607 RALIKQPTVLILDEATSALDAESERVVQEALDRASAGR--TVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGG 684
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
250
....*....|....
gi 109068902 685 LYAELirrqALDAP 698
Cdd:PRK13648 235 ELTRI----GLDLP 244
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
455-670 |
3.99e-26 |
|
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: 106.72 E-value: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRg 531
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 532 QVVGFISQEPVLFGT-TIMENIRF--------GKLAAsdEEVYAAAREANAHEFITSFPEGyntivgergttLSGGQKQR 602
Cdd:cd03292 78 RKIGVVFQDFRLLPDrNVYENVAFalevtgvpPREIR--KRVPAALELVGLSHKHRALPAE-----------LSGGEQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 603 LAIARALIKQPTVLILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLSTV-RGAHRIIVMADGRV 670
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkAGTTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
470-711 |
4.00e-26 |
|
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: 113.24 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 470 FEVLKDFTLTLPPGKIVALVGQSGGGKT----TVASLLERFYDPTAGVVMLDGRDLRTLDPSWL---RGQVVGFISQEPV 542
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELrriRGNRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 -----LF--GTTIMENIRFgKLAASDEEVYAAAREA-------NAHEFITSFP-EgyntivgergttLSGGQKQRLAIAR 607
Cdd:COG4172 103 tslnpLHtiGKQIAEVLRL-HRGLSGAAARARALELlervgipDPERRLDAYPhQ------------LSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 608 ALIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELL 680
Cdd:COG4172 170 ALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAELF 245
|
250 260 270
....*....|....*....|....*....|..
gi 109068902 681 KK-GGLYAelirRQALDAPRTVAPPPKKPEGP 711
Cdd:COG4172 246 AApQHPYT----RKLLAAEPRGDPRPVPPDAP 273
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
455-662 |
5.26e-26 |
|
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: 106.02 E-value: 5.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLErfydPTAGVVMLDGRDLRTLDPSWLR 530
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 531 gqVVGFISQEPVLFGT-TIMENIRF----GKLAASDEEVYAAAREANAHEFItsfpegyNTIVGergtTLSGGQKQRLAI 605
Cdd:COG4133 76 --RLAYLGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVAL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 606 ARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRGAHRI 662
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
471-679 |
7.53e-26 |
|
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: 106.46 E-value: 7.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGT-TIM 549
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVPQGREIFPRlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 550 ENIRFGkLAAsdeevyAAAREANAHEFITS-FPEgYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD-- 626
Cdd:TIGR03410 94 ENLLTG-LAA------LPRRSRKIPDEIYElFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQps 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 627 --AESERVVQEAldRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEEL 679
Cdd:TIGR03410 166 iiKDIGRVIRRL--RAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
455-680 |
1.07e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 106.33 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGrdLRTLDPS----WLR 530
Cdd:PRK09493 2 IEFKNVSKHFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKvderLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 531 gQVVGFISQEPVLF-GTTIMENIRFGKL---AASDEEVYAAAREANAHefitsfpegyntiVG--ERG----TTLSGGQK 600
Cdd:PRK09493 77 -QEAGMVFQQFYLFpHLTALENVMFGPLrvrGASKEEAEKQARELLAK-------------VGlaERAhhypSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 601 QRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEE 678
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222
|
..
gi 109068902 679 LL 680
Cdd:PRK09493 223 LI 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
459-670 |
1.29e-25 |
|
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: 105.35 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 459 NVCFSYPCRpgfEVLKDFTLTLPPGkIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVVGFIS 538
Cdd:cd03264 5 NLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLR-RRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 539 QEPVLF-GTTIMENIRFgkLAA----SDEEVYAAAREANAHEfitsfpeGYNTIVGERGTTLSGGQKQRLAIARALIKQP 613
Cdd:cd03264 79 QEFGVYpNFTVREFLDY--IAWlkgiPSKEVKARVDEVLELV-------NLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 614 TVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRV 670
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKL 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
455-700 |
1.31e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.12 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGrDLRTLDPSWLRGQVV 534
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEP--VLFGTTIMENIRFG------KLAASDEEVYAAAREANAHEFITSFPegyntivgergTTLSGGQKQRLAIA 606
Cdd:PRK13650 84 GMVFQNPdnQFVGATVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 607 RALIKQPTVLILDEATSALDAESE----RVVQEAldRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKK 682
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRleliKTIKGI--RDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
250
....*....|....*...
gi 109068902 683 GGLYAELirrqALDAPRT 700
Cdd:PRK13650 231 GNDLLQL----GLDIPFT 244
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
455-674 |
1.80e-25 |
|
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: 104.64 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqvV 534
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRD--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVLF-GTTIMENIRFG-KLAAS-----DEEVYAAAREANAHEFITSFPegyntivgergTTLSGGQKQRLAIAR 607
Cdd:cd03301 75 AMVFQNYALYpHMTVYDNIAFGlKLRKVpkdeiDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 608 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH-RLSTVRGAHRIIVMADGRVWEAG 674
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
472-639 |
2.05e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.18 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLErfydPTAGVVMLDGRDLRTLDPSWLRGQvVGFISQEPVLFGTT 547
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTllkiVASLIS----PTSGTLLFEGEDISTLKPEIYRQQ-VSYCAQTPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 548 IMENIRFG---KLAASDEEVYAAareanaheFITSF--PEgynTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 622
Cdd:PRK10247 97 VYDNLIFPwqiRNQQPDPAIFLD--------DLERFalPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170
....*....|....*..
gi 109068902 623 SALDAESERVVQEALDR 639
Cdd:PRK10247 166 SALDESNKHNVNEIIHR 182
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
471-678 |
2.66e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 108.50 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlRGQVVGFISQEPVLF-GTTIM 549
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA---ENRHVNTVFQSYALFpHMTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 550 ENIRFG----KLAASD--EEVYAAAREANAHEFITSFPegyntivgergTTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:PRK09452 105 ENVAFGlrmqKTPAAEitPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 624 ALDAESERVVQ---EALDRaSAGRTVLVIAH----RLSTvrgAHRIIVMADGRVWEAGTHEE 678
Cdd:PRK09452 174 ALDYKLRKQMQnelKALQR-KLGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPRE 231
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
181-398 |
2.71e-25 |
|
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: 106.77 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 181 LLILYGVQGLLTFgYLVLLSHI-GERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQE------------FKS 247
Cdd:cd18549 48 LLALYILRTLLNY-FVTYWGHVmGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDiselahhgpedlFIS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 248 SFKLVisqglrsctqvaGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTV 327
Cdd:cd18549 127 IITII------------GSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVV 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 328 RAFAMEQREEERYGAELEACRcRAEELG-RGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL 398
Cdd:cd18549 195 KAFANEEYEIEKFDEGNDRFL-ESKKKAyKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFL 265
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
131-397 |
2.91e-25 |
|
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: 106.41 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 131 LGVAIVLALGAALVNVQIPLLLGQLVEivakytrdhVGSFMTESRKLSTHLLILYGV---QGLLTFGYLVLLSHIGERMA 207
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIID---------DALPQGDLGLLVLLALGMVAVavaSALLGVVQTYLSARIGQGVM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 208 VDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPA 287
Cdd:cd18550 72 YDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 288 LMGVGTLMGSGLRKLSRQCQEQIARAMGVADEAL--GNVRTVRAFAMEQREEERYGAELEACR---CRAEELGRgiALFQ 362
Cdd:cd18550 152 FVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARRSRELRdlgVRQALAGR--WFFA 229
|
250 260 270
....*....|....*....|....*....|....*
gi 109068902 363 GLSnIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSF 397
Cdd:cd18550 230 ALG-LFTAIGPALVYWVGGLLVIGGGLTIGTLVAF 263
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
455-698 |
3.16e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.04 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTA---GVVMLDGRDLrTLDPSWLRG 531
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITL-TAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 532 QVVGFISQEP--VLFGTTIMENIRFG--KLAASDEEVYAAAREANAH----EFITSFPEgyntivgergtTLSGGQKQRL 603
Cdd:PRK13640 84 EKVGIVFQNPdnQFVGATVGDDVAFGleNRAVPRPEMIKIVRDVLADvgmlDYIDSEPA-----------NLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 604 AIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLK 681
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
250
....*....|....*..
gi 109068902 682 KgglyAELIRRQALDAP 698
Cdd:PRK13640 233 K----VEMLKEIGLDIP 245
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
458-675 |
4.88e-25 |
|
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: 104.05 E-value: 4.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASL---LERfydPTAGVVMLDGRDLRTLDP---SWLR 530
Cdd:COG4181 12 RGLTKTVGTGAGeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDEdarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 531 GQVVGFISQEPVLFGT-TIMENIRFGKLAASDEEVYAAAREANAHefitsfpegyntiVG--ERGT----TLSGGQKQRL 603
Cdd:COG4181 89 ARHVGFVFQSFQLLPTlTALENVMLPLELAGRRDARARARALLER-------------VGlgHRLDhypaQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 604 AIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGT 675
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
455-699 |
9.06e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.78 E-value: 9.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPGFE---VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG 531
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 532 QVVGFISQEP--VLFGTTIMENIRFG--KLAASDEEVYAAAREA----NAHEFITSFPEgyntivgergtTLSGGQKQRL 603
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGpeNLGIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 604 AIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLK 681
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
250
....*....|....*...
gi 109068902 682 KgglyAELIRRQALDAPR 699
Cdd:PRK13633 234 E----VEMMKKIGLDVPQ 247
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
388-672 |
9.85e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.13 E-value: 9.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 388 QLTGGDLMsflvasQTVQrsmanlsvLFGQVVRGLS-------------AGA-RVFEYM-ALSPCIPLSGGCCIPKEHLR 452
Cdd:COG4178 295 EITLGGLM------QAAS--------AFGQVQGALSwfvdnyqslaewrATVdRLAGFEeALEAADALPEAASRIETSED 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 453 GSVTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLlerfYDPTAGVVMLDgRDLRTLdpsw 528
Cdd:COG4178 361 GALALEDLTLRTP--DGRPLLEDLSLSLKPGERLLITGPSGSGKSTllraIAGL----WPYGSGRIARP-AGARVL---- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 529 lrgqvvgFISQEPVLFGTTIMENIRFGKLAA--SDEEVYAAAREANAHEFITSFPEGYNtivgeRGTTLSGGQKQRLAIA 606
Cdd:COG4178 430 -------FLPQRPYLPLGTLREALLYPATAEafSDAELREALEAVGLGHLAERLDEEAD-----WDQVLSLGEQQRLAFA 497
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 607 RALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWE 672
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQ 563
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
468-668 |
1.02e-24 |
|
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: 102.79 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQ---VVGFISQEPVLF 544
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrySVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 545 GTTIMENIRFGklAASDEEVYAAAREA-NAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:cd03290 92 NATVEENITFG--SPFNKQRYKAVTDAcSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 109068902 624 ALDAE-SERVVQEALDR--ASAGRTVLVIAHRLSTVRGAHRIIVMADG 668
Cdd:cd03290 170 ALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
458-690 |
1.04e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.43 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYpcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFI 537
Cdd:PRK13647 8 EDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV-GLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 538 SQEP--VLFGTTIMENIRFG----KLAAS--DEEVYAAAREANAHEFITSFPegYNtivgergttLSGGQKQRLAIARAL 609
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAFGpvnmGLDKDevERRVEEALKAVRMWDFRDKPP--YH---------LSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 610 IKQPTVLILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLS-TVRGAHRIIVMADGRVWEAG-----THEELLKK 682
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHnQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQ 233
|
....*...
gi 109068902 683 GGLYAELI 690
Cdd:PRK13647 234 AGLRLPLV 241
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
459-679 |
1.10e-24 |
|
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: 104.55 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 459 NVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswlrgqvVGFIS 538
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 539 QEPVLFGTTIMENIRFGklAASDEEVYAAAREA-NAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLI 617
Cdd:cd03291 105 QFSWIMPGTIKENIIFG--VSYDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109068902 618 LDEATSALDAESERVVQEA-LDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEEL 679
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
454-699 |
1.10e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 104.74 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYPCRPGFE--VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDL--RTLDPSWL 529
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 530 RGQVvGFISQEP--VLFGTTIMENIRFG--KLAASDEEVYAAAREANAhefITSFPegYNTIVGERGTTLSGGQKQRLAI 605
Cdd:PRK13637 82 RKKV-GLVFQYPeyQLFEETIEKDIAFGpiNLGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 606 ARALIKQPTVLILDEATSALDAESErvvQEALDRASA-----GRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEEL 679
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGR---DEILNKIKElhkeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREV 232
|
250 260
....*....|....*....|
gi 109068902 680 LKKgglyAELIRRQALDAPR 699
Cdd:PRK13637 233 FKE----VETLESIGLAVPQ 248
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
454-677 |
1.31e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLERfydPTAGVVMLDGRDL---RTLDPS 527
Cdd:COG4161 2 SIQLKNINCFYG---SHQALFDINLECPSGETLVLLGPSGAGKSSllrVLNLLET---PDSGQLNIAGHQFdfsQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 528 WLRG--QVVGFISQE----PVLfgtTIMEN-----IRFGKLAASdeevyAAAREANAH-------EFITSFPegyntivg 589
Cdd:COG4161 76 AIRLlrQKVGMVFQQynlwPHL---TVMENlieapCKVLGLSKE-----QAREKAMKLlarlrltDKADRFP-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 590 ergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIVMAD 667
Cdd:COG4161 140 ---LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEK 216
|
250
....*....|
gi 109068902 668 GRVWEAGTHE 677
Cdd:COG4161 217 GRIIEQGDAS 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
456-670 |
1.48e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.40 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 456 TFQNVCFSYP-CRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTldPSWLRGqVV 534
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADRG-VV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 gFisQEPVLFG-TTIMENIRFG-KLAAsdeeVYAAAREANAHEFITsfpegyntIVGERGT------TLSGGQKQRLAIA 606
Cdd:COG4525 82 -F--QKDALLPwLNVLDNVAFGlRLRG----VPKAERRARAEELLA--------LVGLADFarrriwQLSGGMRQRVGIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 607 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHR------LSTvrgahRIIVMAD--GRV 670
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITHSveealfLAT-----RLVVMSPgpGRI 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
459-699 |
1.50e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.00 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 459 NVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG-QVVGFI 537
Cdd:PRK13639 6 DLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVrKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 538 SQEP--VLFGTTIMENIRFG--KLAASDEEVYAAAREANAHEFItsfpEGYNTIVGERgttLSGGQKQRLAIARALIKQP 613
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEALKAVGM----EGFENKPPHH---LSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 614 TVLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEELLKKgglyAELIR 691
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSD----IETIR 232
|
....*...
gi 109068902 692 RQALDAPR 699
Cdd:PRK13639 233 KANLRLPR 240
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
473-670 |
3.07e-24 |
|
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: 101.22 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 473 LKDFTLTLP---PGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDL----RTLD-PSWLRGqvVGFISQEPVLF 544
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINlPPQQRK--IGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 545 -GTTIMENIRFGKLAASDEEvyaaaREANAHEFITSFpeGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:cd03297 88 pHLNVRENLAFGLKRKRNRE-----DRISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 109068902 624 ALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RGAHRIIVMADGRV 670
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRL 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
469-680 |
3.63e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.14 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVV-----MLDG-----------RDLRtldpswlrgQ 532
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTarslsqqkgliRQLR---------Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 533 VVGFISQEPVLF-GTTIMENIRFGKLAASDE---EVYAAAREANAHEFITSFPEGYNTivgergtTLSGGQKQRLAIARA 608
Cdd:PRK11264 86 HVGFVFQNFNLFpHRTVLENIIEGPVIVKGEpkeEATARARELLAKVGLAGKETSYPR-------RLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 609 LIKQPTVLILDEATSALDAEserVVQEALDR----ASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELL 680
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
450-669 |
4.06e-24 |
|
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: 101.36 E-value: 4.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 450 HLRGSVTFQnvcfsypcrpgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGR----DLRTLD 525
Cdd:COG4778 17 HLQGGKRLP-------------VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 526 PS---WLRGQVVGFISQ---------------EPVLfgttimenirfgKLAASDEEVYAAAREANAHefitsfpegYNti 587
Cdd:COG4778 84 PReilALRRRTIGYVSQflrviprvsaldvvaEPLL------------ERGVDREEARARARELLAR---------LN-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 588 VGER-----GTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRG-AH 660
Cdd:COG4778 141 LPERlwdlpPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAvAD 220
|
....*....
gi 109068902 661 RIIVMADGR 669
Cdd:COG4778 221 RVVDVTPFS 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
458-698 |
4.14e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.86 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrTLDPSWLRGQVVGFI 537
Cdd:PRK13642 8 ENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL-TAENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 538 SQEP--VLFGTTIMENIRFG--KLAASDEEVYAAAREA----NAHEFITSFPegyntivgergTTLSGGQKQRLAIARAL 609
Cdd:PRK13642 87 FQNPdnQFVGATVEDDVAFGmeNQGIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 610 IKQPTVLILDEATSALD----AESERVVQEALDRASAgrTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGL 685
Cdd:PRK13642 156 ALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSED 233
|
250
....*....|...
gi 109068902 686 YAELirrqALDAP 698
Cdd:PRK13642 234 MVEI----GLDVP 242
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
471-673 |
5.38e-24 |
|
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: 100.37 E-value: 5.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWlrgQVVGFISQEPVLFGT-TIM 549
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL---RRIGALIEAPGFYPNlTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 550 ENIRFGKLaasdeevYAAAREANAHEFITsfpegyntIVGERGT------TLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:cd03268 91 ENLRLLAR-------LLGIRKKRIDEVLD--------VVGLKDSakkkvkGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 109068902 624 ALDAESERVVQEAL-DRASAGRTVLVIAHRLSTVRG-AHRIIVMADGR-VWEA 673
Cdd:cd03268 156 GLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKlIEEG 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
458-670 |
6.08e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 107.12 E-value: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP---SWLRGQV 533
Cdd:PRK10535 8 KDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalAQLRREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 VGFISQE-PVLFGTTIMENIRFGKLAASDEEvyaAAREANAHEFITSFpeGYNTIVGERGTTLSGGQKQRLAIARALIKQ 612
Cdd:PRK10535 88 FGFIFQRyHLLSHLTAAQNVEVPAVYAGLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 613 PTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRGAHRIIVMADGRV 670
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
453-690 |
7.11e-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: 101.85 E-value: 7.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 453 GSVTFQNVCFSYpCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDpTAGVVMLDGRDLRTLDPSWLRgQ 532
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWR-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 533 VVGFISQEPVLFGTTIMENIR-FGKLaaSDEEVYAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIK 611
Cdd:cd03289 78 AFGVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 612 QPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAELI 690
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
181-398 |
1.69e-23 |
|
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: 101.41 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 181 LLILYGVQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:cd18546 45 YLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 261 TQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERY 340
Cdd:cd18546 125 LTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERF 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 341 GAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL 398
Cdd:cd18546 205 AELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFL 262
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
472-692 |
2.20e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.09 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGTTIMEN 551
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 552 IR---------FGKLAASDEEVYAAAREANahefitsfpeGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 622
Cdd:PRK11231 97 VAygrspwlslWGRLSAEDNARVNQAMEQT----------RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 623 SALD----AESERVVQEaldRASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEELLKkgglyAELIRR 692
Cdd:PRK11231 167 TYLDinhqVELMRLMRE---LNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMT-----PGLLRT 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
471-670 |
3.44e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 98.73 E-value: 3.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSW---LRGQVVGFISQ-EPVLFGT 546
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQKLGFIYQfHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 TIMENIRFGKLAASDEEVYAAAReanAHEFITSFpeGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 626
Cdd:PRK11629 103 TALENVAMPLLIGKKKPAEINSR---ALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 109068902 627 AESERVVQEALDR--ASAGRTVLVIAHRLSTVRGAHRIIVMADGRV 670
Cdd:PRK11629 178 ARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
464-679 |
4.13e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 100.81 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 464 YPCRPGF-------EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRGQV 533
Cdd:PRK11308 15 YPVKRGLfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 ----------------VGFISQEPVLFGTTIMenirfgklaasdeevyAAAREANAHEFITSF---PEGYntivGERGTT 594
Cdd:PRK11308 95 qivfqnpygslnprkkVGQILEEPLLINTSLS----------------AAERREKALAMMAKVglrPEHY----DRYPHM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 595 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVV-------QEALdrasaGRTVLVIAHRLSTVRG-AHRIIVMA 666
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVlnlmmdlQQEL-----GLSYVFISHDLSVVEHiADEVMVMY 229
|
250
....*....|...
gi 109068902 667 DGRVWEAGTHEEL 679
Cdd:PRK11308 230 LGRCVEKGTKEQI 242
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
470-670 |
4.54e-23 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 98.21 E-value: 4.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVVGFISQEPVLFG-TTI 548
Cdd:cd03266 18 VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEAR-RRLGFVSDSTGLYDrLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 549 MENIR-FGKLAAsdeeVYAAAREANAHEFITSFpeGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDA 627
Cdd:cd03266 96 RENLEyFAGLYG----LKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 109068902 628 ESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHRIIVMADGRV 670
Cdd:cd03266 170 MATRALREFIRQlRALGKCILFSTHIMQEVeRLCDRVVVLHRGRV 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
472-715 |
4.92e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.23 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLrGQVVGFISQEPVL-FGTTIME 550
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA-SRRVASVPQDTSLsFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 551 NIRFGK------LAASDEEVYAAAREANAHEFITSFpegyntiVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 624
Cdd:PRK09536 97 VVEMGRtphrsrFDTWTETDRAAVERAMERTGVAQF-------ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 625 LDAESE-RVVQEALDRASAGRTVLVIAHRLS-TVRGAHRIIVMADGRVWEAGTHEELLKKGGLYAELIRRQAL------D 696
Cdd:PRK09536 170 LDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAVgtdpatG 249
|
250
....*....|....*....
gi 109068902 697 APRTVAPPPKKPEGPRSQQ 715
Cdd:PRK09536 250 APTVTPLPDPDRTEAAADT 268
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
476-680 |
5.68e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.12 E-value: 5.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 476 FTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlrGQVVGFISQEPVLFG-TTIMENIRF 554
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS---RRPVSMLFQENNLFShLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 555 G-----KL-AASDEEVYAAAREANAHEFITSFPegyntivgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALD-- 626
Cdd:PRK10771 95 GlnpglKLnAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 627 --AESERVVQEALDRASAgrTVLVIAHRLS-TVRGAHRIIVMADGRVWEAGTHEELL 680
Cdd:PRK10771 164 lrQEMLTLVSQVCQERQL--TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
458-680 |
1.47e-22 |
|
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: 96.84 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrTLDPSWLRGQV-VGF 536
Cdd:cd03218 4 ENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMHKRARLgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 537 ISQEPVLF-GTTIMENIRfgkLAASDEEVYAAAREANAHEFITSFpeGYNTIVGERGTTLSGGQKQRLAIARALIKQPTV 615
Cdd:cd03218 80 LPQEASIFrKLTVEENIL---AVLEIRGLSKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 616 LILDEATSALD----AESERVVQEALDRasaGRTVLVIAHRLS-TVRGAHRIIVMADGRVWEAGTHEELL 680
Cdd:cd03218 155 LLLDEPFAGVDpiavQDIQKIIKILKDR---GIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
473-680 |
1.50e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.49 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 473 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG---QVVGFISQEPVLF-GTTI 548
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrKKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 549 MENIRFGK----LAASD--EEVYAAAREANAHEFITSFPEgyntivgergtTLSGGQKQRLAIARALIKQPTVLILDEAT 622
Cdd:PRK10070 124 LDNTAFGMelagINAEErrEKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109068902 623 SALDAESERVVQEALDRASAG--RTVLVIAHRL-STVRGAHRIIVMADGRVWEAGTHEELL 680
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
473-685 |
1.70e-22 |
|
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: 99.80 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 473 LKDFTL----TLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRT------LDPSWLRgqvVGFISQEPV 542
Cdd:TIGR02142 9 LGDFSLdadfTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRR---IGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 LFG-TTIMENIRFGKLAASDEevYAAAREANAHEFItsfpeGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:TIGR02142 86 LFPhLSVRGNLRYGMKRARPS--ERRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 622 TSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEELLKKGGL 685
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
472-674 |
2.09e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 95.81 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDpswlrGQVVGFISQEPVLF-GTTIME 550
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRIGYLPEERGLYpKMKVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 551 NIR-FGKLAASDEEvyAAAREANahEFITSFP-EGYNTIVGErgtTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE 628
Cdd:cd03269 90 QLVyLAQLKGLKKE--EARRRID--EWLERLElSEYANKRVE---ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 109068902 629 SERVVQEAL-DRASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAG 674
Cdd:cd03269 163 NVELLKDVIrELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
468-677 |
2.13e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 101.26 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGT- 546
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGMVHQHFMLVPNl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 TIMENIRFG----KLAASDeevYAAAREAnahefITSFPEGY------NTIVGErgttLSGGQKQRLAIARALIKQPTVL 616
Cdd:COG3845 96 TVAENIVLGleptKGGRLD---RKAARAR-----IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 617 ILDEATSAL-DAESERVVqEALDR-ASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVweAGTHE 677
Cdd:COG3845 164 ILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVMAiADRVTVLRRGKV--VGTVD 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
469-679 |
3.60e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.14 E-value: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGqvVGFISQEPVLF-GTT 547
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-PPYQRP--INMMFQSYALFpHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 548 IMENIRFG----KLAASdeEVYAAARE----ANAHEFITSFPEgyntivgergtTLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:PRK11607 108 VEQNIAFGlkqdKLPKA--EIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109068902 620 EATSALDAE-SERVVQEALD-RASAGRTVLVIAH-RLSTVRGAHRIIVMADGRVWEAGTHEEL 679
Cdd:PRK11607 175 EPMGALDKKlRDRMQLEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
455-670 |
4.11e-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: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLdGRDLRtldpswlrgqvV 534
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVLF--GTTIMENIRfgklaasdeEVYAAAREANAHEFITSF---PEGYNTIVGergtTLSGGQKQRLAIARAL 609
Cdd:COG0488 381 GYFDQHQEELdpDKTVLDELR---------DGAPGGTEQEVRGYLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 610 IKQPTVLILDEATSALDAESERVVQEALDrASAGrTVLVIAH-R--LSTVrgAHRIIVMADGRV 670
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGV 507
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
455-680 |
5.20e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.92 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP-------S 527
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelakrlA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 528 WLRgQVVGFIS----QEPVLFGttimeniRF----GKLAASDEEVYAAA-----REANAHEFITsfpegyntivgergtT 594
Cdd:COG4604 79 ILR-QENHINSrltvRELVAFG-------RFpyskGRLTAEDREIIDEAiayldLEDLADRYLD---------------E 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 595 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAS--AGRTVLVIAHRLS-TVRGAHRIIVMADGRVW 671
Cdd:COG4604 136 LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINfASCYADHIVAMKDGRVV 215
|
....*....
gi 109068902 672 EAGTHEELL 680
Cdd:COG4604 216 AQGTPEEII 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
448-674 |
5.98e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 94.91 E-value: 5.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 448 KEHLRGSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldPS 527
Cdd:cd03220 13 YKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 528 WLRGQVVGFisqEPVLfgtTIMENIRF-----GKLAASDEEVYaaareanahEFITSFPEgyntiVGERGT----TLSGG 598
Cdd:cd03220 87 SLLGLGGGF---NPEL---TGRENIYLngrllGLSRKEIDEKI---------DEIIEFSE-----LGDFIDlpvkTYSSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 599 QKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAG 674
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
458-699 |
1.13e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.68 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrTLDPSW-----LRgQ 532
Cdd:PRK13636 9 EELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK---PIDYSRkglmkLR-E 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 533 VVGFISQEP--VLFGTTIMENIRFG--KLAASDEEVYAAAREANAHEfitsfpeGYNTIVGERGTTLSGGQKQRLAIARA 608
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRT-------GIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 609 LIKQPTVLILDEATSALD----AESERVVQEALDraSAGRTVLVIAHRLSTVR-GAHRIIVMADGRVWEAGTHEELLKKg 683
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQK--ELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE- 232
|
250
....*....|....*.
gi 109068902 684 glyAELIRRQALDAPR 699
Cdd:PRK13636 233 ---KEMLRKVNLRLPR 245
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
467-694 |
1.35e-21 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 97.09 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 467 RPGFEVlkDFTLTLPPGKIVALVGQSGGGKTTVASL---LERfydPTAGVVMLDGRDLrtLD-------PSWLRGqvVGF 536
Cdd:COG4148 11 RGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVL--QDsargiflPPHRRR--IGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 537 ISQEPVLFGT-TIMENIRFGklaasdeevYAAAREANAHEfitSFPE-----GYNTIVGERGTTLSGGQKQRLAIARALI 610
Cdd:COG4148 82 VFQEARLFPHlSVRGNLLYG---------RKRAPRAERRI---SFDEvvellGIGHLLDRRPATLSGGERQRVAIGRALL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 611 KQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEELLKKGGLYA 687
Cdd:COG4148 150 SSPRLLLMDEPLAALDLARKAEILPYLERlrDELDIPILYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLSRPDLLP 229
|
....*..
gi 109068902 688 ELIRRQA 694
Cdd:COG4148 230 LAGGEEA 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
456-651 |
1.35e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.77 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 456 TFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlRTLDPSWLRGQVvg 535
Cdd:PRK11248 3 QISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK--PVEGPGAERGVV-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 536 fISQEPVLFGTTIMENIRFG-KLAAsdeeVYAAAREANAHEFITSFP-EGYNTivgERGTTLSGGQKQRLAIARALIKQP 613
Cdd:PRK11248 76 -FQNEGLLPWRNVQDNVAFGlQLAG----VEKMQRLEIAHQMLKKVGlEGAEK---RYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 109068902 614 TVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH 651
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
455-680 |
1.38e-21 |
|
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: 94.77 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAG-VVMLDGRDLRTLDPSWLRGQV 533
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 vGFIS---QEPVLFGTTIMENI---RFGKLAASDEevYAAAREANAHEFITSFpeGYNTIVGERGTTLSGGQKQRLAIAR 607
Cdd:COG1119 81 -GLVSpalQLRFPRDETVLDVVlsgFFDSIGLYRE--PTDEQRERARELLELL--GLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 608 ALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLV-IAHRLSTV-RGAHRIIVMADGRVWEAGTHEELL 680
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIpPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
471-679 |
1.45e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.69 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlRGQVVGFISQEPVLF-GTTIM 549
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDRKVGFVFQHYALFrHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 550 ENIRFG----------KLAASDEEVYAAAREANAHEFITSFPegyntivgergTTLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:PRK10851 93 DNIAFGltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 620 EATSALDAESE-------RVVQEALDRASagrtVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEEL 679
Cdd:PRK10851 162 EPFGALDAQVRkelrrwlRQLHEELKFTS----VFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
454-677 |
1.71e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 94.31 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYPCRpgfEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLE-----------RFYDPTAGVVMLDGR 519
Cdd:PRK11124 2 SIQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLEmprsgtlniagNHFDFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 520 DLRtldpswlrgQVVGFISQE----PVLfgtTIMEN-----IRFgkLAASDEEVYAAAREANAH----EFITSFPegynt 586
Cdd:PRK11124 79 ELR---------RNVGMVFQQynlwPHL---TVQQNlieapCRV--LGLSKDQALARAEKLLERlrlkPYADRFP----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 587 ivgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIV 664
Cdd:PRK11124 140 ------LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVY 213
|
250
....*....|...
gi 109068902 665 MADGRVWEAGTHE 677
Cdd:PRK11124 214 MENGHIVEQGDAS 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
471-651 |
2.40e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.82 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD--PTA---GVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFG 545
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRRV-QMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 546 T-TIMENIRFG----KLAASDEEVYAAAREAnaHEFITSFPEGYNTIVGERGTtLSGGQKQRLAIARALIKQPTVLILDE 620
Cdd:PRK14247 96 NlSIFENVALGlklnRLVKSKKELQERVRWA--LEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190
....*....|....*....|....*....|.
gi 109068902 621 ATSALDAESERVVQEALDRASAGRTVLVIAH 651
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
466-681 |
2.78e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 98.58 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 466 CRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLErFYDPT----AGVVMLDGRdlrTLDPSWLRgQVVGFISQEP 541
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGM---PIDAKEMR-AISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 542 VLFGT-TIMENIRFGKLAASDEEVYAAAREANAHEFIT--SFPEGYNTIVGERGTT--LSGGQKQRLAIARALIKQPTVL 616
Cdd:TIGR00955 109 LFIPTlTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 617 ILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLST--VRGAHRIIVMADGRVWEAGTHEELLK 681
Cdd:TIGR00955 189 FCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
467-680 |
3.30e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 93.75 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWlRGQVVGFISQEPvlfGT 546
Cdd:COG4167 23 RQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RCKHIRMIFQDP---NT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 TIMENIRFGKLAasDE------EVYAAAREANAHEFITS---FPEGYNTivgeRGTTLSGGQKQRLAIARALIKQPTVLI 617
Cdd:COG4167 99 SLNPRLNIGQIL--EEplrlntDLTAEEREERIFATLRLvglLPEHANF----YPHMLSSGQKQRVALARALILQPKIII 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 618 LDEATSALDAeSERV--------VQEALdrasaGRTVLVIAHRLSTVRgaH---RIIVMADGRVWEAGTHEELL 680
Cdd:COG4167 173 ADEALAALDM-SVRSqiinlmleLQEKL-----GISYIYVSQHLGIVK--HisdKVLVMHQGEVVEYGKTAEVF 238
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
209-690 |
3.87e-21 |
|
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: 99.21 E-value: 3.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 209 DMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRL---TLLLMVAT 285
Cdd:TIGR01271 959 RLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIfiaAIPVAVIF 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 286 PALMGVGTLMGSGLRKLSRQCQEQIARAMGVAdeaLGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLS 365
Cdd:TIGR01271 1039 IMLRAYFLRTSQQLKQLESEARSPIFSHLITS---LKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRI 1115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 366 NIAFNCMVLGTLFIG-GSLVAGQQLTGGDLMSFLVASQTVQRSMaNLSVLFGQVVRGLSagaRVFEYMALSPCIP----- 439
Cdd:TIGR01271 1116 DIIFVFFFIAVTFIAiGTNQDGEGEVGIILTLAMNILSTLQWAV-NSSIDVDGLMRSVS---RVFKFIDLPQEEPrpsgg 1191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 440 -----LSGGCCIPKEHLR------GSVTFQNVCFSYpCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD 508
Cdd:TIGR01271 1192 ggkyqLSTVLVIENPHAQkcwpsgGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS 1270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 509 pTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENI----RFgklaaSDEEVYAAAREANAHEFITSFPEGY 584
Cdd:TIGR01271 1271 -TEGEIQIDGVSWNSVTLQTWR-KAFGVIPQKVFIFSGTFRKNLdpyeQW-----SDEEIWKVAEEVGLKSVIEQFPDKL 1343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 585 NTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIV 664
Cdd:TIGR01271 1344 DFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLV 1423
|
490 500
....*....|....*....|....*.
gi 109068902 665 MADGRVWEAGTHEELLKKGGLYAELI 690
Cdd:TIGR01271 1424 IEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
469-683 |
3.88e-21 |
|
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: 91.82 E-value: 3.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF--YDPTAGVVMLDGRDLRTLDPS--WLRGQVVGFisQEPVLF 544
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEerARLGIFLAF--QYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 545 -GTTIMENIRFgklaasdeevyaaareanahefitsfpegyntiVGErgtTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:cd03217 90 pGVKNADFLRY---------------------------------VNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 624 ALDAESERVVQEALDR-ASAGRTVLVIAH--RLSTVRGAHRIIVMADGRVWEAGTHE---ELLKKG 683
Cdd:cd03217 134 GLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElalEIEKKG 199
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
454-682 |
4.66e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.04 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYPCRPGFE--VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTL----DPS 527
Cdd:PRK13649 2 GINLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 528 WLRGQVvGFISQ--EPVLFGTTIMENIRFG--KLAASDEEVYAAAREANAHEFITsfpegyNTIVGERGTTLSGGQKQRL 603
Cdd:PRK13649 82 QIRKKV-GLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 604 AIARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELLK 681
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQ 234
|
.
gi 109068902 682 K 682
Cdd:PRK13649 235 D 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
469-679 |
5.52e-21 |
|
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: 92.05 E-value: 5.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVVGFISQEPVL-FGTT 547
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVR-RRIGIVFQDLSVdDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 548 IMENIR-FGKLAASDEEVyAAAREANAHEFItSFPEGYNTIVGergtTLSGGQKQRLAIARALIKQPTVLILDEATSALD 626
Cdd:cd03265 90 GWENLYiHARLYGVPGAE-RRERIDELLDFV-GLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 627 AESERVVQEALDR--ASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEEL 679
Cdd:cd03265 164 PQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
470-653 |
6.09e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 93.31 E-value: 6.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD--PTA---GVVMLDGRDL--RTLDPSWLRGQVvGFISQEPV 542
Cdd:PRK14243 23 FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLyaPDVDPVEVRRRI-GMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 LFGTTIMENIRFGKLAAS-----DEEVYAAAREANAHEFITSfpegyntIVGERGTTLSGGQKQRLAIARALIKQPTVLI 617
Cdd:PRK14243 102 PFPKSIYDNIAYGARINGykgdmDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 109068902 618 LDEATSALDAESERVVQEALDRASAGRTVLVIAHRL 653
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
469-684 |
6.18e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.02 E-value: 6.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlrgQVVGFISQEPVLF-GTT 547
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR-----RRIGYLPEERGLYpKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 548 IMENIR-FGKLAASDEevyAAAREaNAHEFITSFPegyntiVGERGT----TLSGGQKQRLAIARALIKQPTVLILDEAT 622
Cdd:COG4152 88 VGEQLVyLARLKGLSK---AEAKR-RADEWLERLG------LGDRANkkveELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 623 SALDAESERVVQEAL-DRASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEELLKKGG 684
Cdd:COG4152 158 SGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
473-668 |
7.37e-21 |
|
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: 92.14 E-value: 7.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 473 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlRGQVVGFISQEPVLfgtTIMENI 552
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD--RMVVFQNYSLLPWL---TVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 553 rfgklAASDEEVYAAAREANAHEFItsfpEGYNTIVG------ERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 626
Cdd:TIGR01184 76 -----ALAVDRVLPDLSKSERRAIV----EEHIALVGlteaadKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 109068902 627 AESERVVQEALDR--ASAGRTVLVIAHRL-STVRGAHRIIVMADG 668
Cdd:TIGR01184 147 ALTRGNLQEELMQiwEEHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
472-670 |
7.60e-21 |
|
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: 90.57 E-value: 7.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEP----VLFGTT 547
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 548 IMENIRFGKLaasdeevyaaareanahefitsfpegyntivgergttLSGGQKQRLAIARALIKQPTVLILDEATSALDA 627
Cdd:cd03215 95 VAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 109068902 628 ESERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHRIIVMADGRV 670
Cdd:cd03215 138 GAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
472-682 |
8.32e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.40 E-value: 8.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTldpSWLRGQVVGFISQEPVLF-GTTIME 550
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRDICMVFQSYALFpHMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 551 NIRFG--KLAASDEEVYAAAREANAHEFITSFPEGYntiVGErgttLSGGQKQRLAIARALIKQPTVLILDEATSALDAE 628
Cdd:PRK11432 98 NVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRY---VDQ----ISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 629 SERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELLKK 682
Cdd:PRK11432 171 LRRSMREKIRelQQQFNITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
458-681 |
8.99e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.01 E-value: 8.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVasllerFY------DPTAGVVMLDGRDLrTLDPSWLRG 531
Cdd:COG1137 7 ENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDI-THLPMHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 532 QV-VGFISQEPVLF-GTTIMENIRfgkLAASDEEVYAAAREANAHEFITSFpeGYNTIVGERGTTLSGGQKQRLAIARAL 609
Cdd:COG1137 77 RLgIGYLPQEASIFrKLTVEDNIL---AVLELRKLSKKEREERLEELLEEF--GITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 610 IKQPTVLILDEATSALD----AESERVVQEALDRasaGRTVLVIAHRlstVRGAHRII----VMADGRVWEAGTHEELLK 681
Cdd:COG1137 152 ATNPKFILLDEPFAGVDpiavADIQKIIRHLKER---GIGVLITDHN---VRETLGICdrayIISEGKVLAEGTPEEILN 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
457-670 |
1.10e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.29 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 457 FQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDgrdlrtldpswlRGQVVGF 536
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------------KGLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 537 ISQEPVLF-GTTIMENIrfgklAASDEEVYAAAREANAHEFITSFPE-----------------GYN------TIVGERG 592
Cdd:COG0488 66 LPQEPPLDdDLTVLDTV-----LDGDAELRALEAELEELEAKLAEPDedlerlaelqeefealgGWEaearaeEILSGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 593 ----------TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAEServVQ--EALDRASAGrTVLVIAH-R--LSTVr 657
Cdd:COG0488 141 fpeedldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSHdRyfLDRV- 215
|
250
....*....|...
gi 109068902 658 gAHRIIVMADGRV 670
Cdd:COG0488 216 -ATRILELDRGKL 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
454-701 |
1.51e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.54 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYpcRPG----FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDL--RTLDpS 527
Cdd:PRK13646 2 TIRFDNVSYTY--QKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthKTKD-K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 528 WLRG--QVVGFISQ--EPVLFGTTIMENIRFG--KLAASDEEVyaaarEANAHEFITSFpeGYN-TIVGERGTTLSGGQK 600
Cdd:PRK13646 79 YIRPvrKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEV-----KNYAHRLLMDL--GFSrDVMSQSPFQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 601 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHE 677
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPK 231
|
250 260
....*....|....*....|....
gi 109068902 678 ELLKKGglyaELIRRQALDAPRTV 701
Cdd:PRK13646 232 ELFKDK----KKLADWHIGLPEIV 251
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
471-679 |
1.75e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.38 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD-----PTAGVVMLDGRDL--RTLDPSWLRGQVvGFISQEPVL 543
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEI-GMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 544 FGTTIMENIRFG-KLAA-SDEEVYAAAREANAHEfiTSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:PRK14239 98 FPMSIYENVVYGlRLKGiKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 622 TSALDAESERVVQEALDRASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEEL 679
Cdd:PRK14239 176 TSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
470-679 |
1.77e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.99 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLdgRDLRTLDPSWLRGQV---------------- 533
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELItnpyskkiknfkelrr 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 -VGFISQEP--VLFGTTIMENIRFGKLAASDEEVYAAAReanAHEFITSFPEGYNTIvgERGT-TLSGGQKQRLAIARAL 609
Cdd:PRK13631 117 rVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKL---AKFYLNKMGLDDSYL--ERSPfGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 610 IKQPTVLILDEATSALDAESER-VVQEALDRASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEEL 679
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
478-679 |
2.18e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 91.20 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 478 LTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWL---RGQVVGFisQEPVLFGT-TIMENIr 553
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQiarMGVVRTF--QHVRLFREmTVIENL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 554 fgkLAASDEEVYA----------AAR--EANAHEFITSFPE--GYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:PRK11300 102 ---LVAQHQQLKTglfsgllktpAFRraESEALDRAATWLErvGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109068902 620 EATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEEL 679
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
473-667 |
3.05e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.46 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 473 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDP---TAGVVMLDGRDLRTLdPSWLRGqvVGFISQEPVLFG-TTI 548
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAL-PAEQRR--IGILFQDDLLFPhLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 549 MENIRFG-----KLAASDEEVYAAAREANAHEFITSFPEgyntivgergtTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:COG4136 94 GENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 109068902 624 ALDAE-----SERVVQEAldRASAGRTVLViAHRLSTVRGAHRIIVMAD 667
Cdd:COG4136 163 KLDAAlraqfREFVFEQI--RQRGIPALLV-THDEEDAPAAGRVLDLGN 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
454-700 |
3.31e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.43 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYPCRPGFEV--LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrTLDPS---- 527
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI-TPETGnknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 528 -WLRGQVvGFISQ--EPVLFGTTIMENIRFG--KLAASDEEvyaaAREAnAHEFITSFpeGYNTIVGERGT-TLSGGQKQ 601
Cdd:PRK13641 81 kKLRKKV-SLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDE----AKEK-ALKWLKKV--GLSEDLISKSPfELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 602 RLAIARALIKQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEEL 679
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
250 260
....*....|....*....|.
gi 109068902 680 LKKgglyAELIRRQALDAPRT 700
Cdd:PRK13641 233 FSD----KEWLKKHYLDEPAT 249
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
467-672 |
3.47e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 90.90 E-value: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--QVVGFISQEPV-- 542
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrRDIQMVFQDSIsa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 -----LFGTTIMENIRfgKLAASDEevyaAAREANAHEFITSFpEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLI 617
Cdd:PRK10419 102 vnprkTVREIIREPLR--HLLSLDK----AERLARASEMLRAV-DLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 618 LDEATSALDaeseRVVQ-EALD-----RASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWE 672
Cdd:PRK10419 175 LDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
465-692 |
3.75e-20 |
|
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: 96.24 E-value: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 465 PC-RPGFEVLkdfTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRT-LDPswLRgQVVGFISQEPV 542
Cdd:TIGR01257 940 PSgRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETnLDA--VR-QSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 LFG-TTIMENIRF-GKLAASDEEVYAAAREANAHEfitsfpEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDE 620
Cdd:TIGR01257 1014 LFHhLTVAEHILFyAQLKGRSWEEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 621 ATSALDAESERVVQEALDRASAGRTVLVIAHRL--STVRGaHRIIVMADGRVWEAGTheELLKKG----GLYAELIRR 692
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdeADLLG-DRIAIISQGRLYCSGT--PLFLKNcfgtGFYLTLVRK 1162
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
471-711 |
3.86e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 96.00 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDgrdlrtldpswlrgQVVGFISQEPVLFGTTIME 550
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--------------RSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 551 NIRFgklaaSDEEvyAAAREANA------HEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 624
Cdd:PTZ00243 740 NILF-----FDEE--DAARLADAvrvsqlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 625 LDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELL------------------KKGGL 685
Cdd:PTZ00243 813 LDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMrtslyatlaaelkenkdsKEGDA 892
|
250 260
....*....|....*....|....*..
gi 109068902 686 YAELIRRQALDA-PRTVAPPPKKPEGP 711
Cdd:PTZ00243 893 DAEVAEVDAAPGgAVDHEPPVAKQEGN 919
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
472-672 |
1.35e-19 |
|
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: 89.09 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG-----QVVGFISQEPVLFGT 546
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrdvQLVFQDSPSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 TIMENIrfGKLAASDEEVYAAAREANAHEFITSFpEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 626
Cdd:TIGR02769 106 TVRQII--GEPLRHLTSLDESEQKARIAELLDMV-GLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 109068902 627 AESERVVQEALD--RASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWE 672
Cdd:TIGR02769 183 MVLQAVILELLRklQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
454-694 |
2.68e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.83 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYPCRPG-------------------FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVV 514
Cdd:COG1134 4 MIEVENVSKSYRLYHEpsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 515 MLDGRdlrtldPSWLRGQVVGFisqEPVLFGttiMENIRFGKLA--ASDEEVyaAAREanahEFITSFPEgyntiVGE-- 590
Cdd:COG1134 84 EVNGR------VSALLELGAGF---HPELTG---RENIYLNGRLlgLSRKEI--DEKF----DEIVEFAE-----LGDfi 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 591 ----RgtTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIV 664
Cdd:COG1134 141 dqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIW 218
|
250 260 270
....*....|....*....|....*....|
gi 109068902 665 MADGRVWEAGTHEELLKkggLYAELIRRQA 694
Cdd:COG1134 219 LEKGRLVMDGDPEEVIA---AYEALLAGRE 245
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
454-679 |
3.04e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.09 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqv 533
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-ERG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 VGFISQEPVLF-GTTIMENIRFG-KLAAS-----DEEVYAAAREAN-AHefitsfpegyntIVGERGTTLSGGQKQRLAI 605
Cdd:PRK11000 77 VGMVFQSYALYpHLSVAENMSFGlKLAGAkkeeiNQRVNQVAEVLQlAH------------LLDRKPKALSGGQRQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 606 ARALIKQPTVLILDEATSALDAeSERV---VQEALDRASAGRTVLVIAH-RLSTVRGAHRIIVMADGRVWEAGTHEEL 679
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDA-ALRVqmrIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
469-680 |
3.97e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.23 E-value: 3.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGV-----VMLDGRDLRTLDPSWLRGQVVGFISQEPVL 543
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 544 FGTTIMENI----RFGKLAASDEevYAAAREANAHEfiTSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:PRK14271 113 FPMSIMDNVlagvRAHKLVPRKE--FRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 620 EATSALDAESERVVQEALDRASAGRTVLVIAHRLS-TVRGAHRIIVMADGRVWEAGTHEELL 680
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
463-665 |
4.16e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 463 SYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGrdlrtldpswlrGQVVGFISQ--- 539
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------------GARVAYVPQrse 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 540 EPVLFGTTIMENIRFG---------KLAASDEEVYAAAREAnahefitsfpEGYNTIVGERGTTLSGGQKQRLAIARALI 610
Cdd:NF040873 66 VPDSLPLTVRDLVAMGrwarrglwrRLTRDDRAAVDDALER----------VGLADLAGRQLGELSGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 611 KQPTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRGAHRIIVM 665
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
478-679 |
4.82e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 87.38 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 478 LTLPPGKIVALVGQSGGGKTTVASLLERFY--DPTAG--------VVMLDGRDLRTLDPSwlRGQVvGFISQEPVLFGT- 546
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGshiellgrTVQREGRLARDIRKS--RANT-GYIFQQFNLVNRl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 TIMENIRFGKLAASD-----EEVYAAAREANAHEFITSFpeGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:PRK09984 102 SVLENVLIGALGSTPfwrtcFSWFTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109068902 622 TSALDAESERVVQEALD--RASAGRTVLVIAHRLS-TVRGAHRIIVMADGRVWEAGTHEEL 679
Cdd:PRK09984 180 IASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
480-674 |
6.82e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.07 E-value: 6.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 480 LPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--QVVGFISQEPV-------LFGTTIME 550
Cdd:PRK10261 347 LWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrRDIQFIFQDPYasldprqTVGDSIME 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 551 NIRFGKLAASDEevyAAAREANAHEFITSFPEGYNTIVGErgttLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-S 629
Cdd:PRK10261 427 PLRVHGLLPGKA---AAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSiR 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 109068902 630 ERVVQEALD-RASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAG 674
Cdd:PRK10261 500 GQIINLLLDlQRDFGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
458-674 |
7.29e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.53 E-value: 7.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYPCRPGF--------EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYdPTAGVVMLDGRDLRTLDPSWL 529
Cdd:PRK15134 279 EQLQVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 530 -----RGQVVgFisQEP---------VLfgTTIMENIRFGK----LAASDEEVYAAARE-----ANAHEFITSFpegynt 586
Cdd:PRK15134 358 lpvrhRIQVV-F--QDPnsslnprlnVL--QIIEEGLRVHQptlsAAQREQQVIAVMEEvgldpETRHRYPAEF------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 587 ivgergttlSGGQKQRLAIARALIKQPTVLILDEATSALDaeseRVVQE---ALDRASAGR---TVLVIAHRLSTVRG-A 659
Cdd:PRK15134 427 ---------SGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlC 493
|
250
....*....|....*
gi 109068902 660 HRIIVMADGRVWEAG 674
Cdd:PRK15134 494 HQVIVLRQGEVVEQG 508
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
458-698 |
7.63e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 7.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYpcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFI 537
Cdd:PRK13652 7 RDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR-KFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 538 SQEP--VLFGTTIMENIRFGKLAAS-DEE-----VYAAAREANAHEFITSFPEgyntivgergtTLSGGQKQRLAIARAL 609
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFGPINLGlDEEtvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 610 IKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEELLkkggLY 686
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIF----LQ 228
|
250
....*....|..
gi 109068902 687 AELIRRQALDAP 698
Cdd:PRK13652 229 PDLLARVHLDLP 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
463-670 |
1.06e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.70 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 463 SYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL--ERfyDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQE 540
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLGVAYIPED 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 541 PVLFGT----TIMENIRFGKLaasDEEVYA-------AAREANAHEFITSF---PEGYNTIVGergtTLSGGQKQRLAIA 606
Cdd:COG3845 342 RLGRGLvpdmSVAENLILGRY---RRPPFSrggfldrKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 607 RALIKQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRV 670
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
468-668 |
1.17e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.84 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQE-PVLFGT 546
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 TIMENIRFGKLAAsdEEV-------YAAARE-ANAHEFITSFPEGYNTIVGErgttLSGGQKQRLAIARALIKQPTVLIL 618
Cdd:PRK09700 96 TVLENLYIGRHLT--KKVcgvniidWREMRVrAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 109068902 619 DEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIVMADG 668
Cdd:PRK09700 170 DEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
453-699 |
1.27e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.99 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 453 GSVTFQNVCFSYPCRPGFE--VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF------------YDPTAGVVML-D 517
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEfkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetgqtivgdYAIPANLKKIkE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 518 GRDLRtldpswlrgQVVGFISQEP--VLFGTTIMENIRFG--KLAASDEEVYAAAREANAhefITSFPEGYntiVGERGT 593
Cdd:PRK13645 85 VKRLR---------KEIGLVFQFPeyQLFQETIEKDIAFGpvNLGENKQEAYKKVPELLK---LVQLPEDY---VKRSPF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 594 TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RGAHRIIVMADGRV 670
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKV 229
|
250 260
....*....|....*....|....*....
gi 109068902 671 WEAGTHEELLKKgglyAELIRRQALDAPR 699
Cdd:PRK13645 230 ISIGSPFEIFSN----QELLTKIEIDPPK 254
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
455-669 |
1.30e-18 |
|
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: 82.88 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVmldgrdlrtldpSWLRGQVV 534
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------TWGSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQepvlfgttimenirfgklaasdeevyaaareanahefitsfpegyntivgergttLSGGQKQRLAIARALIKQPT 614
Cdd:cd03221 66 GYFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 615 VLILDEATSALDAESERVVQEALdRASAGrTVLVIAH-R--LSTVrgAHRIIVMADGR 669
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
118-670 |
1.54e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 89.47 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 118 KLFWQFLRPHLLALGVAIVLALGAALVNVqipLLLGQLVEIVAKYTRDHVGSFMTesrklsthLLILYGVQGLLTFGYLV 197
Cdd:COG4615 2 NLLRLLLRESRWLLLLALLLGLLSGLANA---GLIALINQALNATGAALARLLLL--------FAGLLVLLLLSRLASQL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 198 LLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFkSSFKLVISQGLRSCTQVAGCLVSLSMLSTRL 277
Cdd:COG4615 71 LLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAYLAWLSPPL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 278 TLLLMVAtpalMGVGTLMGsglRKLSRQCQEQIARAMGVADEALGNVRTV----RAFAM-EQREEERYGAELEACRCRAE 352
Cdd:COG4615 150 FLLTLVL----LGLGVAGY---RLLVRRARRHLRRAREAEDRLFKHFRALlegfKELKLnRRRRRAFFDEDLQPTAERYR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 353 EL-GRGIALFqgLSNIAF-NCMVLGtlFIGGSLVAGQQLTGGDL---------MSFLVA--SQTVQR----SMANLSvlF 415
Cdd:COG4615 223 DLrIRADTIF--ALANNWgNLLFFA--LIGLILFLLPALGWADPavlsgfvlvLLFLRGplSQLVGAlptlSRANVA--L 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 416 GQVVRGLSAGARVFEYMALSPCIPLSGGCcipkehlrGSVTFQNVCFSYPC---RPGFEVlKDFTLTLPPGKIVALVGQS 492
Cdd:COG4615 297 RKIEELELALAAAEPAAADAAAPPAPADF--------QTLELRGVTYRYPGedgDEGFTL-GPIDLTIRRGELVFIVGGN 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 493 GGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGqvvgfisqepvLFgTTImenirFgklaaSD----EEVY--- 565
Cdd:COG4615 368 GSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ-----------LF-SAV-----F-----SDfhlfDRLLgld 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 566 AAAREANAHEFITSFP-EGYNTIVGERGTT--LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEAL--DRA 640
Cdd:COG4615 426 GEADPARARELLERLElDHKVSVEDGRFSTtdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTELlpELK 505
|
570 580 590
....*....|....*....|....*....|..
gi 109068902 641 SAGRTVLVIAH--RLSTVrgAHRIIVMADGRV 670
Cdd:COG4615 506 ARGKTVIAISHddRYFDL--ADRVLKMDYGKL 535
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
477-680 |
1.73e-18 |
|
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: 89.48 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 477 TLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML----DGRDLRTLDPSwLRGQV---VGFISQEPVLFG-TTI 548
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRAkryIGILHQEYDLYPhRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 549 MENI----------RFGKLAASDEEVYAAAREANAHEFITSFPEgyntivgergtTLSGGQKQRLAIARALIKQPTVLIL 618
Cdd:TIGR03269 383 LDNLteaiglelpdELARMKAVITLKMVGFDEEKAEEILDKYPD-----------ELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 619 DEATSALDAESERVVQEAL--DRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELL 680
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
471-670 |
2.84e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.11 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVvMLDGR--------DLRTLdpswlrgqvvgFisQEPV 542
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTaplaeareDTRLM-----------F--QDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 LFG-TTIMENIRFGkLAASDEEvyaAAREANAhefitsfPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:PRK11247 92 LLPwKKVIDNVGLG-LKGQWRD---AALQALA-------AVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 109068902 622 TSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHRIIVMADGRV 670
Cdd:PRK11247 161 LGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
472-670 |
3.01e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.14 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGQVVGFISQEPVLfGT----T 547
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRAKYIGRVFQDPMM-GTapsmT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 548 IMENI--------RFG-KLAASdeevyaAAREANAHEFITSFPEGY----NTIVGergtTLSGGQKQRLAIARALIKQPT 614
Cdd:COG1101 99 IEENLalayrrgkRRGlRRGLT------KKRRELFRELLATLGLGLenrlDTKVG----LLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 615 VLILDEATSALD---AE-----SERVVQEaldrasAGRTVLVIAHRLS-TVRGAHRIIVMADGRV 670
Cdd:COG1101 169 LLLLDEHTAALDpktAAlvlelTEKIVEE------NNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
458-679 |
3.97e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.18 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 458 QNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlRGQVVG-- 535
Cdd:PRK15439 15 RSISKQYS---GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA--KAHQLGiy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 536 FISQEPVLFGT-TIMENIRFG--KLAASDEEVYAAAREANAHeFITSFPEGyntivgergtTLSGGQKQRLAIARALIKQ 612
Cdd:PRK15439 90 LVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQ-LDLDSSAG----------SLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 613 PTVLILDEATSALD-AESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEEL 679
Cdd:PRK15439 159 SRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
463-674 |
5.55e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.21 E-value: 5.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 463 SYPCRPGFEvlkDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLD--------------PSW 528
Cdd:PRK11701 15 LYGPRKGCR---DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseaerrrllrTEW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 529 lrgqvvGFISQEP-------VLFGTTIMEnirfgKLAASDEEVYAAAREANAH---------EFITSFPegyntivgerg 592
Cdd:PRK11701 92 ------GFVHQHPrdglrmqVSAGGNIGE-----RLMAVGARHYGDIRATAGDwlerveidaARIDDLP----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 593 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAEservVQ-EALD--R---ASAGRTVLVIAHRLSTVRG-AHRIIVM 665
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQaRLLDllRglvRELGLAVVIVTHDLAVARLlAHRLLVM 225
|
....*....
gi 109068902 666 ADGRVWEAG 674
Cdd:PRK11701 226 KQGRVVESG 234
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
181-428 |
7.11e-18 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 84.93 E-value: 7.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 181 LLILYGVQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:cd18565 60 TVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 261 TQVAGCLVSLSMLSTRLTLLLMVATPaLMGVGTLMGSG-LRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEER 339
Cdd:cd18565 140 VTVLGIGAILFYLNWQLALVALLPVP-LIIAGTYWFQRrIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERER 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 340 YGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLV------AGQQLTGGDLMSFLVASQTVQRSMANLSV 413
Cdd:cd18565 219 VADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVldgpplFTGTLTVGTLVTFLFYTQRLLWPLTRLGD 298
|
250
....*....|....*
gi 109068902 414 LFGQVVRGLSAGARV 428
Cdd:cd18565 299 LIDQYQRAMASAKRV 313
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
472-680 |
9.41e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.56 E-value: 9.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF---YDP---TAGVVMLDGRDLRTLDPSWLRGQvVGFISQEPVLF- 544
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKE-VGMVFQQPNPFp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 545 GTTIMENIRFGKLA---ASDEEVYAAAREANAHefITSFPEGYNTIvGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:PRK14246 104 HLSIYDNIAYPLKShgiKEKREIKKIVEECLRK--VGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 622 TSALDAESERVVQEALDRASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEELL 680
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
474-679 |
9.65e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.14 E-value: 9.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 474 KDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--QVVGFISQEPV-------LF 544
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrSDIQMIFQDPLaslnprmTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 545 GTTIMENIRFGKLAASDEEVYAAAREANA-------------HEFitsfpegyntivgergttlSGGQKQRLAIARALIK 611
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSRQEVKDRVKAMMLkvgllpnlinrypHEF-------------------SGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 612 QPTVLILDEATSALDAESE-RVVQ--EALDRaSAGRTVLVIAHRLSTVRgaH---RIIVMADGRVWEAGTHEEL 679
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQaQVVNllQQLQR-EMGLSLIFIAHDLAVVK--HisdRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
469-670 |
3.17e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRGQVvGFISQEP-VLF 544
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQI-GMIFQDHhLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 545 GTTIMENIRFGKL--AASDEE----VYAAAREANAHEFITSFPegyntivgergTTLSGGQKQRLAIARALIKQPTVLIL 618
Cdd:PRK10908 93 DRTVYDNVAIPLIiaGASGDDirrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 619 DEATSALD-AESERVVQ--EALDRasAGRTVLVIAHRLSTV-RGAHRIIVMADGRV 670
Cdd:PRK10908 162 DEPTGNLDdALSEGILRlfEEFNR--VGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
455-671 |
3.19e-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: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAG-VVMLDGRDLRtldpswlrgqv 533
Cdd:cd03223 1 IELENLSLATP--DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGrIGMPEGEDLL----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 vgFISQEPVLFGTTIMENIrfgklaasdeeVYAAAREanahefitsfpegyntivgergttLSGGQKQRLAIARALIKQP 613
Cdd:cd03223 68 --FLPQRPYLPLGTLREQL-----------IYPWDDV------------------------LSGGEQQRLAFARLLLHKP 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 614 TVLILDEATSALDAESERVVQEALDRASAgrTVLVIAHRLSTVRGAHRIIVMADGRVW 671
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
450-681 |
5.69e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.37 E-value: 5.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 450 HLRGSVTFQ--NVCFSYPCRpgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS 527
Cdd:PRK10575 5 TNHSDTTFAlrNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 528 WLRGQVVGFISQEPVLFGTTIMENI---RF------GKLAASDEEvyaAAREANAHEFITSFPegyNTIVgergTTLSGG 598
Cdd:PRK10575 82 AFARKVAYLPQQLPAAEGMTVRELVaigRYpwhgalGRFGAADRE---KVEEAISLVGLKPLA---HRLV----DSLSGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 599 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIA--HRLS-TVRGAHRIIVMADGRVWEAGT 675
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQGT 231
|
....*.
gi 109068902 676 HEELLK 681
Cdd:PRK10575 232 PAELMR 237
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
467-666 |
6.61e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 79.84 E-value: 6.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGqvVGFISQEPVLFGT 546
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG--LLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 -TIMENIRFGKLAASDEEVYAAAREANAHEFitsfpegYNTIVGergtTLSGGQKQRLAIARALIKQPTVLILDEATSAL 625
Cdd:cd03231 88 lSVLENLRFWHADHSDEQVEEALARVGLNGF-------EDRPVA----QLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 109068902 626 DAESERVVQEALDR--ASAGRTVLVIAHRLSTVRGAHRIIVMA 666
Cdd:cd03231 157 DKAGVARFAEAMAGhcARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
471-680 |
8.06e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.78 E-value: 8.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlRGQVVGFISQEPVLFGT---- 546
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDK--DGQLKVADKNQLRLLRTrltm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 -----------TIMENIRFGK---LAASDEEVYAAAREANAHEFITSFPEGyntivgERGTTLSGGQKQRLAIARALIKQ 612
Cdd:PRK10619 97 vfqhfnlwshmTVLENVMEAPiqvLGLSKQEARERAVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109068902 613 PTVLILDEATSALD----AESERVVQEAldrASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELL 680
Cdd:PRK10619 171 PEVLLFDEPTSALDpelvGEVLRIMQQL---AEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
472-672 |
9.87e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.82 E-value: 9.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP---SWLRGQVVGFISQEPVLFGT-T 547
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAKHVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 548 IMENIRFGKLAASDEEvyAAAREaNAHEFITSFPegyntiVGER----GTTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:PRK10584 105 ALENVELPALLRGESS--RQSRN-GAKALLEQLG------LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 109068902 624 ALDAES-ERVVQE--ALDRASAgRTVLVIAHRLSTVRGAHRIIVMADGRVWE 672
Cdd:PRK10584 176 NLDRQTgDKIADLlfSLNREHG-TTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
467-680 |
1.20e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.60 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWlRGQVVGFISQEPvlfGT 546
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-RSQRIRMIFQDP---ST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 TIMENIRFGKL-------------AASDEEVYAAAREANA-HEFITSFPEgyntivgergtTLSGGQKQRLAIARALIKQ 612
Cdd:PRK15112 99 SLNPRQRISQIldfplrlntdlepEQREKQIIETLRQVGLlPDHASYYPH-----------MLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109068902 613 PTVLILDEATSALD-AESERVVQEALD-RASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELL 680
Cdd:PRK15112 168 PKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
471-670 |
1.32e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.14 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS--WLRGqvVGFIS----QEPVLF 544
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdaIRAG--IAYVPedrkGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 545 GTTIMENI------RFGKLAASDEevyaAAREANAHEFITSF---PEGYNTIVGergtTLSGGQKQRLAIARALIKQPTV 615
Cdd:COG1129 344 DLSIRENItlasldRLSRGGLLDR----RRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 616 LILDEATSALD--AESE--RVVQEAldrASAGRTVLVIAHRLSTVRG-AHRIIVMADGRV 670
Cdd:COG1129 416 LILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVISSELPELLGlSDRILVMREGRI 472
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
203-428 |
1.39e-16 |
|
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: 81.17 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 203 GERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLM 282
Cdd:cd18558 87 AGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVIL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 283 VATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEAcrcrAEELGRGIALFQ 362
Cdd:cd18558 167 AISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEI----AKRNGIKKAITF 242
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 363 GLSNIAFNCMVLGT----LFIGGSLVAGQQLTGGDlmsflvasqtvqrsmaNLSVLFGQVVRGLSAGARV 428
Cdd:cd18558 243 NISMGAAFLLIYASyalaFWYGTYLVTQQEYSIGE----------------VLTVFFSVLIGAFSAGQQV 296
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
471-651 |
2.34e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.50 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD--PTA---GVVMLDGRDLRT--LDPSWLRGQVvGFISQEPVL 543
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSpdVDPIEVRREV-GMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 544 F-GTTIMENIRFG----KLAAS----DEEVYAAAREANAHEFITSFPEGYntivgerGTTLSGGQKQRLAIARALIKQPT 614
Cdd:PRK14267 97 FpHLTIYDNVAIGvklnGLVKSkkelDERVEWALKKAALWDEVKDRLNDY-------PSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 109068902 615 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAH 651
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
472-692 |
2.59e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.65 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGQVVGFISQEPVLFG-TTIME 550
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY-ASKEVARRIGLLAQNATTPGdITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 551 NIR---------FGKLAASDEEVYAAAREANahefitsfpeGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:PRK10253 101 LVArgryphqplFTRWRKEDEEAVTKAMQAT----------GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 622 TSALDAESERVVQEALDRAS--AGRTVLVIAHRLS-TVRGAHRIIVMADGRVWEAGTHEELLKkgglyAELIRR 692
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNreKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT-----AELIER 239
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
470-679 |
2.79e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.13 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSW--------------------- 528
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKekekvleklviqktrfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 529 ---LRGQV-VGFISQEPVLFGTTIMENIRFG--KLAASDEEVYAAAREanahefitsfpegYNTIVG------ERGT-TL 595
Cdd:PRK13651 100 ikeIRRRVgVVFQFAEYQLFEQTIEKDIIFGpvSMGVSKEEAKKRAAK-------------YIELVGldesylQRSPfEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 596 SGGQKQRLAIARALIKQPTVLILDEATSALDAEServVQEALD----RASAGRTVLVIAHRLSTV-RGAHRIIVMADGR- 669
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG---VKEILEifdnLNKQGKTIILVTHDLDNVlEWTKRTIFFKDGKi 243
|
250
....*....|
gi 109068902 670 VWEAGTHEEL 679
Cdd:PRK13651 244 IKDGDTYDIL 253
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
453-668 |
2.93e-16 |
|
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: 77.67 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 453 GSVTFQNVCFSYPCRPGF-EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL-ERfydPTAGVV----MLDGrdlRTLDP 526
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKrQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR---KTAGVItgeiLING---RPLDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 527 SWLRgqVVGFISQEPVLFGT-TIMENIRFGklaasdeevyAAAREanahefitsfpegyntivgergttLSGGQKQRLAI 605
Cdd:cd03232 76 NFQR--STGYVEQQDVHSPNlTVREALRFS----------ALLRG------------------------LSVEQRKRLTI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 606 ARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRGAH--RIIVMADG 668
Cdd:cd03232 120 GVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSASIFEKfdRLLLLKRG 185
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
476-682 |
3.42e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 80.33 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 476 FTLTLPPGKIVALVGQSGGGKTTVASLLERFYDP----TAGVVMLDGRDLRTLDPSWLR---GQVVGFISQEP------- 541
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRkiiGREIAMIFQEPsscldps 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 542 VLFGTTIMENI-----------RFGklaasdeevyAAAREANA---------HEFI-TSFPEgyntivgergtTLSGGQK 600
Cdd:COG4170 106 AKIGDQLIEAIpswtfkgkwwqRFK----------WRKKRAIEllhrvgikdHKDImNSYPH-----------ELTEGEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 601 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHE 677
Cdd:COG4170 165 QKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARlnQLQGTSILLISHDLESIsQWADTITVLYCGQTVESGPTE 244
|
....*
gi 109068902 678 ELLKK 682
Cdd:COG4170 245 QILKS 249
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
470-652 |
4.01e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.08 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFY--DPTAGVVMLDGRDlrtldpswlrgqvvgfISQEpvlfgTT 547
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ----------------FGRE-----AS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 548 IMENI-RFGKLAASdEEVYAAAREANAHEFITSFPEgyntivgergttLSGGQKQRLAIARALIKQPTVLILDEATSALD 626
Cdd:COG2401 102 LIDAIgRKGDFKDA-VELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180
....*....|....*....|....*...
gi 109068902 627 AESERVVQEALDRAS--AGRTVLVIAHR 652
Cdd:COG2401 169 RQTAKRVARNLQKLArrAGITLVVATHH 196
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
467-650 |
4.78e-16 |
|
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: 77.01 E-value: 4.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWlrGQVVGFISQEPVLFGT 546
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 -TIMENIRFGK--LAASDEEVYAAAREAN--AHEfitsfpegyNTIVGergtTLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:TIGR01189 88 lSALENLHFWAaiHGGAQRTIEDALAAVGltGFE---------DLPAA----QLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180
....*....|....*....|....*....
gi 109068902 622 TSALDAESERVVQEALdRASAGRTVLVIA 650
Cdd:TIGR01189 155 TTALDKAGVALLAGLL-RAHLARGGIVLL 182
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
472-670 |
1.12e-15 |
|
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: 76.93 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLERFYDpTAGVVMLDGRDLRtldpswlRGQV---VGFISQEPVLF 544
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPRK-------PDQFqkcVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 545 -GTTIMENIRFGKLAASDEEVYAAAREANAHefITSFPEGYNTIVG-ERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 622
Cdd:cd03234 94 pGLTVRETLTYTAILRLPRKSSDAIRKKRVE--DVLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 109068902 623 SALDAESERVVQEALDR-ASAGRTVLVIAH--RLSTVRGAHRIIVMADGRV 670
Cdd:cd03234 172 SGLDSFTALNLVSTLSQlARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
467-681 |
1.22e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.67 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVV----MLDGR------DLRTLDPSWL---RGQV 533
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkMLLRRrsrqviELSEQSAAQMrhvRGAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 VGFISQEPVL-------FGTTIMENIRFGKLAASDEEVYAAAREANAhefiTSFPEGyNTIVGERGTTLSGGQKQRLAIA 606
Cdd:PRK10261 106 MAMIFQEPMTslnpvftVGEQIAESIRLHQGASREEAMVEAKRMLDQ----VRIPEA-QTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 607 RALIKQPTVLILDEATSALDAESE-------RVVQEALDRAsagrtVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEE 678
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQ 255
|
...
gi 109068902 679 LLK 681
Cdd:PRK10261 256 IFH 258
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
455-699 |
1.31e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.85 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSY-PCRP-GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAG------VVMLDGRDLRTLDP 526
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 527 swLRGQV-VGFISQEPVLFGTTIMENIRFG--KLAASDEEVYAAARE-----ANAHEFITSFPegyntivgergTTLSGG 598
Cdd:PRK13643 82 --VRKKVgVVFQFPESQLFEETVLKDVAFGpqNFGIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 599 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTH 676
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
250 260
....*....|....*....|...
gi 109068902 677 EELLKKgglyAELIRRQALDAPR 699
Cdd:PRK13643 229 SDVFQE----VDFLKAHELGVPK 247
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
181-428 |
1.98e-15 |
|
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: 77.49 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 181 LLILYGVQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRL--TTDVQEFKSSfkLVISQGLR 258
Cdd:cd18570 48 LILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFndANKIREAISS--TTISLFLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 259 SCTQVAGcLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAME----Q 334
Cdd:cd18570 126 LLMVIIS-GIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEeqflK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 335 REEERYGAELEACRcraeELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVL 414
Cdd:cd18570 205 KIEKKFSKLLKKSF----KLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINL 280
|
250
....*....|....
gi 109068902 415 FGQVVRGLSAGARV 428
Cdd:cd18570 281 QPKIQEAKVAADRL 294
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
468-679 |
2.14e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQE----PVL 543
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQElhlvPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 544 fgtTIMENIRFGKLAAS-----DEEVYAAAREANAHEFITSFPegyNTIVGErgttLSGGQKQRLAIARALIKQPTVLIL 618
Cdd:PRK11288 95 ---TVAENLYLGQLPHKggivnRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 619 DEATSALDA-ESE---RVVQEALDRasaGRTVLVIAHRLSTV-RGAHRIIVMADGRvwEAGTHEEL 679
Cdd:PRK11288 165 DEPTSSLSArEIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGR--YVATFDDM 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
469-682 |
5.11e-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: 78.31 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF--YDPTAGVVMLDgrdlRTLDPSWLRGQVVGFISQE-PVLFG 545
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYH----VALCEKCGYVERPSKVGEPcPVCGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 546 TTIMENIRFGKLaasDEEVYAAAREANAHEF----------------ITSFPE-GYN--------------TIVGERGT- 593
Cdd:TIGR03269 88 TLEPEEVDFWNL---SDKLRRRIRKRIAIMLqrtfalygddtvldnvLEALEEiGYEgkeavgravdliemVQLSHRITh 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 594 ---TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAsagrtvlVIAHRLSTVRGAH---------- 660
Cdd:TIGR03269 165 iarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEA-------VKASGISMVLTSHwpeviedlsd 237
|
250 260
....*....|....*....|..
gi 109068902 661 RIIVMADGRVWEAGTHEELLKK 682
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
472-680 |
5.43e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.38 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrtldPSWLR------GQVVGFISQEPVLfg 545
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARharqrvGVVPQFDNLDPDF-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 546 tTIMENIR-----FGKLAASdeevyAAAREANAHEFiTSFPEGYNTIVGErgttLSGGQKQRLAIARALIKQPTVLILDE 620
Cdd:PRK13537 96 -TVRENLLvfgryFGLSAAA-----ARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 621 ATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEELL 680
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
467-677 |
5.45e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdpswLRGQVVGFISQE------ 540
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNLVAYVPQSeevdws 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 541 -PVLFGTTIMENiRFGKLA------ASDEEVYAAAREAnahefiTSFPEGYNTIVGErgttLSGGQKQRLAIARALIKQP 613
Cdd:PRK15056 93 fPVLVEDVVMMG-RYGHMGwlrrakKRDRQIVTAALAR------VDMVEFRHRQIGE----LSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 614 TVLILDEATSALDAESE-RVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHE 677
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
469-680 |
1.34e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.16 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRD--LRTLDPSWLRGqvVGFISQEPVLFGT 546
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisLLPLHARARRG--IGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 TIMENIRFGKLAASDEeVYAAAREANAHEFITSFPEGYntIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 626
Cdd:PRK10895 93 LSVYDNLMAVLQIRDD-LSAEQREDRANELMEEFHIEH--LRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 627 AES----ERVVQEALDRasaGRTVLVIAHRL-STVRGAHRIIVMADGRVWEAGTHEELL 680
Cdd:PRK10895 170 PISvidiKRIIEHLRDS---GLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
474-679 |
1.55e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.97 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 474 KDFTLTLPPGKIVALVGQSGGGKT-TVASLLERF---YDPTAGVVMLDGRdlrTLDPSWLRGQVVGFISQEP-------V 542
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGK---PVAPCALRGRKIATIMQNPrsafnplH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 LFGTTIMENIRFGKLAASDEEVYAAARE---ANAHEFITSFPegyntivgergTTLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:PRK10418 97 TMHTHARETCLALGKPADDATLTAALEAvglENAARVLKLYP-----------FEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109068902 620 EATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEEL 679
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
471-670 |
2.72e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 73.14 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGrdlrtLDPsWLRGQvvGFISQEPVLFGT---- 546
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVP-WKRRK--KFLRRIGVVFGQktql 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 ----TIMENIRFGKLAASDEEVYAAAREANAHEFITSFPEgYNTIVGErgttLSGGQKQRLAIARALIKQPTVLILDEAT 622
Cdd:cd03267 107 wwdlPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEEL-LDTPVRQ----LSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 109068902 623 SALDAESERVVQEALDRASAGR--TVLVIAHRLSTV-RGAHRIIVMADGRV 670
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRL 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
468-653 |
3.11e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.81 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGT- 546
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 TIMENI--------RFGKLAASdeEVYAAAREANAHefiTSFPEGYNTIVGErgttLSGGQKQRLAIARALIKQPTVLIL 618
Cdd:PRK10762 95 TIAENIflgrefvnRFGRIDWK--KMYAEADKLLAR---LNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 109068902 619 DEATSAL-DAESE---RVVQEALDRasaGRTVLVIAHRL 653
Cdd:PRK10762 166 DEPTDALtDTETEslfRVIRELKSQ---GRGIVYISHRL 201
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
471-705 |
5.27e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 5.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVA-SLLERFYDP----TAGVVMLDGRDLRTLDPSWLR---GQVVGFISQEPV 542
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRgvrGNKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 LfGTTIMENIR------------FGKLAASDEEVYAAAREA--NAHEFITSFPEgyntivgergtTLSGGQKQRLAIARA 608
Cdd:PRK15134 103 V-SLNPLHTLEkqlyevlslhrgMRREAARGEILNCLDRVGirQAAKRLTDYPH-----------QLSGGERQRVMIAMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 609 LIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELLKKGgl 685
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAP-- 248
|
250 260
....*....|....*....|
gi 109068902 686 yAELIRRQALDAPRTVAPPP 705
Cdd:PRK15134 249 -THPYTQKLLNSEPSGDPVP 267
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
454-656 |
8.35e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.99 E-value: 8.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYPCRpgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDpTAGVVMLDGR--------DLRTLD 525
Cdd:PRK14258 7 AIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqniYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 526 PSWLRGQVvGFISQEPVLFGTTIMENIRFG-KLAA------SDEEVYAAAREANAHEFITSfpegyntIVGERGTTLSGG 598
Cdd:PRK14258 83 LNRLRRQV-SMVHPKPNLFPMSVYDNVAYGvKIVGwrpkleIDDIVESALKDADLWDEIKH-------KIHKSALDLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 599 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV 656
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
456-651 |
9.59e-14 |
|
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: 74.59 E-value: 9.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 456 TFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLerfydptAGVvmldgrDLRTLDPSWLR-GQVV 534
Cdd:TIGR03719 6 TMNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGV------DKDFNGEARPQpGIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVLFGT-TIMENIRFG----------------KLAASDEEVYAAARE----------ANAHEFITSF------- 580
Cdd:TIGR03719 71 GYLPQEPQLDPTkTVRENVEEGvaeikdaldrfneisaKYAEPDADFDKLAAEqaelqeiidaADAWDLDSQLeiamdal 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 581 --PEGyNTIVgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES----ERVVQEaldraSAGrTVLVIAH 651
Cdd:TIGR03719 151 rcPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE-----YPG-TVVAVTH 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
471-701 |
1.12e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.96 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrTLDPSwLRG-----QVVGFISQEP--VL 543
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYS-KRGllalrQQVATVFQDPeqQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 544 FGTTIMENIRFG--KLAASDEEVyaAAREANAHEFITSFPEGYNTIvgergTTLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:PRK13638 91 FYTDIDSDIAFSlrNLGVPEAEI--TRRVDEALTLVDAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 622 TSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEELLKKGglyaELIRRQALDAPR 699
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACT----EAMEQAGLTQPW 239
|
..
gi 109068902 700 TV 701
Cdd:PRK13638 240 LV 241
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
467-670 |
2.09e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 69.60 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLERFYDPTaGVVMLDGRDLRTlDPSWLRGQVVgFISQEPV 542
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKE-FAEKYPGEII-YVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 LFGT-TIMENIRFgklaasdeevyaaAREANAHEFItsfpegyntivgeRGttLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:cd03233 94 HFPTlTVRETLDF-------------ALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 622 TSALDAEServvqeALDRASAGRTvlvIAH--RLSTVRGAH-----------RIIVMADGRV 670
Cdd:cd03233 146 TRGLDSST------ALEILKCIRT---MADvlKTTTFVSLYqasdeiydlfdKVLVLYEGRQ 198
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
134-394 |
2.40e-13 |
|
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: 71.38 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 134 AIVLALGAALVNVQIPLLLGQLVeivakytrDHVGSFMTESRKLSTHLLILYGVQGLLT--FGYL--VLLSHIGERMAVD 209
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAV--------DALSAPASALLAVPLLLLLAYGLARILSslFNELrdALFARVSQRAVRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 210 MRRALFSSLLRQDIAFFDANKTGQLVSrlttdvqefkssfklVISQGLRSCTQVAG------------CLVSLSMLSTRL 277
Cdd:cd18582 73 LALRVFRHLHSLSLRFHLSRKTGALSR---------------AIERGTRGIEFLLRfllfnilptileLLLVCGILWYLY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 278 TL---LLMVATPALMGVGTLMGSGLR-KLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEE 353
Cdd:cd18582 138 GWsyaLITLVTVALYVAFTIKVTEWRtKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVK 217
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 109068902 354 LGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDL 394
Cdd:cd18582 218 SQTSLALLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDF 258
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
467-703 |
2.71e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.63 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT-VASLLERFYDPTA-------GVVMLDGRDLRTLDPSWL-RGQVV--- 534
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTlLKALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLaRLRAVlpq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 ------GFISQEPVLFGtTIMENIRFGKLAASDEEVYAAAREAnahefitsfpEGYNTIVGERGTTLSGGQKQRLAIARA 608
Cdd:PRK13547 91 aaqpafAFSAREIVLLG-RYPHARRAGALTHRDGEIAWQALAL----------AGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 609 L---------IKQPTVLILDEATSALD-AESERVVQEALDRASAGRT-VLVIAHRLS-TVRGAHRIIVMADGRVWEAGTH 676
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGAP 239
|
250 260 270
....*....|....*....|....*....|...
gi 109068902 677 EELLKkgglyAELIRR------QALDAPRTVAP 703
Cdd:PRK13547 240 ADVLT-----PAHIARcygfavRLVDAGDGVPP 267
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
468-669 |
2.74e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.04 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYdPTA---GVVMLDGRDLR--TLDPSWLRGQVVgfISQEPV 542
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQasNIRDTERAGIAI--IHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 LF-GTTIMENI-------RFGKLaaSDEEVYAAAREANAHEFITSFPegyNTIVGErgttLSGGQKQRLAIARALIKQPT 614
Cdd:PRK13549 93 LVkELSVLENIflgneitPGGIM--DYDAMYLRAQKLLAQLKLDINP---ATPVGN----LGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 615 VLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTVRG-AHRIIVMADGR 669
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIrDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
455-656 |
3.59e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRpgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswLRgqvV 534
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR---I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVLFGTTIMENIRFGKL--AASDEEVYAAAREANAHEFItSFPEgyntivgergTTLSGGQKQRLAIARALIKQ 612
Cdd:PRK09544 70 GYVPQKLYLDTTLPLTVNRFLRLrpGTKKEDILPALKRVQAGHLI-DAPM----------QKLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 109068902 613 PTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV 656
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDLHLV 184
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
457-672 |
4.63e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.31 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 457 FQNVCFSYPcRPGFEVlKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGqvvgf 536
Cdd:PRK10522 325 LRNVTFAYQ-DNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK----- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 537 isqepvLFGTTIMENIRFGKL-----AASDEEVYAA--AREANAHEFitsfpegynTIVGERGTT--LSGGQKQRLAIAR 607
Cdd:PRK10522 398 ------LFSAVFTDFHLFDQLlgpegKPANPALVEKwlERLKMAHKL---------ELEDGRISNlkLSKGQKKRLALLL 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 608 ALIKQPTVLILDEATSALDAESERVV-QEALDRASA-GRTVLVIAHRLSTVRGAHRIIVMADGRVWE 672
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
471-680 |
5.20e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.14 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFG-TTIM 549
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSrMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 550 ENIRFGKLAASDEEVyaAAREANAHEFitsFPEGYNTIVgERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALdaeS 629
Cdd:PRK11614 99 ENLAMGGFFAERDQF--QERIKWVYEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL---A 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 630 ERVVQEALD-----RASAGRTVLVIAHRLSTVRGAHRIIVMADGRVWEAGTHEELL 680
Cdd:PRK11614 170 PIIIQQIFDtieqlREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
475-679 |
5.86e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.52 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 475 DFTLTLPPGKIVALVGQSGGGKTTVA----SLLERfYDPTAGVVMLDGRDLRTLDPSWL---RGQVVGFISQEPVL---- 543
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAfalmGLLAA-NGRIGGSATFNGREILNLPEKELnklRAEQISMIFQDPMTslnp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 544 ---FGTTIMENI----RFGKLAASDEEVYA--AAREANAHEFITSFPEGYntivgergttlSGGQKQRLAIARALIKQPT 614
Cdd:PRK09473 113 ymrVGEQLMEVLmlhkGMSKAEAFEESVRMldAVKMPEARKRMKMYPHEF-----------SGGMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 615 VLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEEL 679
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLNelKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
467-651 |
6.61e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.36 E-value: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLErfydPTAGVVMLDGRDLRTLDPswlrGQVVGFISQ--- 539
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTllrlIAGLLP----PAAGTIKLDGGDIDDPDV----AEACHYLGHrna 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 540 -EPVLfgtTIMENIRF-GKLAASDEEVYAAAREANAHEFITSFPEGYntivgergttLSGGQKQRLAIARALIKQPTVLI 617
Cdd:PRK13539 84 mKPAL---TVAENLEFwAAFLGGEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*
gi 109068902 618 LDEATSALDAESERVVQEAL-DRASAGRTVLVIAH 651
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIrAHLAQGGIVIAATH 185
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
483-681 |
8.03e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.16 E-value: 8.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 483 GKIVALVGQSGGGKTtVASLLERFYDPTAGVVM-----LDGRDLRTLDPSWLR---GQVVGFISQEPVL-------FGTT 547
Cdd:PRK11022 33 GEVVGIVGESGSGKS-VSSLAIMGLIDYPGRVMaekleFNGQDLQRISEKERRnlvGAEVAMIFQDPMTslnpcytVGFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 548 IMENIRFGKLAASdeevyaAAREANAHEFITSF----PEGYNTIVGERgttLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:PRK11022 112 IMEAIKVHQGGNK------KTRRQRAIDLLNQVgipdPASRLDVYPHQ---LSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109068902 624 ALDAESE-RVVQEALDRASAGRTVLV-IAHRLSTV-RGAHRIIVMADGRVWEAGTHEELLK 681
Cdd:PRK11022 183 ALDVTIQaQIIELLLELQQKENMALVlITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
475-678 |
1.02e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 475 DFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDL-----RTLDPSWLRGqvVGFISQEPVLF-GTTI 548
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekGICLPPEKRR--IGYVFQDARLFpHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 549 MENIRFGkLAASDeevyaaareanahefitsfPEGYNTIVGERG---------TTLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:PRK11144 94 RGNLRYG-MAKSM-------------------VAQFDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 620 EATSALDAESERVVQEALDRASagRTV----LVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEE 678
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERLA--REInipiLYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
448-656 |
1.10e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 448 KEHLRGSVTF--QNVCFSYPCRPGFEV-LKDFTLTLPPGKIVALVGQSGGGKTTVASLL-ERFydpTAGVVMLDGR--DL 521
Cdd:TIGR00956 751 MEKESGEDIFhwRNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERV---TTGVITGGDRlvNG 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 522 RTLDPSWLRgqVVGFISQEPVLFGT-TIMENIRFGKLAASDEEVYAAAREANAHEFI-----TSFPEGyntIVGERGTTL 595
Cdd:TIGR00956 828 RPLDSSFQR--SIGYVQQQDLHLPTsTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIkllemESYADA---VVGVPGEGL 902
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109068902 596 SGGQKQRLAIARALIKQPTVLI-LDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV 656
Cdd:TIGR00956 903 NVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSAI 965
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
470-683 |
1.29e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.51 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF--YDPTAGVVMLDGRDLRTLDPSwLRGQVVGFIS-QEPV-LFG 545
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIFLAfQYPIeIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 546 TTimeNIRFGKLAASDEEVYAAAREANAHEFITSFPEGYNtIVGERGTTL--------SGGQKQRLAIARALIKQPTVLI 617
Cdd:CHL00131 99 VS---NADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 618 LDEATSALDAESERVVQEALDR-ASAGRTVLVIAH--RLSTVRGAHRIIVMADGRVWEAGTHE---ELLKKG 683
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElakELEKKG 246
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
442-680 |
2.51e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 442 GGCCIPKEHLRGsvtfqnvcfsypcrPGfevLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDL 521
Cdd:PRK10762 254 GEVRLKVDNLSG--------------PG---VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 522 RTLDPS-WLRGQVVgFISQEP----VLFGTTIMENIrfgKLAASDEEVYAAAREANAHE------FITSF----PeGYNT 586
Cdd:PRK10762 317 VTRSPQdGLANGIV-YISEDRkrdgLVLGMSVKENM---SLTALRYFSRAGGSLKHADEqqavsdFIRLFniktP-SMEQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 587 IVGErgttLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRG-AHRIIV 664
Cdd:PRK10762 392 AIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGmSDRILV 467
|
250 260
....*....|....*....|.
gi 109068902 665 MADGRV-----WEAGTHEELL 680
Cdd:PRK10762 468 MHEGRIsgeftREQATQEKLM 488
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
125-398 |
4.39e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 67.50 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 125 RPHLLALgvaIVLALGAALVNVQIPLLlgqlveivAKYTRDHvgsFMTESRKLS-THLLILYG----VQGLLTFGYLVLL 199
Cdd:cd18540 1 KKLLILL---IILMLLVALLDAVFPLL--------TKYAIDH---FITPGTLDGlTGFILLYLglilIQALSVFLFIRLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 200 SHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTL 279
Cdd:cd18540 67 GKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 280 LLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIA 359
Cdd:cd18540 147 IVLAVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSA 226
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 109068902 360 LF----QGLSNIAfncmVLGTLFIGGSLVAGQQLTGGDLMSFL 398
Cdd:cd18540 227 LFlpivLFLGSIA----TALVLWYGGILVLAGAITIGTLVAFI 265
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
181-414 |
4.93e-12 |
|
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: 67.20 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 181 LLILYGVQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRL--TTDVQEFKSsfKLVISQGLR 258
Cdd:cd18568 48 LLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFqeNQKIRRFLT--RSALTTILD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 259 SCTQVAgCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQ---- 334
Cdd:cd18568 126 LLMVFI-YLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERpirw 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 335 REEERYGAELEAcRCRAEELGRGIALFQGLSNIAFNCMVlgtLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVL 414
Cdd:cd18568 205 RWENKFAKALNT-RFRGQKLSIVLQLISSLINHLGTIAV---LWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGL 280
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
472-669 |
5.21e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.14 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLE-RFYDPT-AGVVMLDGRDLRTldPSWLRgqvVGFISQEPVLF-GTTI 548
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTK--QILKR---TGFVTQDDILYpHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 549 MENIRFGKLAASDEEVYAAAREANAHEFITSF--PEGYNTIVGE---RGttLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:PLN03211 158 RETLVFCSLLRLPKSLTKQEKILVAESVISELglTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 109068902 624 ALDAESE-RVVQEALDRASAGRTVLVIAHRLST--VRGAHRIIVMADGR 669
Cdd:PLN03211 236 GLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
468-672 |
6.43e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 68.66 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYdPTA---GVVMLDG--RDLRTLDPSWLRGQVVgfISQE-- 540
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGevCRFKDIRDSEALGIVI--IHQEla 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 541 --PVLfgtTIMENIRFGKLAASD-----EEVYAAAREANAHEFITSFPEgynTIVGERGTtlsgGQKQRLAIARALIKQP 613
Cdd:NF040905 89 liPYL---SIAENIFLGNERAKRgvidwNETNRRARELLAKVGLDESPD---TLVTDIGV----GKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109068902 614 TVLILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWE 672
Cdd:NF040905 159 KLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
454-669 |
6.50e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.55 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrtldPSWLR--- 530
Cdd:PRK13536 41 AIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARlar 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 531 ---GQVVGFISQEPVLfgtTIMENI-----RFGKLAASDEEVYAAAREANAHEfitsfpegynTIVGERGTTLSGGQKQR 602
Cdd:PRK13536 114 ariGVVPQFDNLDLEF---TVRENLlvfgrYFGMSTREIEAVIPSLLEFARLE----------SKADARVSDLSGGMKRR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 603 LAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAH----------RLSTVRGAHRIivmADGR 669
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHfmeeaerlcdRLCVLEAGRKI---AEGR 255
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
469-693 |
9.69e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.58 E-value: 9.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL--ERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPV---- 542
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVeipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 ----LFGTTIMENIR-FGKLAASDEEVYAAAREANAHefITSFPEGYNTIVGERGttLSGGQKQRLAIARALIKQPTVLI 617
Cdd:PRK09580 93 vsnqFFLQTALNAVRsYRGQEPLDRFDFQDLMEEKIA--LLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 618 LDEATSALDAESERVVQEALDRASAG-RTVLVIAHR---LSTVRGAHrIIVMADGRVWEAGTH---EELLKKGglYAELI 690
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHYqriLDYIKPDY-VHVLYQGRIVKSGDFtlvKQLEEQG--YGWLT 245
|
...
gi 109068902 691 RRQ 693
Cdd:PRK09580 246 EQQ 248
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
469-669 |
1.06e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.93 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYdPTA---GVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLF- 544
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAGIVIIHQELTLVp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 545 GTTIMENIRFG-KLAASDEEVYAAAREANAHEFI--TSFPEGYNT-IVGERGttlsGGQKQRLAIARALIKQPTVLILDE 620
Cdd:TIGR02633 92 ELSVAENIFLGnEITLPGGRMAYNAMYLRAKNLLreLQLDADNVTrPVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 109068902 621 ATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIVMADGR 669
Cdd:TIGR02633 168 PSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
454-679 |
1.11e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.79 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 454 SVTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLlERFydpTAGVVMLDGRDLRTLDPSwL 529
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTllrmVAGL-ERI---TSGEIWIGGRVVNELEPA-D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 530 RGQVVGFisQEPVLF-GTTIMENI-------RFGKlAASDEEVYAAAREANAHEFITSFPEgyntivgergtTLSGGQKQ 601
Cdd:PRK11650 76 RDIAMVF--QNYALYpHMSVRENMayglkirGMPK-AEIEERVAEAARILELEPLLDRKPR-----------ELSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 602 RLAIARALIKQPTVLILDEATSALDAE---SERVVQEALDRaSAGRTVLVIAH-RLSTVRGAHRIIVMADGRVWEAGTHE 677
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDAKlrvQMRLEIQRLHR-RLKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPV 220
|
..
gi 109068902 678 EL 679
Cdd:PRK11650 221 EV 222
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
181-397 |
1.32e-11 |
|
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: 66.07 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 181 LLILYGVQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLttdvQEFKSSFKLVISQGLRSC 260
Cdd:cd18566 48 VVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL----NSLEQIREFLTGQALLAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 261 TQVAGCLVSLSM---LSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREE 337
Cdd:cd18566 124 LDLPFVLIFLGLiwyLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQML 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 338 ERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSF 397
Cdd:cd18566 204 RRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIAC 263
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
473-663 |
1.53e-11 |
|
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: 65.33 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 473 LKDFTLTLPPGKIVALVGQSGGGKTT---------VASLLERFYDPTAGVVMLDGrdLRTLDpswlrgQVVgFISQEPVl 543
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSlindtlypaLARRLHLKKEQPGNHDRIEG--LEHID------KVI-VIDQSPI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 544 fGTT----------IMENIR--F-------------------GK-----LAASDEEvyaaareanAHEFITSFPE----- 582
Cdd:cd03271 81 -GRTprsnpatytgVFDEIRelFcevckgkrynretlevrykGKsiadvLDMTVEE---------ALEFFENIPKiarkl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 583 --------GYNTIvGERGTTLSGGQKQRLAIARALIKQ---PTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIA 650
Cdd:cd03271 151 qtlcdvglGYIKL-GQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIE 229
|
250
....*....|...
gi 109068902 651 HRLSTVRGAHRII 663
Cdd:cd03271 230 HNLDVIKCADWII 242
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
482-670 |
1.62e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 62.78 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 482 PGKIVALVGQSGGGKTTVASLLERFYDPT-AGVVMLDGRDLRTLDPSWLRgqvvgfisqepvlfgttimenirfgklaas 560
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 561 deevyaaareanahefitsfpegyNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD-- 638
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180 190
....*....|....*....|....*....|....*..
gi 109068902 639 -----RASAGRTVLVIAHRLSTVRGAHrIIVMADGRV 670
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPAL-LRRRFDRRI 142
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
470-656 |
1.81e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.83 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGQVVgFISQEPVLFG 545
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKH-YRGDVV-YNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 546 T-TIMENIRFGKLAAS--------DEEVYAAaREANAHEFITSFPEGYNTIVGE---RGttLSGGQKQRLAIARALIKQP 613
Cdd:TIGR00956 152 HlTVGETLDFAARCKTpqnrpdgvSREEYAK-HIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGA 228
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 109068902 614 TVLILDEATSALDAEServvqeALDRASAGRTVLVIAHRLSTV 656
Cdd:TIGR00956 229 KIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLV 265
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
447-678 |
1.99e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.27 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 447 PKEHLRGSVT-FQNVCFSYPCRPGFEvlkDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML--------- 516
Cdd:TIGR03719 314 PGPRLGDKVIeAENLTKAFGDKLLID---DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayv 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 517 -DGRDlrTLDPS---WlrgqvvgfisqEPVLFGTTImenIRFGKlaasdeevyaaaREANAHEFITSFpegyN------- 585
Cdd:TIGR03719 391 dQSRD--ALDPNktvW-----------EEISGGLDI---IKLGK------------REIPSRAYVGRF----Nfkgsdqq 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 586 TIVGErgttLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDrASAGrTVLVIAH------RLSTvrga 659
Cdd:TIGR03719 439 KKVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL-NFAG-CAVVISHdrwfldRIAT---- 508
|
250 260
....*....|....*....|
gi 109068902 660 HRIIVMADGRV-WEAGTHEE 678
Cdd:TIGR03719 509 HILAFEGDSHVeWFEGNFSE 528
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
476-696 |
4.47e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.80 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 476 FTLTLPPGKIVALVGQSGGGKTT----VASLLerfydPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFgttIMEN 551
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTllarMAGLL-----PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPF---AMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 552 IRFGKLAASDEEVYAAAREAnAHEFITSFpeGYNTIVGERGTTLSGGQKQR-------LAIARALIKQPTVLILDEATSA 624
Cdd:PRK03695 87 FQYLTLHQPDKTRTEAVASA-LNEVAEAL--GLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 625 LDaeserVVQE-ALDR-----ASAGRTVLVIAHRLS-TVRGAHRIIVMADGRVWEAGTHEELLKKGGL---YAELIRRQA 694
Cdd:PRK03695 164 LD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENLaqvFGVNFRRLD 238
|
..
gi 109068902 695 LD 696
Cdd:PRK03695 239 VE 240
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
467-663 |
5.88e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.51 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 467 RPGFEVLkDFTLTlpPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLR-----GQVVGFisqEP 541
Cdd:PRK13538 14 RILFSGL-SFTLN--AGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdllylGHQPGI---KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 542 VLfgtTIMENIRFgKLAASDEEVYAAAREANAHefitsfpegyntiVGERGT------TLSGGQKQRLAIARALIKQPTV 615
Cdd:PRK13538 88 EL---TALENLRF-YQRLHGPGDDEALWEALAQ-------------VGLAGFedvpvrQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 109068902 616 LILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHR-LSTVRGAHRII 663
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTHQdLPVASDKVRKL 200
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
477-680 |
1.02e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.67 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 477 TLTLPPGKIVALVGQSGGGKTTVASLL----ERFYDPTAGVVMLDGRDLRTLDPSWLR---GQVVGFISQEP-------V 542
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRklvGHNVSMIFQEPqscldpsE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 LFGTTIMENI-----------RFGKLAASDEEVYAAAREANAHEFITSFPegyntivgergTTLSGGQKQRLAIARALIK 611
Cdd:PRK15093 107 RVGRQLMQNIpgwtykgrwwqRFGWRKRRAIELLHRVGIKDHKDAMRSFP-----------YELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 612 QPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEELL 680
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRlnQNNNTTILLISHDLQMLsQWADKINVLYCGQTVETAPSKELV 247
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
181-397 |
1.02e-10 |
|
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: 63.30 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 181 LLILYGVQGLLTF--GYLVLlsHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLT--TDVQEFKSSfkLVISqG 256
Cdd:cd18555 48 ILILFLLYGLFSFlrGYIII--KLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRANsnVYIRQILSN--QVIS-L 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 257 LRSCTQVAGCLVSLSMLSTRLTLLLMVATpALMGVGTLMGSG-LRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQR 335
Cdd:cd18555 123 IIDLLLLVIYLIYMLYYSPLLTLIVLLLG-LLIVLLLLLTRKkIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKN 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 336 E----EERYGAELEAcrcrAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSF 397
Cdd:cd18555 202 IykkwENLFKKQLKA----FKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAF 263
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
453-651 |
1.77e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 453 GSVTF--QNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLdGRDLR-------- 522
Cdd:PRK11147 316 GKIVFemENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEvayfdqhr 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 523 -TLDPSwlrgqvvgfisqepvlfgTTIMENIRFGKlaasdEEVYAAAREANAHEFITSF---PEGYNTIVgergTTLSGG 598
Cdd:PRK11147 392 aELDPE------------------KTVMDNLAEGK-----QEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGG 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 109068902 599 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAgrTVLVIAH 651
Cdd:PRK11147 445 ERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQG--TVLLVSH 495
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
181-405 |
1.88e-10 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 62.52 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 181 LLILYGVQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRlttdVQEFKSSFKLVISQGLRSC 260
Cdd:cd18588 48 LLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVAR----VRELESIRQFLTGSALTLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 261 TQVAGCLVSLSML---STRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREE 337
Cdd:cd18588 124 LDLVFSVVFLAVMfyySPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQ 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 338 ERYGAELeacrcrAEELGRGIALfQGLSNIAFN-------CMVLGTLFIGGSLVAGQQLTGGDLMSF-LVASQTVQ 405
Cdd:cd18588 204 RRWEELL------ARYVKASFKT-ANLSNLASQivqliqkLTTLAILWFGAYLVMDGELTIGQLIAFnMLAGQVSQ 272
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
455-679 |
2.84e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.70 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPGFEvlkDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--Q 532
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFD---NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 533 VVGFISQEPVLF-GTTIMENIRFgklaasdeevyaAAREanaHefiTSFPEG--YNTI------VGERG------TTLSG 597
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAY------------PLRE---H---TQLPAPllHSTVmmkleaVGLRGaaklmpSELSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 598 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAG 674
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISElnSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHG 226
|
....*
gi 109068902 675 THEEL 679
Cdd:PRK11831 227 SAQAL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
473-651 |
3.43e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.26 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 473 LKDFTLTLPPGKI-----VALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswlrgqvvgfISQEPvlfgtt 547
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-----------------ISYKP------ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 548 imENIRfgklAASDEEVYAAAREANAHEFITSFpegYNTIVGER----------GTTLSGGQKQRLAIARALIKQPTVLI 617
Cdd:COG1245 408 --QYIS----PDYDGTVEEFLRSANTDDFGSSY---YKTEIIKPlgleklldknVKDLSGGELQRVAIAACLSRDADLYL 478
|
170 180 190
....*....|....*....|....*....|....*..
gi 109068902 618 LDEATSALDAEsERV-VQEALDR--ASAGRTVLVIAH 651
Cdd:COG1245 479 LDEPSAHLDVE-QRLaVAKAIRRfaENRGKTAMVVDH 514
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
468-651 |
4.50e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 468 PGFEVLKDFTLTLPPG-KIvALVGQSGGGKTTVASLLerfydptAGVvmldgrdlrtlDPS-----WLR-GQVVGFISQE 540
Cdd:PRK11819 18 PKKQILKDISLSFFPGaKI-GVLGLNGAGKSTLLRIM-------AGV-----------DKEfegeaRPApGIKVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 541 PVLFGT-TIMENIRFG---KLAASDE--EVYAA-----------ARE----------ANAHEfITS----------FPEG 583
Cdd:PRK11819 79 PQLDPEkTVRENVEEGvaeVKAALDRfnEIYAAyaepdadfdalAAEqgelqeiidaADAWD-LDSqleiamdalrCPPW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 584 yNTIVgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES----ERVVQEaldraSAGrTVLVIAH 651
Cdd:PRK11819 158 -DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlEQFLHD-----YPG-TVVAVTH 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
471-670 |
5.30e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.38 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS--WLRG--------QVVGFISQE 540
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqrLARGlvylpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 541 PVLFGT-TIMEN-----IRFGKLAASDEEVYAAAREANAHEfitsfpegyNTIVGergtTLSGGQKQRLAIARALIKQPT 614
Cdd:PRK15439 357 PLAWNVcALTHNrrgfwIKPARENAVLERYRRALNIKFNHA---------EQAAR----TLSGGNQQKVLIAKCLEASPQ 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 615 VLILDEATSALDAeSER--VVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRV 670
Cdd:PRK15439 424 LLIVDEPTRGVDV-SARndIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
135-428 |
5.71e-10 |
|
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: 61.28 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 135 IVLALGAALVNVQIPLLLgqlvEIVAKYTRDHV--GSFMTESRKLStHLLILYGVQGLLtfgYLVL----------LSH- 201
Cdd:cd18554 1 IIITIVIGLVRFGIPLLL----PLILKYIVDDViqGSSLTLDEKVY-KLFTIIGIMFFI---FLILrppveyyrqyFAQw 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 202 IGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLL 281
Cdd:cd18554 73 IANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 282 MVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALF 361
Cdd:cd18554 153 LVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKT 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 362 QGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18554 233 FSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
181-412 |
9.02e-10 |
|
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: 60.30 E-value: 9.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 181 LLILYGVQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRL--TTDVQEFkssfklVISQGLR 258
Cdd:cd18782 48 MLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIseLDTIRGF------LTGTALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 259 SCTQVA---GCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAME-- 333
Cdd:cd18782 122 TLLDVLfsvIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAElk 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 334 --QREEERYGAELEAcrcrAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANL 411
Cdd:cd18782 202 arWRWQNRYARSLGE----GFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRL 277
|
.
gi 109068902 412 S 412
Cdd:cd18782 278 S 278
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
473-668 |
1.29e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 58.10 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 473 LKDFTLTLPPGKIVALVGQSGGGKTTVasLLERFYdpTAGVVMLDGrDLRTLDPSWLrgqvvgfisqepvlfgttimenI 552
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLIS-FLPKFSRNKL----------------------I 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 553 RFGKLaasdeevyaaareanahEFITSFPEGYNTIvGERGTTLSGGQKQRLAIARALIKQP--TVLILDEATSALDAESE 630
Cdd:cd03238 64 FIDQL-----------------QFLIDVGLGYLTL-GQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 109068902 631 RVVQEALDR-ASAGRTVLVIAHRLSTVRGAHRIIVMADG 668
Cdd:cd03238 126 NQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
452-685 |
1.29e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 452 RGSVTFQNVCFSYPCRPGFevlKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVmldgrdlrtldpSWLRG 531
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLF---KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSEN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 532 QVVGFISQEPVL-F--GTTIME-------------NIR--FGKLAASDEEVYAAAReanahefitsfpegyntivgergt 593
Cdd:PRK15064 382 ANIGYYAQDHAYdFenDLTLFDwmsqwrqegddeqAVRgtLGRLLFSQDDIKKSVK------------------------ 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 594 TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAgrTVLVIAHRLSTVRG-AHRII-VMADGRVW 671
Cdd:PRK15064 438 VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSHDREFVSSlATRIIeITPDGVVD 515
|
250
....*....|....
gi 109068902 672 EAGTHEELLKKGGL 685
Cdd:PRK15064 516 FSGTYEEYLRSQGI 529
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
473-651 |
2.58e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 473 LKDFTLTLPPGKI-----VALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswlrgqvvgfISQEPvlfgtt 547
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-----------------ISYKP------ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 548 imENIRfgklAASDEEVYAAAREANAhEFITSF-------PEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDE 620
Cdd:PRK13409 407 --QYIK----PDYDGTVEDLLRSITD-DLGSSYykseiikPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 479
|
170 180 190
....*....|....*....|....*....|...
gi 109068902 621 ATSALDAESERVVQEALDRASAGR--TVLVIAH 651
Cdd:PRK13409 480 PSAHLDVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
471-690 |
2.93e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 59.33 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLErfydPTAGVVMLDGRDlrtldPSWLRGQVVGFISqepVLFGT 546
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILV----PTSGEVRVLGYV-----PFKRRKEFARRIG---VVFGQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 --------TIMENIRFGKlaasdeEVY---AAAREANAHEF-----ITSFpegYNTIVgeRgtTLSGGQKQRLAIARALI 610
Cdd:COG4586 104 rsqlwwdlPAIDSFRLLK------AIYripDAEYKKRLDELvelldLGEL---LDTPV--R--QLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 611 KQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHRIIVMADGRVWEAGTHEELLKKGGLYA 687
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIeALCDRVIVIDHGRIIYDGSLEELKERFGPYK 250
|
...
gi 109068902 688 ELI 690
Cdd:COG4586 251 TIV 253
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
473-684 |
3.17e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.52 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 473 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLerfydptAGV-------VMLDGRDLRtlDPSWlRGQVVGFISQEPV--- 542
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGArkiqqgrVEVLGGDMA--DARH-RRAVCPRIAYMPQglg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 --LFGT-TIMENIRF-GKLAASDeevyAAAREANAHEFITS-----FPE---GyntivgergtTLSGGQKQRLAIARALI 610
Cdd:NF033858 87 knLYPTlSVFENLDFfGRLFGQD----AAERRRRIDELLRAtglapFADrpaG----------KLSGGMKQKLGLCCALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 611 KQPTVLILDEATSALDAESERVVQEALDRASAGR---TVLVI------AHRLstvrgaHRIIVMADGRVWEAGTHEELLK 681
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVAtaymeeAERF------DWLVAMDAGRVLATGTPAELLA 226
|
...
gi 109068902 682 KGG 684
Cdd:NF033858 227 RTG 229
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
473-651 |
3.29e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.19 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 473 LKDFTLTLPPG-----KIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDlrtldpswlrgqvVGFISQEPVLFGTT 547
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-------------VSYKPQYIKADYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 548 IMENIRFGKLAASDEEVYAAAREANahefitsfPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDA 627
Cdd:cd03237 77 TVRDLLSSITKDFYTHPYFKTEIAK--------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180
....*....|....*....|....*.
gi 109068902 628 ESERVVQEALDR--ASAGRTVLVIAH 651
Cdd:cd03237 149 EQRLMASKVIRRfaENNEKTAFVVEH 174
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
573-679 |
3.54e-09 |
|
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: 60.41 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 573 AHEFITSFPE-------------GYNTIvGERGTTLSGGQKQRLAIARALIKQ---PTVLILDEATSALDAESERVVQEA 636
Cdd:TIGR00630 796 AYEFFEAVPSisrklqtlcdvglGYIRL-GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEV 874
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 109068902 637 LDR-ASAGRTVLVIAHRLSTVRGAHRIIVM------ADGRVWEAGTHEEL 679
Cdd:TIGR00630 875 LQRlVDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
476-670 |
4.94e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 476 FTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlRGQVVGFI-------SQEPVLFGTTI 548
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSP---RDAIRAGImlcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 549 MENI---------RFGKLAASDEEvyaaarEANAHEFITSF----PEGYNTIVgergtTLSGGQKQRLAIARALIKQPTV 615
Cdd:PRK11288 349 ADNInisarrhhlRAGCLINNRWE------AENADRFIRSLniktPSREQLIM-----NLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 616 LILDEATSALD--AESErVVQEALDRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRV 670
Cdd:PRK11288 418 ILLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRI 474
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
471-684 |
1.05e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.09 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERfyDPTAGVVMLDGRdlrtldpswlrgqVVGFISQEPV---LFGTT 547
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-------------ISGFPKKQETfarISGYC 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 548 IMENIRFGKLAASDEEVYAA----AREANAHE---FITSFPEGY------NTIVGERGTT-LSGGQKQRLAIARALIKQP 613
Cdd:PLN03140 959 EQNDIHSPQVTVRESLIYSAflrlPKEVSKEEkmmFVDEVMELVeldnlkDAIVGLPGVTgLSTEQRKRLTIAVELVANP 1038
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109068902 614 TVLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTvrgahriivmadgRVWEAGTHEELLKKGG 684
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI-------------DIFEAFDELLLMKRGG 1097
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
447-670 |
2.01e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 447 PKE-HLRGSVTFQ--NVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKT-TVASLLERFYDPTAGVVMLDGRDLR 522
Cdd:PRK13549 249 PREpHTIGEVILEvrNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 523 TLDPSWLRGQVVGFISQEPVLFG-TTIM---ENI------RFGKLAASDEevyaAAREANAHEFI------TSFPEgynt 586
Cdd:PRK13549 329 IRNPQQAIAQGIAMVPEDRKRDGiVPVMgvgKNItlaaldRFTGGSRIDD----AAELKTILESIqrlkvkTASPE---- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 587 ivgERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD----AESERVVQEAldrASAGRTVLVIAHRLSTVRG-AHR 661
Cdd:PRK13549 401 ---LAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakYEIYKLINQL---VQQGVAIIVISSELPEVLGlSDR 474
|
....*....
gi 109068902 662 IIVMADGRV 670
Cdd:PRK13549 475 VLVMHEGKL 483
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
447-670 |
2.80e-08 |
|
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: 56.76 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 447 PKE-HLRGSVTFQ--NVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKT-TVASLLERFYDPTAGVVMLDGRDLR 522
Cdd:TIGR02633 247 PHEpHEIGDVILEarNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 523 TLDPS-WLRGQVV---------GFISQEPVLFGTTIMENIRFGKLAASDE--EVYAAAREANAHEFITSFPegYNTIvge 590
Cdd:TIGR02633 327 IRNPAqAIRAGIAmvpedrkrhGIVPILGVGKNITLSVLKSFCFKMRIDAaaELQIIGSAIQRLKVKTASP--FLPI--- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 591 rgTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHRIIVMADG 668
Cdd:TIGR02633 402 --GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEG 479
|
..
gi 109068902 669 RV 670
Cdd:TIGR02633 480 KL 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
583-686 |
3.56e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 583 GYNTIVGergtTLSGGQKQRLAIARALIKQPTVLILDEATSALD--AESErVVQEALDRASAGRTVLVIAHRLSTVRG-A 659
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKFE-IYQLIAELAKKDKGIIIISSEMPELLGiT 458
|
90 100 110
....*....|....*....|....*....|....
gi 109068902 660 HRIIVMADGRVweAG-------THEELLKKGGLY 686
Cdd:PRK10982 459 DRILVMSNGLV--AGivdtkttTQNEILRLASLH 490
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
470-701 |
4.21e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.21 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGfisqepvlfgttiM 549
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTG-------------I 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 550 ENIRFGKLAA--SDEEVYAAARE----ANAHEFITSFPEGYntivgergttlSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:PRK13546 104 ENIEFKMLCMgfKRKEIKAMTPKiiefSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 624 ALDaesERVVQEALDR----ASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELLKKgglYAELIR------- 691
Cdd:PRK13546 173 VGD---QTFAQKCLDKiyefKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK---YEAFLNdfkkksk 246
|
250
....*....|....*.
gi 109068902 692 ------RQALDAPRTV 701
Cdd:PRK13546 247 aeqkefRNKLDESRFV 262
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
455-659 |
5.91e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 53.34 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRpgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLrgqvv 534
Cdd:PRK13541 2 LSLHQLQFNIEQK----NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GFISQEPVL-FGTTIMENIRF-GKLAASDEEVYAAAREANAHEFITsfpegyntivgERGTTLSGGQKQRLAIARALIKQ 612
Cdd:PRK13541 73 TYIGHNLGLkLEMTVFENLKFwSEIYNSAETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQ 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 109068902 613 PTVLILDEATSALDAESERVVQEALD-RASAGRTVLVIAHRLSTVRGA 659
Cdd:PRK13541 142 SDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSA 189
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
455-651 |
5.95e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYpcrpGFEVL-KDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML----------DGRDlrT 523
Cdd:PRK11819 325 IEAENLSKSF----GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvklayvdQSRD--A 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 524 LDPSwlrgqvvgfisqepvlfgTTIMENIrfgklaaSD--EEVYAAAREANAHEFITSFpegyntivGERGT-------T 594
Cdd:PRK11819 399 LDPN------------------KTVWEEI-------SGglDIIKVGNREIPSRAYVGRF--------NFKGGdqqkkvgV 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 109068902 595 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDrASAGrTVLVIAH 651
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL-EFPG-CAVVISH 500
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
130-411 |
9.61e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 54.39 E-value: 9.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 130 ALGVAIVLALGAALVNVQIPLLLgQLV--EIVAKYTRDhvgsFMTesrKLSTHLLILYGVQGLLTF--GYLVLlsHIGER 205
Cdd:cd18567 3 ALLQILLLSLALELFALASPLYL-QLVidEVIVSGDRD----LLT---VLAIGFGLLLLLQALLSAlrSWLVL--YLSTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 206 MAVDMRRALFSSLLRQDIAFFDANKTGQLVSRL--TTDVQEFkssfklvISQGLrsctqVAG------CLVSLSML---S 274
Cdd:cd18567 73 LNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFgsLDEIQQT-------LTTGF-----VEAlldglmAILTLVMMflyS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 275 TRLTLLLMVATPALMGVGTLMgsgLRKLSRQCQEQI---ARAMGVADEALGNVRTVRAFameQREEERYGAELEAcrcRA 351
Cdd:cd18567 141 PKLALIVLAAVALYALLRLAL---YPPLRRATEEQIvasAKEQSHFLETIRGIQTIKLF---GREAEREARWLNL---LV 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 352 EELGRGI------ALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANL 411
Cdd:cd18567 212 DAINADIrlqrlqILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSL 277
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
133-390 |
1.72e-07 |
|
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: 53.26 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 133 VAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHVgsfmtesrklsTHLLILYGVQGLLTFGYLVLLSH---IGERMAVD 209
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPL-----------SEGYLLALALFLVSLLQSLLLHQyffLSFRLGMR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 210 MRRALFSSL----LRQDIAFFDANKTGQLVSRLTTDVQEFKSSFkLVISQGLRSCTQVAGCLVSLSML---STRLTLLLM 282
Cdd:cd18579 70 VRSALSSLIyrkaLRLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALYLLYRLlgwAALAGLGVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 283 VatpALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMeqreEERYGAELEAcrCRAEELG--RGIAL 360
Cdd:cd18579 149 L---LLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAW----EKPFLKRIEE--LRKKELKalRKFGY 219
|
250 260 270
....*....|....*....|....*....|..
gi 109068902 361 FQGLSNIAFNCM-VLGTLFIGGSLVA-GQQLT 390
Cdd:cd18579 220 LRALNSFLFFSTpVLVSLATFATYVLlGNPLT 251
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
594-653 |
3.17e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 3.17e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109068902 594 TLSGGQKQRLAIARALIKQPTVLILDEATSALDAEsERV-VQEALDRASAGRTVLVIAHRL 653
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDL 271
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
594-655 |
4.15e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.25 E-value: 4.15e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 594 TLSGGQKQRLAIARALIKQPTVLILDEATSALD----AESERVVQEAldrASAGRTVLVIAHRLST 655
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAI 274
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
459-652 |
4.21e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.10 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 459 NVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRGQV--VGF 536
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLcfVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 537 ISQ-EPVLfgtTIMENIRFgklaasdeEVYAAAREANAHEFITSFPEGYntIVGERGTTLSGGQKQRLAIARALIKQPTV 615
Cdd:PRK13540 82 RSGiNPYL---TLRENCLY--------DIHFSPGAVGITELCRLFSLEH--LIDYPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 109068902 616 LILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHR 652
Cdd:PRK13540 149 WLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
482-684 |
5.08e-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: 53.48 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 482 PGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVVGFISQEPVLfgttimenirfGKLAASD 561
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVH-QNMGYCPQFDAI-----------DDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 562 EEVYAAAR---------EANAHEFITSFpeGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERV 632
Cdd:TIGR01257 2031 EHLYLYARlrgvpaeeiEKVANWSIQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 109068902 633 VQEAL-DRASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELLKKGG 684
Cdd:TIGR01257 2109 LWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
571-684 |
6.65e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 571 ANAHEFITSFpeGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVV-QEALDRASAGRTVLVI 649
Cdd:NF000106 123 ARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLT 200
|
90 100 110
....*....|....*....|....*....|....*.
gi 109068902 650 AHRLSTVRG-AHRIIVMADGRVWEAGTHEELLKKGG 684
Cdd:NF000106 201 TQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
593-681 |
8.96e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 52.34 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 593 TTLSGGQKQRLAIARALIK---QPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRGAHRIIvmaD- 667
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRlVDKGNTVVVIEHNLDVIKTADWII---Dl 901
|
90 100
....*....|....*....|..
gi 109068902 668 --------GRVWEAGTHEELLK 681
Cdd:COG0178 902 gpeggdggGEIVAEGTPEEVAK 923
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
455-670 |
9.80e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 455 VTFQNVCFSYPCRPgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMldgRDLRTLDPSWLRGQVV 534
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---RSAKVRMAVFSQHHVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 535 GF-ISQEPVLFgttIMEnirfgklaasdeeVYAAAREANAHEFITSFPEGYNTIVgERGTTLSGGQKQRLAIARALIKQP 613
Cdd:PLN03073 584 GLdLSSNPLLY---MMR-------------CFPGVPEQKLRAHLGSFGVTGNLAL-QPMYTLSGGQKSRVAFAKITFKKP 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 109068902 614 TVLILDEATSALDAESERVVQEALDRASAGrtVLVIAHRLSTVRGA-HRIIVMADGRV 670
Cdd:PLN03073 647 HILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKV 702
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
459-669 |
1.10e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 459 NVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGR--DLRTLDPSWLRGqvVGF 536
Cdd:PRK10982 3 NISKSFP---GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSKEALENG--ISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 537 ISQE-PVLFGTTIMENIRFGK-----LAASDEEVYaaaREANAhefitSFPE-GYNTIVGERGTTLSGGQKQRLAIARAL 609
Cdd:PRK10982 78 VHQElNLVLQRSVMDNMWLGRyptkgMFVDQDKMY---RDTKA-----IFDElDIDIDPRAKVATLSVSQMQMIEIAKAF 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 610 IKQPTVLILDEATSALdAESE-----RVVQEALDRasaGRTVLVIAHRLSTV-RGAHRIIVMADGR 669
Cdd:PRK10982 150 SYNAKIVIMDEPTSSL-TEKEvnhlfTIIRKLKER---GCGIVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
465-670 |
1.27e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 465 PCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVA-SLLERFYDP-TAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPV 542
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 543 LFGTTIMENIRFGKLAASDEEVyAAAREANAHEFITSfPEGYNT---I----VGERGTTLSGGQKQRLAIARALIKQPTV 615
Cdd:NF040905 348 GYGLNLIDDIKRNITLANLGKV-SRRGVIDENEEIKV-AEEYRKkmnIktpsVFQKVGNLSGGNQQKVVLSKWLFTDPDV 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 616 LILDEATSALD--AESE--RVVQEAldrASAGRTVLVIAHRLSTVRG-AHRIIVMADGRV 670
Cdd:NF040905 426 LILDEPTRGIDvgAKYEiyTIINEL---AAEGKGVIVISSELPELLGmCDRIYVMNEGRI 482
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
595-669 |
1.31e-06 |
|
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: 51.67 E-value: 1.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 595 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRasAGRTVLVIAHRLSTVRgAHRIIVMADGR 669
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKSLWK-YHEYLLYMDGR 654
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
593-708 |
1.75e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 593 TTLSGGQKQRLAIARALI---KQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMA-- 666
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGpe 887
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 109068902 667 ----DGRVWEAGTHEELLKKGGLYAELIR---RQALDAPRTVAPPPKKP 708
Cdd:PRK00635 888 ggnlGGYLLASCSPEELIHLHTPTAKALRpylSSPQELPYLPDPSPKPP 936
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
595-656 |
2.00e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 2.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 595 LSGGQkQRLA-IARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLV------------IAHRLSTV 656
Cdd:PRK10938 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacITHRLEFV 476
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
177-395 |
2.43e-06 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 49.91 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 177 LSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTdVQEFKSSFKLVisqG 256
Cdd:cd18586 44 LTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELPLESRPSGYWQQLLRDLDT-LRNFLTGPSLF---A 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 257 LRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQRE 336
Cdd:cd18586 120 FFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNL 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 109068902 337 EERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLM 395
Cdd:cd18586 200 RRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGELTIGALI 258
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
133-340 |
3.46e-06 |
|
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: 49.42 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 133 VAIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHVGSFmtesrkLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDMRR 212
Cdd:cd18580 3 LLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYY------LGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 213 ALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTrltlLLMVATPALMGVG 292
Cdd:cd18580 77 KLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP----YFLIVLPPLLVVY 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 109068902 293 TLMGSGLRKLSRQCQ--EQIARA--MGVADEALGNVRTVRAFAMEQREEERY 340
Cdd:cd18580 153 YLLQRYYLRTSRQLRrlESESRSplYSHFSETLSGLSTIRAFGWQERFIEEN 204
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
478-704 |
4.24e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 478 LTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAG--------VVMLDGRDLRTL-DPSWLRGQVvGFISQEPVLFGTTI 548
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshITRLSFEQLQKLvSDEWQRNNT-DMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 549 MENIRfgklaasdEEVYAAAReanAHEFITSFpeGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE 628
Cdd:PRK10938 103 AEIIQ--------DEVKDPAR---CEQLAQQF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 629 SERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHRIIVMADGRVWEAGTHEELLKKgGLYAELIRRQALDA---PRTVAP 703
Cdd:PRK10938 170 SRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ-ALVAQLAHSEQLEGvqlPEPDEP 248
|
.
gi 109068902 704 P 704
Cdd:PRK10938 249 S 249
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
595-654 |
6.57e-06 |
|
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: 48.13 E-value: 6.57e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 595 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESE----RVVQEaldRASAGRTVLVIAHRLS 654
Cdd:cd03236 140 LSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaaRLIRE---LAEDDNYVLVVEHDLA 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
475-626 |
6.71e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 475 DFT------LTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML-----DGRDLRTldpswlRgQVVGFISQEPVL 543
Cdd:NF033858 278 DFTavdhvsFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDIAT------R-RRVGYMSQAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 544 FGT-TIMENIrfgKLAASDEEVYAAAREANAHEFITSFpeGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 622
Cdd:NF033858 351 YGElTVRQNL---ELHARLFHLPAAEIAARVAEMLERF--DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
....
gi 109068902 623 SALD 626
Cdd:NF033858 426 SGVD 429
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
595-653 |
8.45e-06 |
|
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: 46.80 E-value: 8.45e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109068902 595 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAS--AGRTVLVIAHRL 653
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDL 132
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
474-681 |
9.49e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 474 KDFTLTLPPGKIVALVGQSGGGKTtvaSLLERFY--DPTA-GVVMLDGRDLRTLDPSWLRGQVVGFISQ---EPVLFGT- 546
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISPRSPLDAVKKGMAYITEsrrDNGFFPNf 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 547 TIMENI---RFGKLAA----------SDEEVYAAAREANAHEFITSfpegyntiVGERGTTLSGGQKQRLAIARALIKQP 613
Cdd:PRK09700 357 SIAQNMaisRSLKDGGykgamglfheVDEQRTAENQRELLALKCHS--------VNQNITELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 614 TVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRGA-HRIIVMADGRV------WEAGTHEELLK 681
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLtqiltnRDDMSEEEIMA 504
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
134-399 |
1.55e-05 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 47.22 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 134 AIVLALGAALVNVQIPLLLGQLVEIVAKYTRDHVGSFMTesrklsthLLILYGVQGLL--TFGYL--VLLSHIGERMAVD 209
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDLESAVT--------LILLYALLRFSskLLKELrsLLYRRVQQNAYRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 210 MRRALFSSLLRQDIAFFDANKTGQLVS---RLTTDVQEFKSSFKLVISQGLRSCtqVAGCLVSLSMLSTRLTLLLMVATp 286
Cdd:cd18560 73 LSLKTFAHLHSLSLDWHLSKKTGEVVRimdRGTESANTLLSYLVFYLVPTLLEL--IVVSVVFAFHFGAWLALIVFLSV- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 287 ALMGVGTLMGSGLR-KLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEAcrcrAEELGRGIALFQGLS 365
Cdd:cd18560 150 LLYGVFTIKVTEWRtKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKE----YQKSSVKVQASLSLL 225
|
250 260 270
....*....|....*....|....*....|....*...
gi 109068902 366 NIA----FNCMVLGTLFIGGSLVAGQQLTGGDLMSFLV 399
Cdd:cd18560 226 NVGqqliIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNT 263
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
473-676 |
1.62e-05 |
|
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: 46.87 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 473 LKDFTLTLPPGKIVALVGQSGGGKTTVA-----------------SLLERFYD--PTAGVVMLDGrdlrtLDPSWLRGQv 533
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsAYARQFLGqmDKPDVDSIEG-----LSPAIAIDQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 534 vGFISQEPVLFGTTIMENIRFGKLaasdeeVYAAAREANAHEFITSFPEGYNTiVGERGTTLSGGQKQRLAIARALIKQP 613
Cdd:cd03270 85 -KTTSRNPRSTVGTVTEIYDYLRL------LFARVGIRERLGFLVDVGLGYLT-LSRSAPTLSGGEAQRIRLATQIGSGL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 614 T--VLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRGAHRIIVMADGrvweAGTH 676
Cdd:cd03270 157 TgvLYVLDEPSIGLHPRDNDRLIETLKRlRDLGNTVLVVEHDEDTIRAADHVIDIGPG----AGVH 218
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
477-651 |
1.85e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.16 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 477 TLTLPPGkIVALVGQSGGGKTTVASLLER-FYDPTAGVVMLDgRDLRTLDPS------------------WLRGQVVGFI 537
Cdd:COG0419 18 TIDFDDG-LNLIVGPNGAGKSTILEAIRYaLYGKARSRSKLR-SDLINVGSEeasvelefehggkryrieRRQGEFAEFL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 538 SQEP--------VLFGTTIMENI--RFGKLAASDEEVYAAAREANA-HEFITSFPEGYNTIvgergTTLSGGQKQRLAIA 606
Cdd:COG0419 96 EAKPserkealkRLLGLEIYEELkeRLKELEEALESALEELAELQKlKQEILAQLSGLDPI-----ETLSGGERLRLALA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 109068902 607 RALikqptVLILDeaTSALDAESERVVQEALDRASagrtvlVIAH 651
Cdd:COG0419 171 DLL-----SLILD--FGSLDEERLERLLDALEELA------IITH 202
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
181-418 |
2.52e-05 |
|
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: 46.74 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 181 LLILYGVQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRL--TTDVQEFkssfklVISQGLR 258
Cdd:cd18783 48 VVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMqqIERIRQF------LTGQLFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 259 SCTQVAGCLVSLSML---STRLTLLLMVATPALMG-VGTLMGSGLRKLSRQCQEQIAR-AMGVadEALGNVRTVRAFAME 333
Cdd:cd18783 122 TLLDATSLLVFLPVLffySPTLALVVLAFSALIALiILAFLPPFRRRLQALYRAEGERqAFLV--ETVHGIRTVKSLALE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 334 QREEERYGAEL-EACRcRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLS 412
Cdd:cd18783 200 PRQRREWDERVaRAIR-ARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLA 278
|
....*.
gi 109068902 413 VLFGQV 418
Cdd:cd18783 279 GLVQEY 284
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
583-686 |
2.77e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.76 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 583 GYNTiVGERGTTLSGGQKQRLAIARALIKQPT---VLILDEATSALDAESER----VVQEALDRasaGRTVLVIAHRLST 655
Cdd:PRK00349 820 GYIK-LGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRklleVLHRLVDK---GNTVVVIEHNLDV 895
|
90 100 110
....*....|....*....|....*....|....*..
gi 109068902 656 VRGAHRIIVM------ADGRVWEAGTHEELLKKGGLY 686
Cdd:PRK00349 896 IKTADWIIDLgpeggdGGGEIVATGTPEEVAKVEASY 932
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
472-637 |
3.55e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDgrdlrtldpswlRGQVVGFISQEPVLFgttimen 551
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------------KGIKLGYFAQHQLEF------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 552 irfgkLAASDEEVYAAAR------EANAHEFITSFpeGYN-TIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 624
Cdd:PRK10636 388 -----LRADESPLQHLARlapqelEQKLRDYLGGF--GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170
....*....|...
gi 109068902 625 LDAESERVVQEAL 637
Cdd:PRK10636 461 LDLDMRQALTEAL 473
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
134-424 |
3.68e-05 |
|
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: 46.12 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 134 AIVLALGAALVNVQIPLLLGQLVEIVakYTRDHVGSFMTesrkLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDMRRA 213
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARI--FAGGPWEDIMP----PLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 214 LFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGT 293
Cdd:cd18561 75 LFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 294 LMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMV 373
Cdd:cd18561 155 LWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGT 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 109068902 374 LGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSA 424
Cdd:cd18561 235 ALALGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISA 285
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
181-398 |
5.35e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 45.62 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 181 LLILYGVQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRL--TTDVQEfkssfkLVISQGLR 258
Cdd:cd18779 48 LAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLssNATIRE------LLTSQTLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 259 SC---TQVAGCLVSLSMLSTRLTLLLMVAtpALMGVGTLMGSG--LRKLSRQCQEQIARAMGVADEALGNVRTVRAFAME 333
Cdd:cd18779 122 ALldgTLVLGYLALLFAQSPLLGLVVLGL--AALQVALLLATRrrVRELMARELAAQAEAQSYLVEALSGIETLKASGAE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 334 QREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL 398
Cdd:cd18779 200 DRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALN 264
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
188-356 |
6.27e-05 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 45.67 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 188 QGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFkSSFKLVISQGLRSCTQVAGCL 267
Cdd:cd18559 51 QGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRV-DSMAPQVIKMWMGPLQNVIGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 268 VSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAmeqrEEERYGAELEAc 347
Cdd:cd18559 130 YLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFE----WEEAFIRQVDA- 204
|
....*....
gi 109068902 348 rCRAEELGR 356
Cdd:cd18559 205 -KRDNELAY 212
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
133-422 |
6.46e-05 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 45.60 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 133 VAIVLALGAAlVNVQIPLLLGQLVEivakytrdhvgSFMTESRKLSTHLLILYGV------QGLLTFGYLVLLSHIGERM 206
Cdd:cd18583 1 CFLCLLAERV-LNVLVPRQLGIIVD-----------SLSGGSGKSPWKEIGLYVLlrflqsGGGLGLLRSWLWIPVEQYS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 207 AVDMRRALFSSLLRQDIAFFDANKTGQLVSrlttdvqefkssfklVISQGlRSCTQ------------VAGCLVSLSMLS 274
Cdd:cd18583 69 YRALSTAAFNHVMNLSMDFHDSKKSGEVLK---------------AIEQG-SSINDlleqilfqivpmIIDLVIAIVYLY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 275 TR----LTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRcR 350
Cdd:cd18583 133 YLfdpyMGLIVAVVMVLYVWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQ-K 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109068902 351 AE-ELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGL 422
Cdd:cd18583 212 AErKYLFSLNLLNAVQSLILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDL 284
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
484-526 |
1.23e-04 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 43.50 E-value: 1.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 109068902 484 KIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP 526
Cdd:pfam06414 12 KAILLGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELHP 54
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
593-629 |
2.75e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 2.75e-04
10 20 30
....*....|....*....|....*....|....*..
gi 109068902 593 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES 629
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
594-626 |
3.93e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 3.93e-04
10 20 30
....*....|....*....|....*....|...
gi 109068902 594 TLSGGQKQRLAIARALIKQPTVLILDEATSALD 626
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
593-682 |
4.67e-04 |
|
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: 43.46 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 593 TTLSGGQKQRLAIARALIKQPT-VL-ILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRIIVMA--- 666
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIGSGLTgVLyVLDEPSIGLhQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIGpga 566
|
90
....*....|....*....
gi 109068902 667 ---DGRVWEAGTHEELLKK 682
Cdd:TIGR00630 567 gehGGEVVASGTPEEILAN 585
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
480-651 |
4.72e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 41.98 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 480 LPPGKIVALVGQSGGGKTTVASLLerfydptaGVVMLDGRdlrtldpSWLRGQVVGfiSQEPVLFGTTIMENIRFGK-LA 558
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDL--------AAAVATGK-------PWLGGPRVP--EQGKVLYVSAEGPADELRRrLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 559 ASdeevyAAAREANAHEFITSFPEGYNTIVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSAL-----DAESERVV 633
Cdd:pfam13481 93 AA-----GADLDLPARLLFLSLVESLPLFFLDRGGPLLDADVDALEAALEEVEDPDLVVIDPLARALggdenSNSDVGRL 167
|
170 180
....*....|....*....|
gi 109068902 634 QEALDR--ASAGRTVLVIAH 651
Cdd:pfam13481 168 VKALDRlaRRTGATVLLVHH 187
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
478-653 |
7.15e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 478 LTLPPGKIVALVGQSGGGKTTVasllerfydptagvvmldgrdLRTldpswlrgqvVGFIsqepvLFGTtiMENIRFGKL 557
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTI---------------------LDA----------IGLA-----LGGA--QSATRRRSG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 558 AASDEEVyaAAREAnahEFITSFPegyntivgergtTLSGGQKQRLAIARAL----IKQPTVLILDEATSALDAESERVV 633
Cdd:cd03227 58 VKAGCIV--AAVSA---ELIFTRL------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQAL 120
|
170 180
....*....|....*....|.
gi 109068902 634 QEAL-DRASAGRTVLVIAHRL 653
Cdd:cd03227 121 AEAIlEHLVKGAQVIVITHLP 141
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
132-394 |
7.74e-04 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 42.24 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 132 GVAIVLALGAALVNVQiPLLLGQlveIVAKYTRDHVGSfMTESRKLSTHLLILYGVQGLLTFGYLVLLSHIGERMAVDMR 211
Cdd:cd18594 1 LLGILLFLEESLKIVQ-PLLLGR---LVAYFVPDSTVT-KTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 212 RALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFK----LVISQGLRSCTQV-------AGCLVSLSMLstrLTLL 280
Cdd:cd18594 76 SLIYKKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVylhfLWIAPLQVIVLTGllwreigPSSLAGLGVL---LLLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 281 LMVAtpalmgvgtLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMeqreEERYGAELEACRCRAEELGRGIAL 360
Cdd:cd18594 153 PLQA---------YLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTW----EESFAKLIENIRKKELKLIRKAAY 219
|
250 260 270
....*....|....*....|....*....|....
gi 109068902 361 FQGLsNIAFncMVLGTLFIGGSLVAGQQLTGGDL 394
Cdd:cd18594 220 IRAF-NMAF--FFFSPTLVSFATFVPYVLTGNTL 250
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
587-651 |
8.52e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.05 E-value: 8.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109068902 587 IVGERGTtLSGGQKQ------RLAIARALIKQPTVLILDEATSALDAES-ERVVQEALD--RASAGRTVLVIAH 651
Cdd:cd03240 109 LLDMRGR-CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEerKSQKNFQLIVITH 181
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
595-663 |
3.17e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 3.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109068902 595 LSGGQKQRLAIarALI-----KQPTVL-ILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHRII 663
Cdd:pfam02463 1078 LSGGEKTLVAL--ALIfaiqkYKPAPFyLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
187-242 |
3.55e-03 |
|
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: 40.15 E-value: 3.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 109068902 187 VQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDV 242
Cdd:cd18606 47 LQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDT 102
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
181-379 |
3.92e-03 |
|
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: 39.82 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 181 LLILYGVQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:cd18605 48 YGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 261 TQVAGCLVSLSMLSTRLTLLLMVatpaLMGVGTLMGSGLRKLSRqcqeQIARAMGVA--------DEALGNVRTVRAFAM 332
Cdd:cd18605 128 FGLLGYLVVICYQLPWLLLLLLP----LAFIYYRIQRYYRATSR----ELKRLNSVNlsplythfSETLKGLVTIRAFRK 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 109068902 333 EQREEERYGAELEACRcRAEELGRGIAL-----FQGLSNIAFNCMVLGTLFI 379
Cdd:cd18605 200 QERFLKEYLEKLENNQ-RAQLASQAASQwlsirLQLLGVLIVTFVALTAVVQ 250
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
588-668 |
4.04e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 588 VGERGTTLSGGQKQRLAIARALI---KQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRGAHRII 663
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
....*
gi 109068902 664 VMADG 668
Cdd:PRK00635 1773 EMGPG 1777
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
172-272 |
6.35e-03 |
|
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: 39.38 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109068902 172 TESRKLSTHLLILYG----VQGLLTFGYLVLLSHIGERMAVDMRRALFSSLLRQDIAFFDANKTGQLVSRLTTDVQEFKS 247
Cdd:cd18603 34 TQDTEQRDYRLGVYGalglGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDN 113
|
90 100
....*....|....*....|....*
gi 109068902 248 SFKLVISQGLRSCTQVAGCLVSLSM 272
Cdd:cd18603 114 TLPQNIRSFLNCLFQVISTLVVISI 138
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