|
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: 590.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 117 WKLFWQFLHPHLLVLGVAVVLALGAALVNVQIPLLLGQLV-EVVAKYTRDHVGSfmtesqnLSTHLLILYGVQGLLTFGY 195
Cdd:COG1132 9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGDLSALLL-------LLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 196 LVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLST 275
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 276 RLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELG 355
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 356 RGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFEYMALN 435
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 436 PCIPLSGGCcVPKEQLRGSVTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVM 515
Cdd:COG1132 322 PEIPDPPGA-VPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 516 LDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTL 595
Cdd:COG1132 399 IDGVDIRDLTLESLRRQI-GVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 596 SGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGT 675
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570 580
....*....|....*....|..
gi 156105685 676 HEELLKKGGLYAELIRRQALDA 697
Cdd:COG1132 558 HEELLARGGLYARLYRLQFGEE 579
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
145-428 |
9.35e-163 |
|
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: 470.49 E-value: 9.35e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 145 NVQIPLLLGQLVEVVAKYTRDHVGSFMTESQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDIT 224
Cdd:cd18574 12 NIQIPLLLGDLVNVISRSLKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 225 FFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSR 304
Cdd:cd18574 92 FFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 305 QCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLV 384
Cdd:cd18574 172 RAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGLSNLALNGIVLGVLYYGGSLV 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 156105685 385 AGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18574 252 SRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
121-693 |
2.78e-156 |
|
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: 464.56 E-value: 2.78e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 121 WQFLHPHLLVLGVAVVLALGAALVNVQIPLLLGQLVevvakytrDHvgSFMTESQNLSTH----LLILYGVQGLLTFGYL 196
Cdd:TIGR02204 10 WPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMI--------DH--GFSKDSSGLLNRyfafLLVVALVLALGTAARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 197 VLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTR 276
Cdd:TIGR02204 80 YLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 277 LTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEAC------RCR 350
Cdd:TIGR02204 160 LTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAyeaarqRIR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 351 AEELGRGIALFQGLSNIAfncmvlGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFE 430
Cdd:TIGR02204 240 TRALLTAIVIVLVFGAIV------GVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 431 YMALNPCIPLSGGCCVPKEQLRGSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPT 510
Cdd:TIGR02204 314 LLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 511 AGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGE 590
Cdd:TIGR02204 394 SGRILLDGVDLRQLDPAELR-ARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 591 RGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRV 670
Cdd:TIGR02204 473 RGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRI 552
|
570 580
....*....|....*....|...
gi 156105685 671 WEAGTHEELLKKGGLYAELIRRQ 693
Cdd:TIGR02204 553 VAQGTHAELIAKGGLYARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
204-690 |
2.37e-153 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 461.88 E-value: 2.37e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 204 ERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMV 283
Cdd:TIGR00958 230 ARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLI 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 284 ATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACR--CRAEELGRgiALF 361
Cdd:TIGR00958 310 NLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLqlNKRKALAY--AGY 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 362 QGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFEYMALNPCIPLS 441
Cdd:TIGR00958 388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLT 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 442 GGccVPKEQLRGSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDL 521
Cdd:TIGR00958 468 GT--LAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 522 RTLDPSWLRGQVVgFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQ 601
Cdd:TIGR00958 546 VQYDHHYLHRQVA-LVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQ 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 602 RLAIARALIKQPTVLILDEATSALDAESERVVQEalDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLK 681
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702
|
....*....
gi 156105685 682 KGGLYAELI 690
Cdd:TIGR00958 703 DQGCYKHLV 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
181-694 |
6.44e-148 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 447.74 E-value: 6.44e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRlttdVQEFKSSFKLVISQGLRSC 260
Cdd:COG2274 202 LLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASR----FRDVESIREFLTGSLLTAL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 261 TQVAGCLVSLSML---STRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREE 337
Cdd:COG2274 278 LDLLFVLIFLIVLffySPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFR 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 338 ERYgAELEACRCRAEELGRGIALFQGLSNIAFNCMV-LGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFG 416
Cdd:COG2274 358 RRW-ENLLAKYLNARFKLRRLSNLLSTLSGLLQQLAtVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQ 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 417 QVVRGLSAGARVFEYMALnPCIPLSGGCCVPKEQLRGSVTFQNVCFSYPcRPGFEVLKDFTLTLPPGKIVALVGQSGGGK 496
Cdd:COG2274 437 RFQDAKIALERLDDILDL-PPEREEGRSKLSLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGK 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 497 TTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEF 576
Cdd:COG2274 515 STLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQI-GVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDF 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 577 ITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTV 656
Cdd:COG2274 594 IEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTI 673
|
490 500 510
....*....|....*....|....*....|....*...
gi 156105685 657 RGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQA 694
Cdd:COG2274 674 RLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
455-693 |
4.89e-143 |
|
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: 417.71 E-value: 4.89e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVv 534
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPT 614
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 615 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
181-693 |
9.41e-129 |
|
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: 393.70 E-value: 9.41e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSS----FKLVISQG 256
Cdd:TIGR02203 60 VIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAatdaFIVLVRET 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 257 LrsctQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQRE 336
Cdd:TIGR02203 140 L----TVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 337 EERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFG 416
Cdd:TIGR02203 216 TRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 417 QVVRGLSAGARVFEYMAlNPCIPLSGGccVPKEQLRGSVTFQNVCFSYPCRpGFEVLKDFTLTLPPGKIVALVGQSGGGK 496
Cdd:TIGR02203 296 PMQRGLAAAESLFTLLD-SPPEKDTGT--RAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGK 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 497 TTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKL-EASDEEVYTAAREANAHE 575
Cdd:TIGR02203 372 STLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQV-ALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQD 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 576 FITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLST 655
Cdd:TIGR02203 451 FVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLST 530
|
490 500 510
....*....|....*....|....*....|....*...
gi 156105685 656 VRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:TIGR02203 531 IEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
455-689 |
3.17e-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: 361.93 E-value: 3.17e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPGFeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVv 534
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPT 614
Cdd:cd03251 79 GLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 615 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAEL 689
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
181-694 |
1.85e-118 |
|
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: 367.99 E-value: 1.85e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLT--FGYL--VLLSHVGERMavdMRR-AL--FSSLLRQDITFFDANKTGQLvSRlttdvqefkssfklVI 253
Cdd:COG5265 80 LLLAYGLLRLLSvlFGELrdALFARVTQRA---VRRlALevFRHLHALSLRFHLERQTGGL-SR--------------DI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 254 SQGLRSctqvAGCLVSLSMLSTRLTLL--LMVA-----------------TPALMGVGTLMGSGLR-KLSRQCQEQIARA 313
Cdd:COG5265 142 ERGTKG----IEFLLRFLLFNILPTLLeiALVAgillvkydwwfalitlvTVVLYIAFTVVVTEWRtKFRREMNEADSEA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 314 MGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGD 393
Cdd:COG5265 218 NTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGD 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 394 LMsfLVASQTVQRSMA--NLSVLFGQVVRGLSAGARVFEYMALNPCI-------PLSGGccvpkeqlRGSVTFQNVCFSY 464
Cdd:COG5265 298 FV--LVNAYLIQLYIPlnFLGFVYREIRQALADMERMFDLLDQPPEVadapdapPLVVG--------GGEVRFENVSFGY 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 465 pcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLF 544
Cdd:COG5265 368 --DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLR-AAIGIVPQDTVLF 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 545 GTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 624
Cdd:COG5265 445 NDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 625 LDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQA 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 |
2.85e-115 |
|
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: 346.52 E-value: 2.85e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 534
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLR-RAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPT 614
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 615 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
181-684 |
4.06e-106 |
|
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: 334.42 E-value: 4.06e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:COG4988 64 LLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 261 TQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARamgVADEALGNVR---TVRAFAMEQREE 337
Cdd:COG4988 144 LVPLLILVAVFPLDWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALAR---LSGHFLDRLRgltTLKLFGRAKAEA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 338 ERYGAELEACRCRAEELGRgIALfqgLSN-----IAFNCMVLGTLFIGGSLVAGQqLTGGDLMSFLVASQTVQRSMANLS 412
Cdd:COG4988 221 ERIAEASEDFRKRTMKVLR-VAF---LSSavlefFASLSIALVAVYIGFRLLGGS-LTLFAALFVLLLAPEFFLPLRDLG 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 413 VLFGQVVRGLSAGARVFEYMALNPCIPLSGGCCVPKEQlRGSVTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQS 492
Cdd:COG4988 296 SFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 493 GGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREAN 572
Cdd:COG4988 373 GAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQI-AWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAG 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 573 AHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHR 652
Cdd:COG4988 452 LDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHR 531
|
490 500 510
....*....|....*....|....*....|..
gi 156105685 653 LSTVRGAHCIVVMADGRVWEAGTHEELLKKGG 684
Cdd:COG4988 532 LALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
198-692 |
5.72e-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: 326.34 E-value: 5.72e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 198 LLSH-VGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTR 276
Cdd:COG4987 77 LVSHdATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 277 LTLLLMVAtpaLMGVGTLMGSGLRKLSRQCQEQIARAMG----VADEALGNVRTVRAFAMEQREEERYgAELEACRCRAE 352
Cdd:COG4987 157 LALVLALG---LLLAGLLLPLLAARLGRRAGRRLAAARAalraRLTDLLQGAAELAAYGALDRALARL-DAAEARLAAAQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 353 E-LGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFEY 431
Cdd:COG4987 233 RrLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 432 MALNPCIPLSGGCCVPKEQlrGSVTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTA 511
Cdd:COG4987 313 LDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 512 GVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGER 591
Cdd:COG4987 390 GSITLGGVDLRDLDEDDLR-RRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEG 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 592 GTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVW 671
Cdd:COG4987 469 GRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
490 500
....*....|....*....|.
gi 156105685 672 EAGTHEELLKKGGLYAELIRR 692
Cdd:COG4987 549 EQGTHEELLAQNGRYRQLYQR 569
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
181-693 |
1.82e-102 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 325.82 E-value: 1.82e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTfGYLvlLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:PRK11176 74 LMILRGITSFIS-SYC--ISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 261 TQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERY 340
Cdd:PRK11176 151 ASIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRF 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 341 GAELEACRCRAEEL--GRGIA--LFQGLSNIAFNCMvlgtLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFG 416
Cdd:PRK11176 231 DKVSNRMRQQGMKMvsASSISdpIIQLIASLALAFV----LYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 417 QVVRGLSAGARVFEYMALNPCIPlSGGCCVpkEQLRGSVTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGK 496
Cdd:PRK11176 307 QFQRGMAACQTLFAILDLEQEKD-EGKRVI--ERAKGDIEFRNVTFTYPGKEV-PALRNINFKIPAGKTVALVGRSGSGK 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 497 TTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLEA-SDEEVYTAAREANAHE 575
Cdd:PRK11176 383 STIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQV-ALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMD 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 576 FITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLST 655
Cdd:PRK11176 462 FINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLST 541
|
490 500 510
....*....|....*....|....*....|....*...
gi 156105685 656 VRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:PRK11176 542 IEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
453-684 |
1.07e-101 |
|
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: 311.08 E-value: 1.07e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 453 GSVTFQNVCFSYpcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQ 532
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 533 VvGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQ 612
Cdd:cd03254 79 I-GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156105685 613 PTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGG 684
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
267-705 |
1.59e-95 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 307.66 E-value: 1.59e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 267 LVSLSM-LSTRLTLLLMVatpaLMGVGTLMGS-GLRK---LSRQCQEQIARAMGVADEALGNVRTVRAFAmeqreeeRYG 341
Cdd:PRK13657 147 LLPLALfMNWRLSLVLVV----LGIVYTLITTlVMRKtkdGQAAVEEHYHDLFAHVSDAIGNVSVVQSYN-------RIE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 342 AELEACRCRAEELGRG-------IALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL-VASQTVQRsmanLSV 413
Cdd:PRK13657 216 AETQALRDIADNLLAAqmpvlswWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVgFATLLIGR----LDQ 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 414 LFGQVVRGLSAGARVFEYMALNPCIPLSG--GCCVPKEQLRGSVTFQNVCFSYP-CRPGfevLKDFTLTLPPGKIVALVG 490
Cdd:PRK13657 292 VVAFINQVFMAAPKLEEFFEVEDAVPDVRdpPGAIDLGRVKGAVEFDDVSFSYDnSRQG---VEDVSFEAKPGQTVAIVG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 491 QSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAARE 570
Cdd:PRK13657 369 PTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR-RNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAER 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 571 ANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIA 650
Cdd:PRK13657 448 AQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIA 527
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 651 HRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQALDAPRTAAPPP 705
Cdd:PRK13657 528 HRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGMLQEDERRKQP 582
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
455-693 |
5.02e-94 |
|
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: 291.70 E-value: 5.02e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYpcRP-GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQV 533
Cdd:cd03252 1 ITFEHVRFRY--KPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 vGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQP 613
Cdd:cd03252 79 -GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 614 TVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
451-670 |
2.03e-88 |
|
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: 276.66 E-value: 2.03e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 451 LRGSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLR 530
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 531 GQVVgFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALI 610
Cdd:cd03248 88 SKVS-LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 611 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRV 670
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
187-691 |
1.72e-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: 284.53 E-value: 1.72e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 187 VQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTD--VQEFKSSfklvisqglrsctQVA 264
Cdd:TIGR03796 206 LQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLNdqVAEFLSG-------------QLA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 265 GCLVSLSMLSTRLtLLLMVATPALMGVGTLMG----------SGLRK-LSRQCQEQIARAMGVADEALGNVRTVRAFAME 333
Cdd:TIGR03796 273 TTALDAVMLVFYA-LLMLLYDPVLTLIGIAFAainvlalqlvSRRRVdANRRLQQDAGKLTGVAISGLQSIETLKASGLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 334 QREEERY-GAELEACRCRaEELGRGIALFQGLSNI--AFNCMVLgtLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMAN 410
Cdd:TIGR03796 352 SDFFSRWaGYQAKLLNAQ-QELGVLTQILGVLPTLltSLNSALI--LVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNN 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 411 LsVLFGQVVRGLSAGARVFEYMALNPCIPL------SGGCCVPKEQLRGSVTFQNVCFSYPcRPGFEVLKDFTLTLPPGK 484
Cdd:TIGR03796 429 L-VGFGGTLQELEGDLNRLDDVLRNPVDPLleepegSAATSEPPRRLSGYVELRNITFGYS-PLEPPLIENFSLTLQPGQ 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 485 IVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLEASDEEV 564
Cdd:TIGR03796 507 RVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSV-AMVDQDIFLFEGTVRDNLTLWDPTIPDADL 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 565 YTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAsaGR 644
Cdd:TIGR03796 586 VRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRR--GC 663
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 156105685 645 TVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIR 691
Cdd:TIGR03796 664 TCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
148-428 |
3.06e-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: 267.89 E-value: 3.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 148 IPLLLGQLVEVVAKYTRDHVgsfmteSQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFD 227
Cdd:cd18557 15 LPYLIGRLIDTIIKGGDLDV------LNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 228 ANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQ 307
Cdd:cd18557 89 KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 308 EQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQ 387
Cdd:cd18557 169 DALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 156105685 388 QLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18557 249 QLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
455-669 |
1.98e-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: 253.46 E-value: 1.98e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVv 534
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVLFGTTIMENIrfgkleasdeevytaareanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQPT 614
Cdd:cd03228 79 AYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 615 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGR 669
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
190-707 |
6.73e-73 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 246.93 E-value: 6.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 190 LLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQefkssfKLVISQGLRSCT----QVAG 265
Cdd:PRK10789 51 LLRYVWRVLLFGASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVD------RVVFAAGEGVLTlvdsLVMG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 266 CLVSLSM---LSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGA 342
Cdd:PRK10789 125 CAVLIVMstqISWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 343 ELEACRCRAEELGRGIALFQ-------GLSNIafncmvlgtLFIGGS--LVAGQQLTGGDLMSFLVASQTVQRSMANLSV 413
Cdd:PRK10789 205 DAEDTGKKNMRVARIDARFDptiyiaiGMANL---------LAIGGGswMVVNGSLTLGQLTSFVMYLGLMIWPMLALAW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 414 LFGQVVRGLSAGARVFEYMALNPCIpLSGGCCVPKEqlRGSVTFQNVCFSYP--CRPgfeVLKDFTLTLPPGKIVALVGQ 491
Cdd:PRK10789 276 MFNIVERGSAAYSRIRAMLAEAPVV-KDGSEPVPEG--RGELDVNIRQFTYPqtDHP---ALENVNFTLKPGQMLGICGP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 492 SGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREA 571
Cdd:PRK10789 350 TGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRL-AVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 572 NAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAH 651
Cdd:PRK10789 429 SVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 652 RLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQALDAPRTAAPPPKK 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 |
8.82e-73 |
|
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: 249.49 E-value: 8.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 205 RMAVDMRRALFSSLLRQDITFFDANKTGQLVSRlttdVQEFKSSFKLVISQGLRSCTQVAGCLVSLSML---STRLTLLL 281
Cdd:TIGR03797 206 RMDASLQAAVWDRLLRLPVSFFRQYSTGDLASR----AMGISQIRRILSGSTLTTLLSGIFALLNLGLMfyySWKLALVA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 282 MVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYgAELEACRCRAEELGRGIALF 361
Cdd:TIGR03797 282 VALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARW-AKLFSRQRKLELSAQRIENL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 362 QGLSNIAFNCMVLGTLF-IGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGAR---VFEymalnpC 437
Cdd:TIGR03797 361 LTVFNAVLPVLTSAALFaAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERakpILE------A 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 438 IPLSGGCCVPKEQLRGSVTFQNVCFSYPCRpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLD 517
Cdd:TIGR03797 435 LPEVDEAKTDPGKLSGAIEVDRVTFRYRPD-GPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYD 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 518 GRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIrFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSG 597
Cdd:TIGR03797 514 GQDLAGLDVQAVRRQL-GVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSG 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 598 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRtvLVIAHRLSTVRGAHCIVVMADGRVWEAGTHE 677
Cdd:TIGR03797 592 GQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYD 669
|
490
....*....|....*.
gi 156105685 678 ELLKKGGLYAELIRRQ 693
Cdd:TIGR03797 670 ELMAREGLFAQLARRQ 685
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
177-693 |
1.49e-71 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 243.86 E-value: 1.49e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 177 LSTHLLILYGVQGLLTfGYLVL-----LSHVGE-----RMAVD----MRRALFSSLLRQDITFFDANKTGQLVSRLTTDV 242
Cdd:PRK10790 54 VAKGNLPLGLVAGLAA-AYVGLqllaaGLHYAQsllfnRAAVGvvqqLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDT 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 243 QEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALG 322
Cdd:PRK10790 133 EVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVIN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 323 NVRTVRAFameqREEERYGAELEACRcRAEELGR-------GIALFQGLSniAFNCMVLGTLFIGGSLVAGQQLTGGDLM 395
Cdd:PRK10790 213 GMSVIQQF----RQQARFGERMGEAS-RSHYMARmqtlrldGFLLRPLLS--LFSALILCGLLMLFGFSASGTIEVGVLY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 396 SFL---------VASQTVQRSMANLSVLfgqvvrglsAGARVFEYMAL------NPCIPLSGGccvpkeqlrgSVTFQNV 460
Cdd:PRK10790 286 AFIsylgrlnepLIELTTQQSMLQQAVV---------AGERVFELMDGprqqygNDDRPLQSG----------RIDIDNV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 461 CFSYpcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQE 540
Cdd:PRK10790 347 SFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR-QGVAMVQQD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 541 PVLFGTTIMENIRFGKlEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDE 620
Cdd:PRK10790 424 PVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDE 502
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156105685 621 ATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
174-682 |
1.68e-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: 240.42 E-value: 1.68e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 174 SQNLSTHL------LILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANkTGQLVSRLTTdVQEFKS 247
Cdd:COG4618 53 SRSVDTLLmltllaLGLYAVMGLLDAVRSRILVRVGARLDRRLGPRVFDAAFRAALRGGGGA-AAQALRDLDT-LRQFLT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 248 SfklvisQGLrsctqVAGC--------LVSLSMLSTRLTLLlmvatpALMGVGTLMGSGL------RKLSRQCQEQIARA 313
Cdd:COG4618 131 G------PGL-----FALFdlpwapifLAVLFLFHPLLGLL------ALVGALVLVALALlnerltRKPLKEANEAAIRA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 314 MGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLS---NIAFNCMVLGTlfiGGSLVAGQQLT 390
Cdd:COG4618 194 NAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAGGFSALSkflRLLLQSAVLGL---GAYLVIQGEIT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 391 GGDLM--SFLVAsqtvqRSMANLSVLFG---QVVRGLSAGARVFEYMALNPCIPlsggccvPKEQL---RGSVTFQNVCF 462
Cdd:COG4618 271 PGAMIaaSILMG-----RALAPIEQAIGgwkQFVSARQAYRRLNELLAAVPAEP-------ERMPLprpKGRLSVENLTV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 463 SYPC--RPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLrGQVVGFISQE 540
Cdd:COG4618 339 VPPGskRP---ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL-GRHIGYLPQD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 541 PVLFGTTIMENI-RFGklEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:COG4618 415 VELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLD 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156105685 620 EATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKK 682
Cdd:COG4618 493 EPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
145-428 |
2.38e-67 |
|
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: 223.55 E-value: 2.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 145 NVQIPLLLGQLVEVVAKYTRDHVGSFMTESQnLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDIT 224
Cdd:cd18573 12 TMSVPFAIGKLIDVASKESGDIEIFGLSLKT-FALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 225 FFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSR 304
Cdd:cd18573 91 FFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 305 QCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLV 384
Cdd:cd18573 171 QVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 156105685 385 AGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18573 251 ASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
453-670 |
2.92e-67 |
|
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: 220.54 E-value: 2.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 453 GSVTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQ 532
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 533 VVGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQ 612
Cdd:cd03245 79 NIGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 613 PTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRV 670
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
181-665 |
8.40e-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: 226.78 E-value: 8.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:TIGR02857 50 LALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 261 TQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERY 340
Cdd:TIGR02857 130 IVPLAILAAVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 341 GAELEACRCRAEELGRgIALfqgLSNIAFNcmVLGTL-------FIGGSLVAGQQLTGGDLMSFLVASQTVQrSMANLSV 413
Cdd:TIGR02857 210 RRSSEEYRERTMRVLR-IAF---LSSAVLE--LFATLsvalvavYIGFRLLAGDLDLATGLFVLLLAPEFYL-PLRQLGA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 414 LFGQVVRGLSAGARVFEYMALNPcIPLSGGCCVPKEQLRgSVTFQNVCFSYPCRPgfEVLKDFTLTLPPGKIVALVGQSG 493
Cdd:TIGR02857 283 QYHARADGVAAAEALFAVLDAAP-RPLAGKAPVTAAPAS-SLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 494 GGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANA 573
Cdd:TIGR02857 359 AGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQI-AWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 574 HEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRL 653
Cdd:TIGR02857 438 DEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRL 517
|
490
....*....|..
gi 156105685 654 STVRGAHCIVVM 665
Cdd:TIGR02857 518 ALAALADRIVVL 529
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
174-682 |
1.42e-64 |
|
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: 223.76 E-value: 1.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 174 SQNLSTHLLI------LYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDAnKTGQLVSRLTTdVQEFKS 247
Cdd:TIGR01842 39 SGSVPTLLMLtvlalgLYLFLGLLDALRSFVLVRIGEKLDGALNQPIFAASFSATLRRGSG-DGLQALRDLDQ-LRQFLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 248 SfklvisQGLrsctqVAGC--------LVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADE 319
Cdd:TIGR01842 117 G------PGL-----FAFFdapwmpiyLLVCFLLHPWIGILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 320 ALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGdlmSFLV 399
Cdd:TIGR01842 186 ALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPG---MMIA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 400 ASQTVQRSMANLSVLFG---QVVRGLSAGARVFEYMALNPciplSGGCCVPKEQLRGSVTFQNVCFSYPcRPGFEVLKDF 476
Cdd:TIGR01842 263 GSILVGRALAPIDGAIGgwkQFSGARQAYKRLNELLANYP----SRDPAMPLPEPEGHLSVENVTIVPP-GGKKPTLRGI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 477 TLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLrGQVVGFISQEPVLFGTTIMENI-RFG 555
Cdd:TIGR01842 338 SFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETF-GKHIGYLPQDVELFPGTVAENIaRFG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 556 KlEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQE 635
Cdd:TIGR01842 417 E-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALAN 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 156105685 636 ALDRASA-GRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKK 682
Cdd:TIGR01842 496 AIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
453-675 |
1.98e-64 |
|
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: 213.12 E-value: 1.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 453 GSVTFQNVCFSYpcRPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG 531
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 532 QVvGFISQEPVLFGTTIMENIR-FGklEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALI 610
Cdd:cd03244 79 RI-SIIPQDPVLFSGTIRSNLDpFG--EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 611 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGT 675
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
198-653 |
9.51e-64 |
|
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: 221.08 E-value: 9.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 198 LLSH-VGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFklvisqgLRSCTQVAGCLVsLSMLSTR 276
Cdd:TIGR02868 75 LVGHdAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLY-------VRVIVPAGVALV-VGAAAVA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 277 LTLLLMVATPALMGVGTLMGSGL-----RKLSRQCQEQIARAMG----VADEALGNVRTVRAF-AME--QREEERYGAEL 344
Cdd:TIGR02868 147 AIAVLSVPAALILAAGLLLAGFVaplvsLRAARAAEQALARLRGelaaQLTDALDGAAELVASgALPaaLAQVEEADREL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 345 EACRCRAeelGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSA 424
Cdd:TIGR02868 227 TRAERRA---AAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 425 GARVFEYMALNPCI-----PLSGGCCVPKEQLRgsvtFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTV 499
Cdd:TIGR02868 304 AERIVEVLDAAGPVaegsaPAAGAVGLGKPTLE----LRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 500 ASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITS 579
Cdd:TIGR02868 378 LATLAGLLDPLQGEVTLDGVPVSSLDQDEVR-RRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRA 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156105685 580 FPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRL 653
Cdd:TIGR02868 457 LPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
177-690 |
2.82e-63 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 223.85 E-value: 2.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 177 LSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTtDVQEFKSSFKLVISQG 256
Cdd:TIGR01193 198 ISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 257 LRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAME--- 333
Cdd:TIGR01193 277 FLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEaer 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 334 -QREEERYGAELE-ACRCRAEELGRGiaLFQGLSNIAFNCMVLgtlFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANL 411
Cdd:TIGR01193 357 ySKIDSEFGDYLNkSFKYQKADQGQQ--AIKAVTKLILNVVIL---WTGAYLVMRGKLTLGQLITFNALLSYFLTPLENI 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 412 SVLFGQVVRGLSAGARVFEyMALNPCIPLSGGCCVPKEQLRGSVTFQNVCFSYpcrpGF--EVLKDFTLTLPPGKIVALV 489
Cdd:TIGR01193 432 INLQPKLQAARVANNRLNE-VYLVDSEFINKKKRTELNNLNGDIVINDVSYSY----GYgsNILSDISLTIKMNSKTTIV 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 490 GQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFG-KLEASDEEVYTAA 568
Cdd:TIGR01193 507 GMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR-QFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAAC 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 569 REANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAgRTVLV 648
Cdd:TIGR01193 586 EIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIF 664
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 156105685 649 IAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELI 690
Cdd:TIGR01193 665 VAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
148-428 |
5.55e-58 |
|
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: 198.09 E-value: 5.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 148 IPLLLGQLVEVVakytrdHVGSFMTESQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFD 227
Cdd:cd18576 15 FPLLAGQLIDAA------LGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 228 ANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQ 307
Cdd:cd18576 89 ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 308 EQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQ 387
Cdd:cd18576 169 DELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 156105685 388 QLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18576 249 ELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
477-693 |
9.13e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 206.23 E-value: 9.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 477 TLTLPPGKIVALVGQSGGGKTTVASLLERFYdPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGK 556
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHL-SWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 557 LEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEA 636
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 637 LDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 693
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
145-428 |
3.74e-57 |
|
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: 196.23 E-value: 3.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 145 NVQIPLLLGQLVEVVAkytrdHVGSFMTESQNLsTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDIT 224
Cdd:cd18572 12 ELAIPHYTGAVIDAVV-----ADGSREAFYRAV-LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 225 FFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSR 304
Cdd:cd18572 86 FFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 305 QCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLV 384
Cdd:cd18572 166 EIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLV 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 156105685 385 AGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18572 246 LSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
337-693 |
5.20e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 200.82 E-value: 5.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 337 EERYGAELEACRCRAEELGRGIALFQGLSN---IAFNCM-VLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLS 412
Cdd:PRK11160 219 EDRYRQQLEQTEQQWLAAQRRQANLTGLSQalmILANGLtVVLMLWLAAGGVGGNAQPGALIALFVFAALAAFEALMPVA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 413 VLF---GQVVrglSAGARVFEYMALNPCIPLSGGCCVPKEQlrGSVTFQNVCFSYPCRPgFEVLKDFTLTLPPGKIVALV 489
Cdd:PRK11160 299 GAFqhlGQVI---ASARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQP-QPVLKGLSLQIKAGEKVALL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 490 GQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAR 569
Cdd:PRK11160 373 GRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR-QAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQ 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 570 EANAHEFITSfPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVI 649
Cdd:PRK11160 452 QVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMI 530
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 156105685 650 AHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 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 ... |
145-428 |
4.25e-54 |
|
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: 187.84 E-value: 4.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 145 NVQIPLLLGQLVEVVAKYTRDHVGSFMTESQNLSTHLLILYGVQGLLTF--GYLVLLShvGERMAVDMRRALFSSLLRQD 222
Cdd:cd18780 12 NLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFlrSWLFTLA--GERVVARLRKRLFSAIIAQE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 223 ITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKL 302
Cdd:cd18780 90 IAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 303 SRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGS 382
Cdd:cd18780 170 SKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGR 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 156105685 383 LVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18780 250 LVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
150-428 |
6.00e-54 |
|
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: 187.68 E-value: 6.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 150 LLLGQLVEVVAKYTRDHVGS--FMTESQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFD 227
Cdd:cd18577 20 IVFGDLFDAFTDFGSGESSPdeFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 228 ANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQ-VAGCLVSLSMlSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQC 306
Cdd:cd18577 100 KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTfIAGFIIAFIY-SWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 307 QEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEacrcRAEELGRGIALFQGLSNIAFNCMVLGT----LFIGGS 382
Cdd:cd18577 179 QEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALE----KARKAGIKKGLVSGLGLGLLFFIIFAMyalaFWYGSR 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 156105685 383 LVAGQQLTGGD----LMSFLVASQTVQRSMANLSVLfgqvVRGLSAGARV 428
Cdd:cd18577 255 LVRDGEISPGDvltvFFAVLIGAFSLGQIAPNLQAF----AKARAAAAKI 300
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
182-667 |
4.47e-51 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 192.94 E-value: 4.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 182 LILYG-VQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTgqlvSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:PTZ00265 103 LVLIGiFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQVNAGIGTKFITI 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 261 TQVAGCLVSLSMLS----TRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQR- 335
Cdd:PTZ00265 179 FTYASAFLGLYIWSlfknARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTi 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 336 ------EEERYGA-ELEACRCRAEELGrgiaLFQG--LSNIAFNcMVLGTLFIGGSLVAGQ---QLTGGDLMSFLVAsqt 403
Cdd:PTZ00265 259 lkkfnlSEKLYSKyILKANFMESLHIG----MINGfiLASYAFG-FWYGTRIIISDLSNQQpnnDFHGGSVISILLG--- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 404 VQRSMANLSVLFGQV---VRGLSAGARVFEYMALNPCIPLSGGccvpKEQLRG--SVTFQNVCFSYPCRPGFEVLKDFTL 478
Cdd:PTZ00265 331 VLISMFMLTIILPNIteyMKSLEATNSLYEIINRKPLVENNDD----GKKLKDikKIQFKNVRFHYDTRKDVEIYKDLNF 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 479 TLPPGKIVALVGQSGGGKTTVASLLERFYDPTAG-VVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFG-- 555
Cdd:PTZ00265 407 TLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdIIINDSHNLKDINLKWWRSKI-GVVSQDPLLFSNSIKNNIKYSly 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 556 ---KLEA----------------------------------------------------SDEEVYTAAREANAHEFITSF 580
Cdd:PTZ00265 486 slkDLEAlsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtiKDSEVVDVSKKVLIHDFVSAL 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 581 PEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG 658
Cdd:PTZ00265 566 PDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRY 645
|
....*....
gi 156105685 659 AHCIVVMAD 667
Cdd:PTZ00265 646 ANTIFVLSN 654
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
202-691 |
6.70e-49 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 186.39 E-value: 6.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 202 VGERMAVDMRRALFSSLLRQDITFFD--ANKTGQLVSRLTTDVQEFKSS--------------FKLVISQGLRSCTQVAG 265
Cdd:PTZ00265 893 IGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGlvnnivifthfivlFLVSMVMSFYFCPIVAA 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 266 CLVSLSMLSTRLTLLL--MVATPALMGVGTLMGSGLRKLSRQcQEQIARAMGVADEALGNVRTVRAFAMEQreeerYGAE 343
Cdd:PTZ00265 973 VLTGTYFIFMRVFAIRarLTANKDVEKKEINQPGTVFAYNSD-DEIFKDPSFLIQEAFYNMNTVIIYGLED-----YFCN 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 344 L--EACRCRAEELGRGI---ALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLM----SFLVASQTVQRSMAnlsvl 414
Cdd:PTZ00265 1047 LieKAIDYSNKGQKRKTlvnSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMkslfTFLFTGSYAGKLMS----- 1121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 415 fgqvVRGLSAGARV-FE-YMAL-----NPCIPLSGGCCVP-KEQLRGSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIV 486
Cdd:PTZ00265 1122 ----LKGDSENAKLsFEkYYPLiirksNIDVRDNGGIRIKnKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTT 1197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 487 ALVGQSGGGKTTVASLLERFYD------------------------------------------------------PTAG 512
Cdd:PTZ00265 1198 AIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSG 1277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 513 VVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERG 592
Cdd:PTZ00265 1278 KILLDGVDICDYNLKDLR-NLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYG 1356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 593 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEAL--DRASAGRTVLVIAHRLSTVRGAHCIVVMAD--- 667
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIVVFNNpdr 1436
|
570 580
....*....|....*....|....*..
gi 156105685 668 --GRVWEAGTHEELLK-KGGLYAELIR 691
Cdd:PTZ00265 1437 tgSFVQAHGTHEELLSvQDGVYKKYVK 1463
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
181-428 |
1.43e-48 |
|
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: 172.74 E-value: 1.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:cd07346 45 LLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 261 TQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERY 340
Cdd:cd07346 125 LTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 341 GAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVR 420
Cdd:cd07346 205 REANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQ 284
|
....*...
gi 156105685 421 GLSAGARV 428
Cdd:cd07346 285 ALASLERI 292
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
181-428 |
1.70e-48 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 172.61 E-value: 1.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:cd18552 45 IIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 261 TQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERY 340
Cdd:cd18552 125 LTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 341 GAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVR 420
Cdd:cd18552 205 RKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQR 284
|
....*...
gi 156105685 421 GLSAGARV 428
Cdd:cd18552 285 GLAAAERI 292
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
455-682 |
4.45e-47 |
|
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: 166.35 E-value: 4.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 534
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELR-RKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPV--LFGTTIMENIRFGkLEA---SDEEVYTAAREA----NAHEFITSFPegyntvvgergTTLSGGQKQRLAI 605
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEDVAFG-PENlglPREEIRERVEEAlelvGLEHLADRPP-----------HELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 606 ARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLKK 682
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
145-408 |
7.37e-47 |
|
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: 167.43 E-value: 7.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 145 NVQIPLLLGQLVEVVAKYTRDHvgsfmTESQNL-STHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDI 223
Cdd:pfam00664 15 SPAFPLVLGRILDVLLPDGDPE-----TQALNVySLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 224 TFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRS-CTQVAGCLVSLSmLSTRLTLLLMVATPALMGVGTLMGSGLRKL 302
Cdd:pfam00664 90 SFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSlATIVGGIIVMFY-YGWKLTLVLLAVLPLYILVSAVFAKILRKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 303 SRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGS 382
Cdd:pfam00664 169 SRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAY 248
|
250 260
....*....|....*....|....*.
gi 156105685 383 LVAGQQLTGGDLMSFLVASQTVQRSM 408
Cdd:pfam00664 249 LVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
174-695 |
1.02e-46 |
|
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: 179.76 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 174 SQNLSTHLLILYG----VQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSF 249
Cdd:TIGR00957 1000 TQNNTSLRLSVYGalgiLQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMI 1079
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 250 KLVISQGLRSCTQVAGCLVSLsMLSTRLTLLLMvatPALMGVGTLMGSGLRKLSRQCQ--EQIARAMGVA--DEALGNVR 325
Cdd:TIGR00957 1080 PPVIKMFMGSLFNVIGALIVI-LLATPIAAVII---PPLGLLYFFVQRFYVASSRQLKrlESVSRSPVYShfNETLLGVS 1155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 326 TVRAFAMEQREEERYGAELEACR--------------CRAEELGRGIALFQGL-SNIAFNCMVLGtlFIGGSLVAGQQLT 390
Cdd:TIGR00957 1156 VIRAFEEQERFIHQSDLKVDENQkayypsivanrwlaVRLECVGNCIVLFAALfAVISRHSLSAG--LVGLSVSYSLQVT 1233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 391 GgdLMSFLVasqtvqRSMANLSVlfgqvvrGLSAGARVFEYMALNPCIPLSGGCCVPKEQL--RGSVTFQNVCFSYpcRP 468
Cdd:TIGR00957 1234 F--YLNWLV------RMSSEMET-------NIVAVERLKEYSETEKEAPWQIQETAPPSGWppRGRVEFRNYCLRY--RE 1296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVgFISQEPVLFGTT 547
Cdd:TIGR00957 1297 DLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKIT-IIPQDPVLFSGS 1375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 IMENIR-FGKLeaSDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 626
Cdd:TIGR00957 1376 LRMNLDpFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 627 AESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQAL 695
Cdd:TIGR00957 1454 LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
458-670 |
1.07e-45 |
|
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: 160.46 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYP--CRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvG 535
Cdd:cd03246 4 ENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHV-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 536 FISQEPVLFGTTIMENIrfgkleasdeevytaareanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQPTV 615
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 616 LILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLSTVRGAHCIVVMADGRV 670
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
456-651 |
1.45e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 158.83 E-value: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 456 TFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVg 535
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 536 FISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREAnAHEFitSFPEGYntvVGERGTTLSGGQKQRLAIARALIKQPTV 615
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLRERKFDRERALEL-LERL--GLPPDI---LDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 156105685 616 LILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH 651
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
457-679 |
2.12e-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: 158.88 E-value: 2.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 457 FQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD-----PTAGVVMLDGRDLRTLD--PSWL 529
Cdd:cd03260 3 LRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDvdVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 530 RGQVvGFISQEPVLFGTTIMENIRFG-KL------EASDEEVYTAAREANAHEFitsfpegyntvVGER--GTTLSGGQK 600
Cdd:cd03260 80 RRRV-GMVFQKPNPFPGSIYDNVAYGlRLhgiklkEELDERVEEALRKAALWDE-----------VKDRlhALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 601 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEEL 679
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
455-680 |
1.85e-43 |
|
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: 164.31 E-value: 1.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPG--FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLR-- 530
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 531 GQVVGFISQEPV--LF-----GTTIMENIRFGKLeASDEEVYTAAREANAH-----EFITSFPegyntvvgergTTLSGG 598
Cdd:COG1123 341 RRRVQMVFQDPYssLNprmtvGDIIAEPLRLHGL-LSRAERRERVAELLERvglppDLADRYP-----------HELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 599 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGT 675
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
....*
gi 156105685 676 HEELL 680
Cdd:COG1123 489 TEEVF 493
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
150-426 |
3.95e-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: 157.65 E-value: 3.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 150 LLLGQLVevvaKYTRDHvGSFMTESQNLSTHLLILYGVQGLLTFG-----YLVllSHVGERMAVDMRRALFSSLLRQDIT 224
Cdd:cd18575 13 LALGQGL----RLLIDQ-GFAAGNTALLNRAFLLLLAVALVLALAsalrfYLV--SWLGERVVADLRKAVFAHLLRLSPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 225 FFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSR 304
Cdd:cd18575 86 FFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 305 QCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEAC------RCRAEELGRGIALFQGLSNIAFncmvlgTLF 378
Cdd:cd18575 166 ASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAfaaalrRIRARALLTALVIFLVFGAIVF------VLW 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 156105685 379 IGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRglSAGA 426
Cdd:cd18575 240 LGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQR--AAGA 285
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
455-694 |
4.66e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.61 E-value: 4.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgqVV 534
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR--RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVLFGT-TIMENIRF-GKLEASDEEVytaaREANAHEFITSF--PEGYNTVVGergtTLSGGQKQRLAIARALI 610
Cdd:COG1131 76 GYVPQEPALYPDlTVRENLRFfARLYGLPRKE----ARERIDELLELFglTDAADRKVG----TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 611 KQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKKG--GLY 686
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARLleDVF 227
|
....*...
gi 156105685 687 AELIRRQA 694
Cdd:COG1131 228 LELTGEEA 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
457-669 |
1.83e-42 |
|
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: 153.01 E-value: 1.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 457 FQNVCFSYPcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPsWLRGQVVGF 536
Cdd:cd03225 2 LKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSL-KELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 537 ISQEP--VLFGTTIMENIRFG--KLEASDEEVYTAAREANAHEFITSFPEgyntvvgERGTTLSGGQKQRLAIARALIKQ 612
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALELVGLEGLRD-------RSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 613 PTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHCIVVMADGR 669
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
453-675 |
1.86e-42 |
|
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: 152.95 E-value: 1.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 453 GSVTFQNVCFSY-PCRPgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG 531
Cdd:cd03369 5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 532 QVvGFISQEPVLFGTTIMENI-RFGklEASDEEVYTAAReanahefitsfpegyntvVGERGTTLSGGQKQRLAIARALI 610
Cdd:cd03369 83 SL-TIIPQDPTLFSGTIRSNLdPFD--EYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 611 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGT 675
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
455-670 |
2.14e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 153.28 E-value: 2.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLERfydPTAGVVMLDGRDLRTLDP---S 527
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSErelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 528 WLRGQVVGFISQEPVLFGT-TIMENIRFGKLEASdeeVYTAAREANAHEFITSFpeGyntvVGERG----TTLSGGQKQR 602
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVALPLLLAG---VSRKERRERARELLERV--G----LGDRLdhrpSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 603 LAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRGAHCIVVMADGRV 670
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
148-428 |
4.81e-42 |
|
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: 154.51 E-value: 4.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 148 IPLLLGQLVEVVAKyTRDHVGSFMTesqnlsthLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFD 227
Cdd:cd18551 18 QPLLVKNLIDALSA-GGSSGGLLAL--------LVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 228 ANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQ 307
Cdd:cd18551 89 RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 308 EQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQ 387
Cdd:cd18551 169 DALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 156105685 388 QLTGGDLMSFLV-ASQTVQrSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18551 249 ALTVGTLVAFLLyLFQLIT-PLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
473-623 |
5.51e-42 |
|
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: 149.34 E-value: 5.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQvVGFISQEPVLF-GTTIMEN 551
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE-IGYVFQDPQLFpRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156105685 552 IRFGkleASDEEVYTAAREANAHEFITSFPEGY--NTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:pfam00005 80 LRLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
455-670 |
6.61e-42 |
|
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: 151.87 E-value: 6.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLERfydPTAGVVMLDGRDLRTLDPSWL- 529
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 530 --RGQVVGFISQEPVLFGT-TIMENIRFGKLEASDEevyTAAREANAHEFITSF--PEGYNTVVGErgttLSGGQKQRLA 604
Cdd:cd03255 78 afRRRHIGFVFQSFNLLPDlTALENVELPLLLAGVP---KKERRERAEELLERVglGDRLNHYPSE----LSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 605 IARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRGAHCIVVMADGRV 670
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
148-428 |
9.07e-42 |
|
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: 153.74 E-value: 9.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 148 IPLLLGQLV-EVVAKYTRDHVGsfmtesqNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFF 226
Cdd:cd18542 18 IPLLIRRIIdSVIGGGLRELLW-------LLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 227 DANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQC 306
Cdd:cd18542 91 DKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 307 QEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAG 386
Cdd:cd18542 171 REQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVIN 250
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 156105685 387 QQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18542 251 GEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
455-711 |
5.03e-41 |
|
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: 157.37 E-value: 5.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPgFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTA---GVVMLDGRDLRTLDPsWLRG 531
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSE-ALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 532 QVVGFISQEP--VLFGTTIMENIRFG--KLEASDEEVYTAAREANAHEFITSFPEGYNTvvgergtTLSGGQKQRLAIAR 607
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 608 ALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKKgg 684
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA-- 233
|
250 260
....*....|....*....|....*..
gi 156105685 685 lYAELIRRQALDAPRTAAPPPKKPEGP 711
Cdd:COG1123 234 -PQALAAVPRLGAARGRAAPAAAAAEP 259
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
455-669 |
5.49e-41 |
|
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: 148.77 E-value: 5.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRP--GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL--ErfYDPTAGVVMLDGRdlrtldpswlr 530
Cdd:cd03250 1 ISVEDASFTWDSGEqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 531 gqvVGFISQEPVLFGTTIMENIRFGKLEasDEEVYTAAREANA-HEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARAL 609
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENILFGKPF--DEERYEKVIKACAlEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 610 IKQPTVLILDEATSALDAES-----ERVVQEALdraSAGRTVLVIAHRLSTVRGAHCIVVMADGR 669
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
198-428 |
2.06e-40 |
|
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: 149.77 E-value: 2.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 198 LLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRL 277
Cdd:cd18784 59 LFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 278 TLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEacrcRAEELGRG 357
Cdd:cd18784 139 SLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLK----DTYKLKIK 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 358 IALFQG----LSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18784 215 EALAYGgyvwSNELTELALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
463-674 |
2.87e-40 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 147.65 E-value: 2.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 463 SYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWL--RGQVVGFISQ 539
Cdd:cd03257 10 SFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkiRRKEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 540 EPVL-------FGTTIMENIRFGKLEASDEEVYTAAREANAH-----EFITSFPegyntvvgergTTLSGGQKQRLAIAR 607
Cdd:cd03257 90 DPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvglpeEVLNRYP-----------HELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 608 ALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAG 674
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
455-698 |
3.06e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 146.04 E-value: 3.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGrdLRTLDPS--WLRG 531
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEEnlWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 532 QVVGFISQEP--VLFGTTIMENIRFGkLE----ASDE---EVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQR 602
Cdd:TIGR04520 77 KKVGMVFQNPdnQFVGATVEDDVAFG-LEnlgvPREEmrkRVDEALKLVGMEDFRDREPH-----------LLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 603 LAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELL 680
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRklNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIF 224
|
250
....*....|....*...
gi 156105685 681 KKGglyaELIRRQALDAP 698
Cdd:TIGR04520 225 SQV----ELLKEIGLDVP 238
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
455-682 |
9.71e-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: 143.49 E-value: 9.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVA---SLLERfydPTAGVVMLDGRDLRTLDPSWLR 530
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIrciNGLER---PTSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 531 G--QVVGFISQEPVLFGT-TIMENIRFgKLE---ASDEEVYTAARE----ANAHEFITSFPegyntvvgergTTLSGGQK 600
Cdd:cd03258 79 KarRRIGMIFQHFNLLSSrTVFENVAL-PLEiagVPKAEIEERVLEllelVGLEDKADAYP-----------AQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 601 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHE 677
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
....*
gi 156105685 678 ELLKK 682
Cdd:cd03258 227 EVFAN 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
456-691 |
1.10e-38 |
|
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: 143.46 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 456 TFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRGQVvG 535
Cdd:COG4555 3 EVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQI-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 536 FISQEPVLF-GTTIMENIR-FGKLEASDEEVYTAAREANAHEFItsFPEGYNTVVGErgttLSGGQKQRLAIARALIKQP 613
Cdd:COG4555 78 VLPDERGLYdRLTVRENIRyFAELYGLFDEELKKRIEELIELLG--LEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 614 TVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVrGAHC--IVVMADGRVWEAGTHEELLKKGG---LYA 687
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEV-EALCdrVVILHKGKVVAQGSLDELREEIGeenLED 230
|
....
gi 156105685 688 ELIR 691
Cdd:COG4555 231 AFVA 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
455-692 |
1.36e-38 |
|
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: 143.65 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 534
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-RRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVL-FGTTIMENI---------RFGKLEASDEE-VYTAAREANAHEFItsfpegyntvvgERG-TTLSGGQKQR 602
Cdd:COG1120 78 AYVPQEPPApFGLTVRELValgryphlgLFGRPSAEDREaVEEALERTGLEHLA------------DRPvDELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 603 LAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEEL 679
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
250
....*....|...
gi 156105685 680 LKkgglyAELIRR 692
Cdd:COG1120 226 LT-----PELLEE 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
455-674 |
2.61e-38 |
|
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: 140.14 E-value: 2.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlRGQVV 534
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA--LSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVLFGTTIMENIrfgkleasdeevytaareanahefitsfpegyntvvgerGTTLSGGQKQRLAIARALIKQPT 614
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 615 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAG 674
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
150-438 |
5.50e-38 |
|
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: 143.75 E-value: 5.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 150 LLLGQLVEVVAKYTRDHVgsfMTESQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFD-- 227
Cdd:cd18578 30 ILFSKLISVFSLPDDDEL---RSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 228 ANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVsLSM-LSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQC 306
Cdd:cd18578 107 ENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLI-IAFvYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 307 QEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSN-IAFNCMVLGtLFIGGSLVA 385
Cdd:cd18578 186 KKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQsLTFFAYALA-FWYGGRLVA 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 386 GQQLTGGD----LMSFLVASQTVQRSMAnlsvLFGQVVRGLSAGARVFEYMALNPCI 438
Cdd:cd18578 265 NGEYTFEQffivFMALIFGAQSAGQAFS----FAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
150-684 |
1.03e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 151.67 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 150 LLLGQLVEVVAKYTRDHVGSFMTE---SQNLSTHLLILygVQGLLTFG----------YLVLLS-HVGERMavdmRRALF 215
Cdd:PLN03232 917 LLVCYLTTEVLRVSSSTWLSIWTDqstPKSYSPGFYIV--VYALLGFGqvavtftnsfWLISSSlHAAKRL----HDAML 990
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 216 SSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTR-----LTLLLMVATPALMG 290
Cdd:PLN03232 991 NSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTIslwaiMPLLILFYAAYLYY 1070
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 291 VGTlmGSGLRKLSRQCQEQIARAMGvadEALGNVRTVRAFAMEQREEERYGAELEacrcraeelgrgialfqglSNIAFN 370
Cdd:PLN03232 1071 QST--SREVRRLDSVTRSPIYAQFG---EALNGLSSIRAYKAYDRMAKINGKSMD-------------------NNIRFT 1126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 371 cmvLGTLFIGGSLVAGQQLTGGdLMSFLVASQTVQRS-------------------MANLSVLFGQVVR-------GLSA 424
Cdd:PLN03232 1127 ---LANTSSNRWLTIRLETLGG-VMIWLTATFAVLRNgnaenqagfastmglllsyTLNITTLLSGVLRqaskaenSLNS 1202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 425 GARVFEYMAL---NPCI-----PLSGGccvpkeQLRGSVTFQNVCFSYpcRPGFE-VLKDFTLTLPPGKIVALVGQSGGG 495
Cdd:PLN03232 1203 VERVGNYIDLpseATAIiennrPVSGW------PSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAG 1274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 496 KTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIR-FGklEASDEEVYTAAREANAH 574
Cdd:PLN03232 1275 KSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLR-RVLSIIPQSPVLFSGTVRFNIDpFS--EHNDADLWEALERAHIK 1351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 575 EFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLS 654
Cdd:PLN03232 1352 DVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLN 1431
|
570 580 590
....*....|....*....|....*....|
gi 156105685 655 TVRGAHCIVVMADGRVWEAGTHEELLKKGG 684
Cdd:PLN03232 1432 TIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
455-680 |
2.18e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 142.91 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVA---SLLERfydPTAGVVMLDGRDLRTLDPSWLR 530
Cdd:COG1135 2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 531 G--QVVGFISQEPVLFGT-TIMENIRFGkLEASDeeVYTAAREANAHEFITsfpegyntVVG--ERGTT----LSGGQKQ 601
Cdd:COG1135 79 AarRKIGMIFQHFNLLSSrTVAENVALP-LEIAG--VPKAEIRKRVAELLE--------LVGlsDKADAypsqLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 602 RLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEE 678
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLD 227
|
..
gi 156105685 679 LL 680
Cdd:COG1135 228 VF 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
458-670 |
3.04e-37 |
|
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: 137.14 E-value: 3.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRGQVvGFI 537
Cdd:cd03230 4 RNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRI-GYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 538 SQEPVLFGT-TIMENIRfgkleasdeevytaareanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQPTVL 616
Cdd:cd03230 79 PEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 617 ILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRV 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 |
4.31e-37 |
|
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: 138.37 E-value: 4.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYP-CRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlrgqv 533
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 VGFISQEPVLFG-TTIMENIRFGkLEASDeeVYTAAREANAHEFITsfpegyntVVGERGT------TLSGGQKQRLAIA 606
Cdd:cd03293 75 RGYVFQQDALLPwLTVLDNVALG-LELQG--VPKAEARERAEELLE--------LVGLSGFenayphQLSGGMRQRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 607 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHCIVVMA--DGRV 670
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSarPGRI 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
455-674 |
5.32e-37 |
|
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: 137.65 E-value: 5.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPsWLRGqvV 534
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP-ERRN--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVLFGT-TIMENIRFG------KLEASDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIAR 607
Cdd:cd03259 75 GMVFQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 608 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAG 674
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
458-681 |
6.25e-37 |
|
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: 138.78 E-value: 6.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYP-CRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGF 536
Cdd:COG1124 5 RNLSVSYGqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV-QM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 537 ISQEPVL-------FGTTIMENIRFGKLEASDEEVYTAAREAN-AHEFITSFPEgyntvvgergtTLSGGQKQRLAIARA 608
Cdd:COG1124 84 VFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 609 LIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTVrgAH-C--IVVMADGRVWEAGTHEEL 679
Cdd:COG1124 153 LILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVV--AHlCdrVAVMQNGRIVEELTVADL 226
|
..
gi 156105685 680 LK 681
Cdd:COG1124 227 LA 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
455-670 |
7.11e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.07 E-value: 7.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlrgqv 533
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 VGFISQEPVLFG-TTIMENIRFGkLEASDeeVYTAAREANAHEFI---------TSFPegyntvvgergTTLSGGQKQRL 603
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALG-LELRG--VPKAERRERARELLelvglagfeDAYP-----------HQLSGGMRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 604 AIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH------RLSTvRgahcIVVMAD--GRV 670
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFLAD-R----VVVLSArpGRI 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
456-669 |
1.68e-36 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 134.29 E-value: 1.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 456 TFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvG 535
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 536 FISQepvlfgttimenirfgkleasdeevytaareanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQPTV 615
Cdd:cd00267 77 YVPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 616 LILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTV-RGAHCIVVMADGR 669
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
451-691 |
3.20e-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: 136.96 E-value: 3.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 451 LRGSVTFQNVCFSYP--CRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSW 528
Cdd:cd03288 16 LGGEIKIHDLCVRYEnnLKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 529 LRGQVvGFISQEPVLFGTTIMENIRfGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARA 608
Cdd:cd03288 93 LRSRL-SIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 609 LIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELL-KKGGLYA 687
Cdd:cd03288 171 FVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFA 250
|
....
gi 156105685 688 ELIR 691
Cdd:cd03288 251 SLVR 254
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
169-691 |
4.59e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 146.81 E-value: 4.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 169 SFMTESQNLSTHLLILY-GVQGLLTFG---------YLVLLSHVgeRMAVDMRRALFSSLLRQDITFFDANKTGQLVSRL 238
Cdd:PLN03130 939 SEWTDQGTPKTHGPLFYnLIYALLSFGqvlvtllnsYWLIMSSL--YAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRF 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 239 TTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQcqEQIARAMGVAD 318
Cdd:PLN03130 1017 AKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRL--DSITRSPVYAQ 1094
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 319 --EALGNVRTVRAFAMEQREEERYGAELEacrcraeelgrgialfqglSNIAFNCMVLGtlfiGGSLVAGQQLTGGDLMS 396
Cdd:PLN03130 1095 fgEALNGLSTIRAYKAYDRMAEINGRSMD-------------------NNIRFTLVNMS----SNRWLAIRLETLGGLMI 1151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 397 FLVASQTV--------QRSMA-----------NLSVLFGQVVR-------GLSAGARVFEYMALNPCIPL--SGGCCVPK 448
Cdd:PLN03130 1152 WLTASFAVmqngraenQAAFAstmglllsyalNITSLLTAVLRlaslaenSLNAVERVGTYIDLPSEAPLviENNRPPPG 1231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 449 EQLRGSVTFQNVCFSYpcRPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS 527
Cdd:PLN03130 1232 WPSSGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLM 1309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 528 WLRgQVVGFISQEPVLFGTTIMENIR-FGklEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIA 606
Cdd:PLN03130 1310 DLR-KVLGIIPQAPVLFSGTVRFNLDpFN--EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLA 1386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 607 RALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELL-KKGGL 685
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLsNEGSA 1466
|
....*.
gi 156105685 686 YAELIR 691
Cdd:PLN03130 1467 FSKMVQ 1472
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
458-698 |
3.06e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 135.14 E-value: 3.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYP--CRPGfevLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrTLDPSW-LRGQVv 534
Cdd:PRK13635 9 EHISFRYPdaATYA---LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-SEETVWdVRRQV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEP--VLFGTTIMENIRFGkLEASD-------EEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAI 605
Cdd:PRK13635 84 GMVFQNPdnQFVGATVQDDVAFG-LENIGvpreemvERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 606 ARALIKQPTVLILDEATSALDAESErvvQEALD-----RASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELL 680
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
250
....*....|....*...
gi 156105685 681 KKGglyaELIRRQALDAP 698
Cdd:PRK13635 229 KSG----HMLQEIGLDVP 242
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
458-681 |
4.30e-35 |
|
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: 135.57 E-value: 4.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDP---TAGVVMLDGRDLRTLDPS---WLR 530
Cdd:COG0444 5 RNLKVYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKelrKIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 531 GQVVGFISQEP---------VlfGTTIMENIRFGKLeASDEEVYTAAREA-------NAHEFITSFP-Egyntvvgergt 593
Cdd:COG0444 85 GREIQMIFQDPmtslnpvmtV--GDQIAEPLRIHGG-LSKAEARERAIELlervglpDPERRLDRYPhE----------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 594 tLSGGQKQRLAIARALIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTVRG-AHCIVVMA 666
Cdd:COG0444 151 -LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVAEiADRVAVMY 225
|
250
....*....|....*
gi 156105685 667 DGRVWEAGTHEELLK 681
Cdd:COG0444 226 AGRIVEEGPVEELFE 240
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
455-669 |
8.61e-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: 130.38 E-value: 8.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWL-RGQV 533
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPpLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 VGFISQEPVLF-GTTIMENIRFGkleasdeevytaareanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQ 612
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 613 PTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHCIVVMADGR 669
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
459-651 |
2.03e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 130.07 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 459 NVCFSYpcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrtldPSWLRGQVVGFIS 538
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 539 QEP--VLFGTTIMENIRFGKLEASD--EEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPT 614
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAgnEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 156105685 615 VLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAH 651
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITH 184
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
454-679 |
2.68e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.46 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGqv 533
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-PPEKRN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 VGFISQEPVLFG-TTIMENIRFGkLEASDeeVYTAAREANAHEF-----ITSFpegyntvvGERG-TTLSGGQKQRLAIA 606
Cdd:COG3842 79 VGMVFQDYALFPhLTVAENVAFG-LRMRG--VPKAEIRARVAELlelvgLEGL--------ADRYpHQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 607 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH------RLSTVrgahcIVVMADGRVWEAGTHEE 678
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHdqeealALADR-----IAVMNDGRIEQVGTPEE 222
|
.
gi 156105685 679 L 679
Cdd:COG3842 223 I 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
455-674 |
1.22e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.63 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRg 531
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 532 QVVGFISQE-PVLFGTTIMENIRFGkLEA---SDEEVYTAAREA----NAHEFITSFPEgyntvvgergtTLSGGQKQRL 603
Cdd:COG2884 79 RRIGVVFQDfRLLPDRTVYENVALP-LRVtgkSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156105685 604 AIARALIKQPTVLILDEATSALDAE-SERVVqEALDRASA-GRTVLVIAHRLSTVRGAHC-IVVMADGRVWEAG 674
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRrGTTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
181-690 |
1.36e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 138.96 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVqgllTFGYLV---LLSHVGeRMAVDMRRALFSSLLRQDITF-FDANK---TGQLVSRLTTDVQEFKSsfklvI 253
Cdd:PLN03232 345 FLIFFGV----TFGVLCesqYFQNVG-RVGFRLRSTLVAAIFHKSLRLtHEARKnfaSGKVTNMITTDANALQQ-----I 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 254 SQGLRSCTQVAGCL-VSLSMLSTRL-------TLLLMVATPalmgVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVR 325
Cdd:PLN03232 415 AEQLHGLWSAPFRIiVSMVLLYQQLgvaslfgSLILFLLIP----LQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMD 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 326 TVRAFAMEQREEERYGAeleacrCRAEELgrgiALF---QGLSniAFNCMVLGTLFIGGSLVAGQQ--LTGGDL-----M 395
Cdd:PLN03232 491 TVKCYAWEKSFESRIQG------IRNEEL----SWFrkaQLLS--AFNSFILNSIPVVVTLVSFGVfvLLGGDLtparaF 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 396 SFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFEY-------MALNPciPLSGGccVPkeqlrgSVTFQNVCFSYPCRP 468
Cdd:PLN03232 559 TSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELllseeriLAQNP--PLQPG--AP------AISIKNGYFSWDSKT 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVAS--LLERFYDPTAGVVmldgrdlrtldpswLRGQVvGFISQEPVLFGT 546
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISamLGELSHAETSSVV--------------IRGSV-AYVPQVSWIFNA 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 TIMENIRFGklEASDEEVYTAAREANA--HEfITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 624
Cdd:PLN03232 694 TVRENILFG--SDFESERYWRAIDVTAlqHD-LDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 625 LDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELI 690
Cdd:PLN03232 771 LDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
455-670 |
2.32e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 128.64 E-value: 2.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--Q 532
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 533 VVGFISQEPVLFG-TTIMENIRFGKLEA-----------SDEEVytaareANAHEFITSfpegyntvVG------ERGTT 594
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVLAGRLGRtstwrsllglfPPEDR------ERALEALER--------VGladkayQRADQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 595 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRgAHC--IVVMADGRV 670
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLAR-RYAdrIIGLRDGRV 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
455-681 |
4.41e-33 |
|
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: 127.40 E-value: 4.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRG 531
Cdd:COG1127 6 IEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 532 QVvGFISQEPVLFGT-TIMENIRF-----GKLeaSDEEVYTAAREA----NAHEFITSFPegyntvvGErgttLSGGQKQ 601
Cdd:COG1127 83 RI-GMLFQGGALFDSlTVFENVAFplrehTDL--SEAEIRELVLEKlelvGLPGAADKMP-------SE----LSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 602 RLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEE 678
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRelRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
...
gi 156105685 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 |
6.11e-33 |
|
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: 125.24 E-value: 6.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFI 537
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA-RKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 538 SQepvlfgttIMENIRFGKLeasdeevytaareanAHEFITsfpegyntvvgergtTLSGGQKQRLAIARALIKQPTVLI 617
Cdd:cd03214 79 PQ--------ALELLGLAHL---------------ADRPFN---------------ELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 618 LDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAG 674
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
455-680 |
7.89e-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: 127.03 E-value: 7.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 534
Cdd:cd03295 1 IEFENVTKRYG--GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR-RKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVLF-GTTIMENIRF-GKLEASDEEvytaAREANAHEFITSF---PEGYntvvGER-GTTLSGGQKQRLAIARA 608
Cdd:cd03295 78 GYVIQQIGLFpHMTVEENIALvPKLLKWPKE----KIRERADELLALVgldPAEF----ADRyPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 609 LIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRL-STVRGAHCIVVMADGRVWEAGTHEELL 680
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRlqQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
455-680 |
1.29e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 126.26 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTV---ASLLERfydPTAGVVMLDGRDL--RTLDPSWL 529
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLtdSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 530 RGQVvGFISQEPVLFG-TTIMENIrfgkLEA-------SDEEVYTAAREANAH----EFITSFPEgyntvvgergtTLSG 597
Cdd:COG1126 76 RRKV-GMVFQQFNLFPhLTVLENV----TLApikvkkmSKAEAEERAMELLERvglaDKADAYPA-----------QLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 598 GQKQRLAIARALIKQPTVLILDEATSALDAEserVVQEALD--R--ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWE 672
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVE 216
|
....*...
gi 156105685 673 AGTHEELL 680
Cdd:COG1126 217 EGPPEEFF 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
456-679 |
2.59e-32 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 125.37 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 456 TFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQV-- 533
Cdd:cd03256 2 EVENLSKTYP--NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 VGFISQEPVLFG-TTIMENIRFGKLeasdeevytaareaNAHEFITS----FPE-------------GYNTVVGERGTTL 595
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRL--------------GRRSTWRSlfglFPKeekqralaalervGLLDKAYQRADQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 596 SGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRgAHC--IVVMADGRVW 671
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAR-EYAdrIVGLKDGRIV 224
|
....*...
gi 156105685 672 EAGTHEEL 679
Cdd:cd03256 225 FDGPPAEL 232
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
210-428 |
3.10e-32 |
|
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: 126.68 E-value: 3.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 210 MRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALM 289
Cdd:cd18590 71 LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 290 GVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAF 369
Cdd:cd18590 151 IAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQ 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 370 NCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18590 231 LGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
145-428 |
3.92e-32 |
|
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: 126.36 E-value: 3.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 145 NVQIPLLLGQLVEVVAKYTRDHVGSFMTESQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDIT 224
Cdd:cd18547 15 SVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 225 FFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSR 304
Cdd:cd18547 95 YFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 305 QCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGA---ELEACRCRAEELGrGIA--LFQGLSNIAFncmvLGTLFI 379
Cdd:cd18547 175 KQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEineELYKASFKAQFYS-GLLmpIMNFINNLGY----VLVAVV 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 156105685 380 GGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18547 250 GGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
469-681 |
5.01e-32 |
|
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: 124.47 E-value: 5.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS--WLRGQVVGFisQEPVLFGT 546
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHeiARLGIGRTF--QIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 -TIMENIR--------FGKLEASDEEVYTAAREAnAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLI 617
Cdd:cd03219 90 lTVLENVMvaaqartgSGLLLARARREEREARER-AEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 618 LDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLK 681
Cdd:cd03219 167 LDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
455-679 |
1.21e-31 |
|
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: 122.61 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPgFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVV 534
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAAR-QSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVLFGT-TIMENIRF-GKLEASDEEvyTAAREANAHEFITSFPEGYNTVVGergtTLSGGQKQRLAIARALIKQ 612
Cdd:cd03263 78 GYCPQFDALFDElTVREHLRFyARLKGLPKS--EIKEEVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156105685 613 PTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAH------RLSTvRgahcIVVMADGRVWEAGTHEEL 679
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdeaeALCD-R----IAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
457-698 |
1.42e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 124.33 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 457 FQNVCFSYPcrPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvG 535
Cdd:PRK13632 10 VENVSFSYP--NSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKI-G 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 536 FISQEP--VLFGTTIMENIRFGkLEAS-------DEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIA 606
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFG-LENKkvppkkmKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 607 RALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKgg 684
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN-- 232
|
250
....*....|....
gi 156105685 685 lyAELIRRQALDAP 698
Cdd:PRK13632 233 --KEILEKAKIDSP 244
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
455-681 |
2.56e-31 |
|
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: 122.23 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--Q 532
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 533 VVGFISQEPVLFGT-TIMENIRFG---KLEASDEEVYTAARE----ANAHEFITSFPegyntvvGErgttLSGGQKQRLA 604
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLEkleaVGLRGAEDLYP-------AE----LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 605 IARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLK 681
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
455-680 |
1.15e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.58 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRtldpswLRGQVV 534
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR------RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVL---FGTTIMENIR---------FGKLEASDEEvytAAREA----NAHEFItsfpegyNTVVGErgttLSGG 598
Cdd:COG1121 78 GYVPQRAEVdwdFPITVRDVVLmgrygrrglFRRPSRADRE---AVDEAlervGLEDLA-------DRPIGE----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 599 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRgAHC--IVVMADGRVwEAGT 675
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVR-EYFdrVLLLNRGLV-AHGP 221
|
....*
gi 156105685 676 HEELL 680
Cdd:COG1121 222 PEEVL 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
454-681 |
2.90e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 122.56 E-value: 2.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASL---LERfydPTAGVVMLDGRDLRTLDPSWLR 530
Cdd:COG1118 2 SIEVRNISKRFG---SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 531 GqvVGFISQEPVLFG-TTIMENIRFG--KLEASDEEvytaaREANAHEFITSFP-EGYntvvGER-GTTLSGGQKQRLAI 605
Cdd:COG1118 76 R--VGFVFQHYALFPhMTVAENIAFGlrVRPPSKAE-----IRARVEELLELVQlEGL----ADRyPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 606 ARALIKQPTVLILDEATSALDA----ESERVVQEALDRaSAGRTVLV---------IAHRlstvrgahcIVVMADGRVWE 672
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDE-LGGTTVFVthdqeealeLADR---------VVVMNQGRIEQ 214
|
....*....
gi 156105685 673 AGTHEELLK 681
Cdd:COG1118 215 VGTPDEVYD 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
458-680 |
3.36e-30 |
|
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: 125.57 E-value: 3.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYPCRPG--------FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFyDPTAGVVMLDGRDLRTLDPSWL 529
Cdd:COG4172 279 RDLKVWFPIKRGlfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 530 RG-----QVVgFisQEPvlFGT---------TIMENIRFGKLEASDEEVYTAAREANA-------------HEFitsfpe 582
Cdd:COG4172 358 RPlrrrmQVV-F--QDP--FGSlsprmtvgqIIAEGLRVHGPGLSAAERRARVAEALEevgldpaarhrypHEF------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 583 gyntvvgergttlSGGQKQRLAIARALIKQPTVLILDEATSALDaeseRVVQ-EALD-----RASAGRTVLVIAHRLSTV 656
Cdd:COG4172 427 -------------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVV 489
|
250 260
....*....|....*....|....*
gi 156105685 657 RG-AHCIVVMADGRVWEAGTHEELL 680
Cdd:COG4172 490 RAlAHRVMVMKDGKVVEQGPTEQVF 514
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
469-670 |
3.55e-30 |
|
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: 118.40 E-value: 3.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSW--LRgQVVGFISQEPVLFG- 545
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLR-QKVGMVFQQFNLFPh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 546 TTIMENIRFGKLEA---SDEEVYTAAREANAH----EFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPTVLIL 618
Cdd:cd03262 91 LTVLENITLAPIKVkgmSKAEAEERALELLEKvglaDKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 619 DEATSALDAEserVVQEALD----RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 670
Cdd:cd03262 160 DEPTSALDPE---LVGEVLDvmkdLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
456-680 |
4.96e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 118.70 E-value: 4.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 456 TFQNVCFSYPcrpgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqvVG 535
Cdd:COG3840 3 RLDDLTYRYG-----DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERP--VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 536 FISQEPVLFG-TTIMENIRFG-----KLEASD-EEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIARA 608
Cdd:COG3840 75 MLFQENNLFPhLTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 609 LIKQPTVLILDEATSALD----AESERVVQEAldRASAGRTVLVIAHRLSTVR--GAHCIVVmADGRVWEAGTHEELL 680
Cdd:COG3840 144 LVRKRPILLLDEPFSALDpalrQEMLDLVDEL--CRERGLTVLMVTHDPEDAAriADRVLLV-ADGRIAADGPTAALL 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
178-679 |
5.77e-30 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 127.59 E-value: 5.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 178 STHLLILYGVQGLLTFGY---LVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVIS 254
Cdd:PTZ00243 998 ATYLYVYLGIVLLGTFSVplrFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYL 1077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 255 QgLRSCTqvagCLVSLSMLSTRLT--LLLMVATPALMGVGTLMG---SGLRKLSRQCQEQIARAMGVADEALGNVRTVRA 329
Cdd:PTZ00243 1078 Y-LLQCL----FSICSSILVTSASqpFVLVALVPCGYLYYRLMQfynSANREIRRIKSVAKSPVFTLLEEALQGSATITA 1152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 330 FAMEQ---REEERYGAELEACRCRAEELGRGIAL-FQGLSNIAFNCMVLgTLFIGGSLVAGQQLTGGDLMSFLVASQT-- 403
Cdd:PTZ00243 1153 YGKAHlvmQEALRRLDVVYSCSYLENVANRWLGVrVEFLSNIVVTVIAL-IGVIGTMLRATSQEIGLVSLSLTMAMQTta 1231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 404 ------------------VQR-----------SMANLSVLFGQVVRGLSAGARVFEYMALNPCIPLSGGccvPKEQLRGS 454
Cdd:PTZ00243 1232 tlnwlvrqvatveadmnsVERllyytdevpheDMPELDEEVDALERRTGMAADVTGTVVIEPASPTSAA---PHPVQAGS 1308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYpcRPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQV 533
Cdd:PTZ00243 1309 LVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 vGFISQEPVLFGTTIMENIR-FgkLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQ 612
Cdd:PTZ00243 1387 -SMIPQDPVLFDGTVRQNVDpF--LEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKK 1463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 613 PTVLIL-DEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEEL 679
Cdd:PTZ00243 1464 GSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
473-680 |
6.83e-30 |
|
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: 119.29 E-value: 6.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWL---RGQVVGFISQEPVLF-GTTI 548
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelRRKKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 549 MENIRFGkLE---ASDEEVYTAAREA----NAHEFITSFPegyntvvGErgttLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:cd03294 120 LENVAFG-LEvqgVPRAEREERAAEAlelvGLEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156105685 622 TSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEELL 680
Cdd:cd03294 188 FSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
458-679 |
9.43e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 118.60 E-value: 9.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGV-----VMLDGRDL--RTLDPSWLR 530
Cdd:COG1117 15 RNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 531 GQVvGFISQEPVLFGTTIMENIRFG--------KLEAsDEEVYTAAREANAhefitsfpegYNTV---VGERGTTLSGGQ 599
Cdd:COG1117 92 RRV-GMVFQKPNPFPKSIYDNVAYGlrlhgiksKSEL-DEIVEESLRKAAL----------WDEVkdrLKKSALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 600 KQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEE 678
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEFGPTEQ 239
|
.
gi 156105685 679 L 679
Cdd:COG1117 240 I 240
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
472-682 |
1.11e-29 |
|
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: 117.82 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqvVGFISQEPVLF-GTTIME 550
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-KRD--ISYVPQNYALFpHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 551 NIRFG-------KLEAsDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:cd03299 91 NIAYGlkkrkvdKKEI-ERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156105685 624 ALDAESERVVQEALDRA--SAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLKK 682
Cdd:cd03299 159 ALDVRTKEKLREELKKIrkEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
181-428 |
1.23e-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: 119.54 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:cd18564 60 LVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 261 TQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERY 340
Cdd:cd18564 140 LTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 341 GAE----LEAcRCRAEELGrgiALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFG 416
Cdd:cd18564 220 AREnrksLRA-GLRAARLQ---ALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTG 295
|
250
....*....|..
gi 156105685 417 QVVRGLSAGARV 428
Cdd:cd18564 296 RIAKASASAERV 307
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
145-399 |
1.59e-29 |
|
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: 119.05 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 145 NVQIPLLLGQLVevvakytrDHVgsfmtESQNLSTHLLILYG--------VQGLLTFGYLVLLSHVGERMAVDMRRALFS 216
Cdd:cd18541 15 QLLIPRIIGRAI--------DAL-----TAGTLTASQLLRYAllilllalLIGIFRFLWRYLIFGASRRIEYDLRNDLFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 217 SLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMG 296
Cdd:cd18541 82 HLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 297 SGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGT 376
Cdd:cd18541 162 KKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIV 241
|
250 260
....*....|....*....|...
gi 156105685 377 LFIGGSLVAGQQLTGGDLMSFLV 399
Cdd:cd18541 242 LWYGGRLVIRGTITLGDLVAFNS 264
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
455-670 |
2.95e-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: 114.06 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlrgqvv 534
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 gfisqepvlfgttimenirfgkleasdeevytaaREANAHefitsfpeGYNTVvgergTTLSGGQKQRLAIARALIKQPT 614
Cdd:cd03216 70 ----------------------------------RDARRA--------GIAMV-----YQLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 615 VLILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 670
Cdd:cd03216 103 LLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
455-679 |
6.46e-29 |
|
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: 115.41 E-value: 6.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqvV 534
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-KRP--V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVLF-GTTIMENIRFG----KLEASD--EEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIAR 607
Cdd:cd03300 75 NTVFQNYALFpHLTVFENIAFGlrlkKLPKAEikERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 608 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS---TVrgAHCIVVMADGRVWEAGTHEEL 679
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
469-680 |
8.41e-29 |
|
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: 114.84 E-value: 8.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGQV-VGFISQEPVLFGT- 546
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGL-PPHERARAgIGYVPEGRRIFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 TIMENIRFG-------KLEASDEEVYTAareanahefitsFPegyntVVGER----GTTLSGGQKQRLAIARALIKQPTV 615
Cdd:cd03224 91 TVEENLLLGayarrraKRKARLERVYEL------------FP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 616 LILDEATSALdaeSERVVQEALDR----ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELL 680
Cdd:cd03224 154 LLLDEPSEGL---APKIVEEIFEAirelRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
181-428 |
1.65e-28 |
|
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: 116.04 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTD---VQEFKSSFKLVISQGL 257
Cdd:cd18543 45 LLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDlslVQRFLAFGPFLLGNLL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 258 rsctQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREE 337
Cdd:cd18543 125 ----TLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERREL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 338 ER--------YGAELEACRCRAeelgRGIALFQGLSNIAfncmVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMA 409
Cdd:cd18543 201 DRfeaaarrlRATRLRAARLRA----RFWPLLEALPELG----LAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVR 272
|
250
....*....|....*....
gi 156105685 410 NLSVLFGQVVRGLSAGARV 428
Cdd:cd18543 273 MLGWLLAMAQRARAAAERV 291
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
464-679 |
1.99e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 116.75 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 464 YPCRPGF-----EVLK---DFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG---- 531
Cdd:COG4608 17 FPVRGGLfgrtvGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 532 -QVVgFisQEP---------VlfGTTIMENIRFGKLeASDEEVYTAAREA-------------NAHEFitsfpegyntvv 588
Cdd:COG4608 97 mQMV-F--QDPyaslnprmtV--GDIIAEPLRIHGL-ASKAERRERVAELlelvglrpehadrYPHEF------------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 589 gergttlSGGQKQRLAIARALIKQPTVLILDEATSALD----AEserVV------QEALdrasaGRTVLVIAHRLSTVRG 658
Cdd:COG4608 159 -------SGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQ---VLnlledlQDEL-----GLTYLFISHDLSVVRH 223
|
250 260
....*....|....*....|..
gi 156105685 659 -AHCIVVMADGRVWEAGTHEEL 679
Cdd:COG4608 224 iSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
457-670 |
3.34e-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: 112.63 E-value: 3.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 457 FQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTldpSWLRgqvVGF 536
Cdd:cd03235 2 VEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKR---IGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 537 ISQEPVL---FGTTIMENIR---------FGKLEASDEEvytAAREAnaHEFItsfpeGYNTVVGERGTTLSGGQKQRLA 604
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLmglyghkglFRRLSKADKA---KVDEA--LERV-----GLSELADRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 605 IARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRgAHC-IVVMADGRV 670
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVL-EYFdRVLLLNRTV 209
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
455-675 |
3.76e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 116.05 E-value: 3.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPC-RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLERfydPTAGVVMLDGRDLRTLDPSWLR 530
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 531 G--QVVGFISQE-PVLFGTTIMENIRFgKLEA---SDEEVYTAARE-------ANAHEFitsFPegyntvvgergTTLSG 597
Cdd:PRK11153 79 KarRQIGMIFQHfNLLSSRTVFDNVAL-PLELagtPKAEIKARVTEllelvglSDKADR---YP-----------AQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 598 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAG 674
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
.
gi 156105685 675 T 675
Cdd:PRK11153 224 T 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
468-670 |
5.92e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.20 E-value: 5.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP--SWLRGqvVGFISQEPVLFG 545
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdAQAAG--IAIIHQELNLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 546 T-TIMENIRFGKLEAS-----DEEVYTAAREAnAHEFITSFPEgyNTVVGErgttLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:COG1129 93 NlSVAENIFLGREPRRgglidWRAMRRRAREL-LARLGLDIDP--DTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 620 EATSAL-DAESER---VVQEaLdrASAGRTVLVIAHRLSTVRgAHC--IVVMADGRV 670
Cdd:COG1129 166 EPTASLtEREVERlfrIIRR-L--KAQGVAIIYISHRLDEVF-EIAdrVTVLRDGRL 218
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
148-428 |
6.41e-28 |
|
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: 114.03 E-value: 6.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 148 IPLLLGQLV-EVVAKYTRDHV---GSFMtesqnlsthlLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDI 223
Cdd:cd18548 18 LPTLMADIIdEGIANGDLSYIlrtGLLM----------LLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 224 TFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLS 303
Cdd:cd18548 88 AEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 304 RQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSL 383
Cdd:cd18548 168 KKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHL 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 156105685 384 VAGQQLTGGDLMSFL-VASQTVQrSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18548 248 INAGSLQVGDLVAFInYLMQILM-SLMMLSMVFVMLPRASASAKRI 292
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
195-398 |
7.76e-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: 113.72 E-value: 7.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 195 YLVLLSHVGERMavdmRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLS 274
Cdd:cd18589 60 YNITMSRIHSRL----QGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 275 TRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRC--RAE 352
Cdd:cd18589 136 PKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRlnKKE 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 156105685 353 ELGRGIALF-QGLSNIAfncMVLGTLFIGGSLVAGQQLTGGDLMSFL 398
Cdd:cd18589 216 AAAYAVSMWtSSFSGLA---LKVGILYYGGQLVTAGTVSSGDLVTFV 259
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
453-679 |
1.20e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.79 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 453 GSVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTvasLLeR----FYDPTAGVVMLDGRDLRTLDPSw 528
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKST---LL-RmiagLEDPTSGEILIGGRDVTDLPPK- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 529 LRGqvVGFISQEPVLFGT-TIMENIRFG----KLEAS--DEEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQ 601
Cdd:COG3839 74 DRN--IAMVFQSYALYPHmTVYENIAFPlklrKVPKAeiDRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 602 RLAIARALIKQPTVLILDEATSALDAESeRV--------VQEALDRAsagrTVLV---------IAHRlstvrgahcIVV 664
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRLGTT----TIYVthdqveamtLADR---------IAV 206
|
250
....*....|....*
gi 156105685 665 MADGRVWEAGTHEEL 679
Cdd:COG3839 207 MNDGRIQQVGTPEEL 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
469-670 |
2.39e-27 |
|
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: 111.67 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWL--RGQVVGFisQEPVLFGT 546
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarLGIARTF--QNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 -TIMENI-----------------RFGKLEASDEEVYTAAREAnAHEFitsfpeGYNTVVGERGTTLSGGQKQRLAIARA 608
Cdd:COG0411 94 lTVLENVlvaaharlgrgllaallRLPRARREEREARERAEEL-LERV------GLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 609 LIKQPTVLILDEATSAL-DAESERVVQ--EALdRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 670
Cdd:COG0411 167 LATEPKLLLLDEPAAGLnPEETEELAEliRRL-RDERGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
454-696 |
3.34e-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: 3.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYpCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswlrgqv 533
Cdd:TIGR00957 636 SITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 VGFISQEPVLFGTTIMENIRFGKleASDEEVYTAAREANAH-EFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQ 612
Cdd:TIGR00957 701 VAYVPQQAWIQNDSLRENILFGK--ALNEKYYQQVLEACALlPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 613 PTVLILDEATSALDAESERVVQEAL---DRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAEL 689
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
....*..
gi 156105685 690 IRRQALD 696
Cdd:TIGR00957 859 LRTYAPD 865
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
454-679 |
3.93e-27 |
|
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: 110.51 E-value: 3.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlRGQV 533
Cdd:cd03296 2 SIEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 VGFISQEPVLFG-TTIMENIRFG-KLEASDEEVYTAAREANAHEFI-----TSFPEGYNTvvgergtTLSGGQKQRLAIA 606
Cdd:cd03296 76 VGFVFQHYALFRhMTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYPA-------QLSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 607 RALIKQPTVLILDEATSALDA----ESERVVQEALDRASAgRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEEL 679
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHV-TTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
454-670 |
1.14e-26 |
|
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: 107.64 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYPCRPG---FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL--ERFYDPTAGVVMLDGRDLrtlDPSW 528
Cdd:cd03213 3 TLSFRNLTVTVKSSPSksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 529 LRGQVvGFISQEPVLFGT-TIMENIRFgkleasdeevytAAREanahefitsfpegyntvvgeRGttLSGGQKQRLAIAR 607
Cdd:cd03213 80 FRKII-GYVPQDDILHPTlTVRETLMF------------AAKL--------------------RG--LSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 608 ALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRGAHC--IVVMADGRV 670
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSEIFELFdkLLLLSQGRV 190
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
469-680 |
2.06e-26 |
|
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: 108.15 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGT-T 547
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 IMENIRFG--------KLEASDEEVYTAareanahefitsFPegyntVVGER----GTTLSGGQKQRLAIARALIKQPTV 615
Cdd:COG0410 95 VEENLLLGayarrdraEVRADLERVYEL------------FP-----RLKERrrqrAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 616 LILDEATSALdaeSERVVQE---ALDR-ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELL 680
Cdd:COG0410 158 LLLDEPSLGL---APLIVEEifeIIRRlNREGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELL 224
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
149-428 |
2.19e-26 |
|
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: 109.91 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 149 PLLLGQLVevvakytrDHVgsFMTESQNLSTHLLILY-----GVQGLLTF-----GYLvlLSHVGERMAVDMRRALFSSL 218
Cdd:cd18563 19 PYLTKILI--------DDV--LIQLGPGGNTSLLLLLvlglaGAYVLSALlgilrGRL--LARLGERITADLRRDLYEHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 219 LRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSG 298
Cdd:cd18563 87 QRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 299 LRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIafnCMVLGTLF 378
Cdd:cd18563 167 IRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTF---LTSLGTLI 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 156105685 379 I---GGSLVAGQQLTGGDLMSFLV-ASQTVQRsMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18563 244 VwyfGGRQVLSGTMTLGTLVAFLSyLGMFYGP-LQWLSRLNNWITRALTSAERI 296
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
455-701 |
4.04e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.95 E-value: 4.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPGFE--VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML------DGRDLRTLDP 526
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 527 swLRgQVVGFISQ--EPVLFGTTIMENIRFGKLE--ASDEEVYTAAREANA-----HEFITSFPegyntvvgergTTLSG 597
Cdd:PRK13634 83 --LR-KKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIElvglpEELLARSP-----------FELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 598 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAG 674
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQG 228
|
250 260
....*....|....*....|....*..
gi 156105685 675 THEELLKKGglyAELIRRQaLDAPRTA 701
Cdd:PRK13634 229 TPREIFADP---DELEAIG-LDLPETV 251
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
455-698 |
5.59e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.91 E-value: 5.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPGFeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 534
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR-KHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEP--VLFGTTIMENIRFG------KLEASDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIA 606
Cdd:PRK13648 86 GIVFQNPdnQFVGSIVKYDVAFGlenhavPYDEMHRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 607 RALIKQPTVLILDEATSALDAESERVVQEALDRASAGR--TVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGG 684
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
250
....*....|....
gi 156105685 685 LYAELirrqALDAP 698
Cdd:PRK13648 235 ELTRI----GLDLP 244
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
475-674 |
5.92e-26 |
|
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: 106.04 E-value: 5.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 475 DFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlrGQVVGFISQEPVLFG-TTIMENIR 553
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRPVSMLFQENNLFAhLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 554 FG-----KLEASDEE-VYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIARALIKQPTVLILDEATSALD- 626
Cdd:cd03298 93 LGlspglKLTAEDRQaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDp 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 156105685 627 AESERVVQEALD-RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAG 674
Cdd:cd03298 162 ALRAEMLDLVLDlHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
181-398 |
7.84e-26 |
|
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: 108.31 E-value: 7.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFgYLVLLSHV-GERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQE------------FKS 247
Cdd:cd18549 48 LLALYILRTLLNY-FVTYWGHVmGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDiselahhgpedlFIS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 248 SFKLVisqglrsctqvaGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTV 327
Cdd:cd18549 127 IITII------------GSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVV 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156105685 328 RAFAMEQREEERYGAELEACRcRAEELG-RGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL 398
Cdd:cd18549 195 KAFANEEYEIEKFDEGNDRFL-ESKKKAyKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFL 265
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
455-664 |
1.25e-25 |
|
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: 104.87 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLErfydPTAGVVMLDGRDLRTLDPSWLR 530
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 531 gqVVGFISQEPVLFGT-TIMENIRF----GKLEASDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAI 605
Cdd:COG4133 76 --RLAYLGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 606 ARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRGAHCIVV 664
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
277-690 |
2.23e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 112.91 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 277 LTLLLMVATPalmgvgTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAeleacrCRAEELG- 355
Cdd:PLN03130 448 LMLVLMFPIQ------TFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQT------VRDDELSw 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 356 -RGIALFQGLSNIAFNCM-VLGTL-------FIGGSLVAGQQLTGGDLMS------FLVASQTVQRSMANLSVLFGQVVr 420
Cdd:PLN03130 516 fRKAQLLSAFNSFILNSIpVLVTVvsfgvftLLGGDLTPARAFTSLSLFAvlrfplFMLPNLITQAVNANVSLKRLEEL- 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 421 gLSAGARVfeyMALNPciPLSGGccVPkeqlrgSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVA 500
Cdd:PLN03130 595 -LLAEERV---LLPNP--PLEPG--LP------AISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLI 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 501 SLLERFYDPTAGVVMLdgrdlrtldpswLRGQVvGFISQEPVLFGTTIMENIRFGkLEASDEEVYTAAREANAHEFITSF 580
Cdd:PLN03130 661 SAMLGELPPRSDASVV------------IRGTV-AYVPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLL 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 581 PEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESER-VVQEALDRASAGRT-VLVI--AHRLSTV 656
Cdd:PLN03130 727 PGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRqVFDKCIKDELRGKTrVLVTnqLHFLSQV 806
|
410 420 430
....*....|....*....|....*....|....
gi 156105685 657 RGahcIVVMADGRVWEAGTHEELLKKGGLYAELI 690
Cdd:PLN03130 807 DR---IILVHEGMIKEEGTYEELSNNGPLFQKLM 837
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
471-679 |
2.77e-25 |
|
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: 104.91 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGT-TIM 549
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVPQGREIFPRlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 550 ENIRFGkLEAsdeevyTAAREANAHEFITS-FPEgYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD-- 626
Cdd:TIGR03410 94 ENLLTG-LAA------LPRRSRKIPDEIYElFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQps 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 627 --AESERVVQEAldRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEEL 679
Cdd:TIGR03410 166 iiKDIGRVIRRL--RAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
459-670 |
3.60e-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: 103.81 E-value: 3.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 459 NVCFSYPCRpgfEVLKDFTLTLPPGkIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVVGFIS 538
Cdd:cd03264 5 NLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLR-RRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 539 QEPvlfgtTIMENIRfgkleaSDEEVYTAAR-----EANAHEFITSFPE--GYNTVVGERGTTLSGGQKQRLAIARALIK 611
Cdd:cd03264 79 QEF-----GVYPNFT------VREFLDYIAWlkgipSKEVKARVDEVLElvNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 612 QPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 670
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKL 207
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
471-694 |
3.71e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 104.76 E-value: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL---ERfYDPTAGVVMLDGRDLRTLDPS--WLRGQVVGFisQEPV--- 542
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPDerARAGIFLAF--QYPVeip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 -----LFGTTIMENIRFGKLEASD--EEVYTAAREAN-AHEFITSfpeGYNtvVGergttLSGGQKQRLAIARALIKQPT 614
Cdd:COG0396 91 gvsvsNFLRTALNARRGEELSAREflKLLKEKMKELGlDEDFLDR---YVN--EG-----FSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 615 VLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAH--RLSTVRGAHCIVVMADGRVWEAGTHE---ELLKKGglYAE 688
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKElalELEEEG--YDW 238
|
....*.
gi 156105685 689 LIRRQA 694
Cdd:COG0396 239 LKEEAA 244
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
455-674 |
6.32e-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: 103.10 E-value: 6.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqvV 534
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRD--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVLF-GTTIMENIRFG-KL-----EASDEEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIAR 607
Cdd:cd03301 75 AMVFQNYALYpHMTVYDNIAFGlKLrkvpkDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 608 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH-RLSTVRGAHCIVVMADGRVWEAG 674
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
148-428 |
6.33e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 105.31 E-value: 6.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 148 IPLLLGQLVEVVAKYTRDHVGSFmtesqNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFD 227
Cdd:cd18778 18 PPWLIRELVDLVTIGSKSLGLLL-----GLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 228 ANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQ 307
Cdd:cd18778 93 DRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 308 EQIARAMGVADEALGNVRTVRAFAMEQREEERYGAelEACRCRAEELGrgiALFqgLSNIAFNCMV----LGT---LFIG 380
Cdd:cd18778 173 EALGELNALLQDNLSGIREIQAFGREEEEAKRFEA--LSRRYRKAQLR---AMK--LWAIFHPLMEfltsLGTvlvLGFG 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 156105685 381 GSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18778 246 GRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
455-680 |
7.09e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 105.07 E-value: 7.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDlrTLDPSWLRG--Q 532
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGirK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 533 VVGFISQEP--VLFGTTIMENIRFGK----LEASD--EEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLA 604
Cdd:PRK13644 78 LVGIVFQNPetQFVGRTVEEDLAFGPenlcLPPIEirKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 605 IARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELL 680
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
181-428 |
8.33e-25 |
|
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: 105.24 E-value: 8.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVqefkSSFKLVISQGL--- 257
Cdd:cd18545 46 FLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDV----NSLSDLLSNGLinl 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 258 -RSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQRE 336
Cdd:cd18545 122 iPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDEN 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 337 EER--------YGAELEACRcraeelgrgiaLFQGLSNIAFNCMVLGT---LFIGGSLVAGQQLTGGDLMSFLVASQTVQ 405
Cdd:cd18545 202 EEIfdelnrenRKANMRAVR-----------LNALFWPLVELISALGTalvYWYGGKLVLGGAITVGVLVAFIGYVGRFW 270
|
250 260
....*....|....*....|...
gi 156105685 406 RSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18545 271 QPIRNLSNFYNQLQSAMASAERI 293
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
455-698 |
8.82e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.88 E-value: 8.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTA---GVVMLDGRDLrTLDPSWLRG 531
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITL-TAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 532 QVVGFISQEP--VLFGTTIMENIRFGkLE---ASDEEVYTAAREANAH----EFITSFPEgyntvvgergtTLSGGQKQR 602
Cdd:PRK13640 84 EKVGIVFQNPdnQFVGATVGDDVAFG-LEnraVPRPEMIKIVRDVLADvgmlDYIDSEPA-----------NLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 603 LAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELL 680
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231
|
250
....*....|....*...
gi 156105685 681 KKgglyAELIRRQALDAP 698
Cdd:PRK13640 232 SK----VEMLKEIGLDIP 245
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
149-679 |
9.91e-25 |
|
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: 110.77 E-value: 9.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 149 PLLLGQlveVVAKYTRDHvgsfmTESQNLSTHLLI----LYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDIT 224
Cdd:TIGR01271 100 PLLLGR---IIASYDPFN-----APEREIAYYLALglclLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 225 FFDANKTGQLVSRLTTDVQEFKSSFklvisqGLRSCTQVA--GCLVSLSMLSTRLTLLLMVATPALMGVGtLMGSGLRKL 302
Cdd:TIGR01271 172 VLDKISTGQLVSLLSNNLNKFDEGL------ALAHFVWIAplQVILLMGLIWELLEVNGFCGLGFLILLA-LFQACLGQK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 303 SRQCQEQ----IARAMGVADEALGNVRTVRAF----AMEQREEERYGAELEACR----CR-------------------- 350
Cdd:TIGR01271 245 MMPYRDKragkISERLAITSEIIENIQSVKAYcweeAMEKIIKNIRQDELKLTRkiayLRyfyssafffsgffvvflsvv 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 351 AEELGRGIALFQGLSNIAFnCMVLgtlfiggSLVAGQQLTGG------------DLMSFLVASQ--TVQRSMANLSVLFG 416
Cdd:TIGR01271 325 PYALIKGIILRRIFTTISY-CIVL-------RMTVTRQFPGAiqtwydslgaitKIQDFLCKEEykTLEYNLTTTEVEMV 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 417 QVVRGLSAG-ARVFEYMALNPCiplsggccvPKEQLRG--SVTFQNvcFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSG 493
Cdd:TIGR01271 397 NVTASWDEGiGELFEKIKQNNK---------ARKQPNGddGLFFSN--FSLYVTP---VLKNISFKLEKGQLLAVAGSTG 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 494 GGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswlrgqvVGFISQEPVLFGTTIMENIRFGKleASDEEVYTAAREA-N 572
Cdd:TIGR01271 463 SGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPGTIKDNIIFGL--SYDEYRYTSVIKAcQ 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 573 AHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESER-VVQEALDRASAGRTVLVIAH 651
Cdd:TIGR01271 527 LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKeIFESCLCKLMSNKTRILVTS 606
|
570 580
....*....|....*....|....*...
gi 156105685 652 RLSTVRGAHCIVVMADGRVWEAGTHEEL 679
Cdd:TIGR01271 607 KLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
472-639 |
1.00e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.87 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLErfydPTAGVVMLDGRDLRTLDPSWLRGQvVGFISQEPVLFGTT 547
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTllkiVASLIS----PTSGTLLFEGEDISTLKPEIYRQQ-VSYCAQTPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 IMENIRFG---KLEASDEEVYTAareanaheFITSF--PEgynTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 622
Cdd:PRK10247 97 VYDNLIFPwqiRNQQPDPAIFLD--------DLERFalPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170
....*....|....*..
gi 156105685 623 SALDAESERVVQEALDR 639
Cdd:PRK10247 166 SALDESNKHNVNEIIHR 182
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
458-703 |
1.03e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.08 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSypcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPsWLRGQVVGFI 537
Cdd:PRK13548 6 RNLSVR---LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 538 SQEPVL-FGTTIMENIRFGKL------EASDEEVYTAAREANAHEFITSFpegYntvvgergTTLSGGQKQRLAIARALI 610
Cdd:PRK13548 82 PQHSSLsFPFTVEEVVAMGRAphglsrAEDDALVAAALAQVDLAHLAGRD---Y--------PQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 611 ------KQPTVLILDEATSALD-AESERVVQEALDRA-SAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEELLK 681
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAhERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
250 260
....*....|....*....|....*...
gi 156105685 682 kgglyAELIRR------QALDAPRTAAP 703
Cdd:PRK13548 231 -----PETLRRvygadvLVQPHPETGAP 253
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
455-701 |
1.12e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.43 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGrDLRTLDPSWLRGQVV 534
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEP--VLFGTTIMENIRFG------KLEASDEEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIA 606
Cdd:PRK13650 84 GMVFQNPdnQFVGATVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 607 RALIKQPTVLILDEATSALDAESE----RVVQEAldRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKK 682
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRleliKTIKGI--RDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
250
....*....|....*....
gi 156105685 683 GGLYAELirrqALDAPRTA 701
Cdd:PRK13650 231 GNDLLQL----GLDIPFTT 245
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
187-397 |
2.07e-24 |
|
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: 104.10 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 187 VQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGC 266
Cdd:cd18550 51 ASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVAT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 267 LVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEAL--GNVRTVRAFAMEQREEERYGAEL 344
Cdd:cd18550 131 LVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARRS 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 345 EACR---CRAEELGRgiALFQGLSnIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSF 397
Cdd:cd18550 211 RELRdlgVRQALAGR--WFFAALG-LFTAIGPALVYWVGGLLVIGGGLTIGTLVAF 263
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
458-690 |
2.27e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 103.28 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYpcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFI 537
Cdd:PRK13647 8 EDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV-GLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 538 SQEP--VLFGTTIMENIRFG--KLEASDEEVYTAAREA----NAHEFITSFPegYNtvvgergttLSGGQKQRLAIARAL 609
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAFGpvNMGLDKDEVERRVEEAlkavRMWDFRDKPP--YH---------LSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 610 IKQPTVLILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAG-----THEELLKK 682
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHnQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQ 233
|
....*...
gi 156105685 683 GGLYAELI 690
Cdd:PRK13647 234 AGLRLPLV 241
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
468-668 |
2.36e-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: 101.64 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQ---VVGFISQEPVLF 544
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrySVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 545 GTTIMENIRFGklEASDEEVYTAAREA-NAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:cd03290 92 NATVEENITFG--SPFNKQRYKAVTDAcSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 156105685 624 ALDAE-SERVVQEALDR--ASAGRTVLVIAHRLSTVRGAHCIVVMADG 668
Cdd:cd03290 170 ALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
181-428 |
2.88e-24 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 103.62 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:cd18544 47 YLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 261 TQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERY 340
Cdd:cd18544 127 LLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEF 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 341 GA---ELEACRCRAEELGrgiALF----QGLSNIAfncmVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSV 413
Cdd:cd18544 207 DEinqEYRKANLKSIKLF---ALFrplvELLSSLA----LALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAE 279
|
250
....*....|....*
gi 156105685 414 LFGQVVRGLSAGARV 428
Cdd:cd18544 280 KFNILQSAMASAERI 294
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
455-670 |
4.01e-24 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 100.95 E-value: 4.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRg 531
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 532 QVVGFISQEPVLFGT-TIMENIRFGkLEASD-------EEVYTAAREANAHEFITSFPEGyntvvgergttLSGGQKQRL 603
Cdd:cd03292 78 RKIGVVFQDFRLLPDrNVYENVAFA-LEVTGvppreirKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 604 AIARALIKQPTVLILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLSTV-RGAHCIVVMADGRV 670
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkAGTTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
459-701 |
4.30e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.46 E-value: 4.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 459 NVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG-QVVGFI 537
Cdd:PRK13639 6 DLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVrKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 538 SQEP--VLFGTTIMENIRFGKLEA--SDEEVYTAAREANAHEFItsfpEGYNTVVGERgttLSGGQKQRLAIARALIKQP 613
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEALKAVGM----EGFENKPPHH---LSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 614 TVLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKKgglyAELIR 691
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSD----IETIR 232
|
250
....*....|
gi 156105685 692 RQALDAPRTA 701
Cdd:PRK13639 233 KANLRLPRVA 242
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
470-711 |
4.90e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 106.69 E-value: 4.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 470 FEVLKDFTLTLPPGKIVALVGQSGGGKT----TVASLLERFYDPTAGVVMLDGRDLRTLDPSWL---RGQVVGFISQEPV 542
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELrriRGNRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 -----LF--GTTIMENIRFgKLEASDEEVYTAAREA-------NAHEFITSFP-EgyntvvgergttLSGGQKQRLAIAR 607
Cdd:COG4172 103 tslnpLHtiGKQIAEVLRL-HRGLSGAAARARALELlervgipDPERRLDAYPhQ------------LSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 608 ALIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELL 680
Cdd:COG4172 170 ALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAELF 245
|
250 260 270
....*....|....*....|....*....|..
gi 156105685 681 KK-GGLYAelirRQALDAPRTAAPPPKKPEGP 711
Cdd:COG4172 246 AApQHPYT----RKLLAAEPRGDPRPVPPDAP 273
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
459-679 |
5.81e-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: 102.24 E-value: 5.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 459 NVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswlrgqvVGFIS 538
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 539 QEPVLFGTTIMENIRFGKleASDEEVYTAAREA-NAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLI 617
Cdd:cd03291 105 QFSWIMPGTIKENIIFGV--SYDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156105685 618 LDEATSALDAESERVVQEA-LDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEEL 679
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
472-714 |
7.32e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.54 E-value: 7.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLrGQVVGFISQEPVL-FGTTIME 550
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA-SRRVASVPQDTSLsFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 551 NIRFGK------LEASDEEVYTAAREANAHEFITSFpegyntvVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 624
Cdd:PRK09536 97 VVEMGRtphrsrFDTWTETDRAAVERAMERTGVAQF-------ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 625 LDAESE-RVVQEALDRASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEELLKKGGLyaelirRQALDA----- 697
Cdd:PRK09536 170 LDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTADTL------RAAFDArtavg 243
|
250 260
....*....|....*....|....*...
gi 156105685 698 --PRTAAP---------PPKKPEGPRSH 714
Cdd:PRK09536 244 tdPATGAPtvtplpdpdRTEAAADTRVH 271
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
458-675 |
7.76e-24 |
|
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: 100.59 E-value: 7.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASL---LERfydPTAGVVMLDGRDLRTLDP---SWLR 530
Cdd:COG4181 12 RGLTKTVGTGAGeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDEdarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 531 GQVVGFISQEPVLFGT-TIMENIRFGKLEASDEEVYTAAREANAhefitsfpegynTV-VGERGT----TLSGGQKQRLA 604
Cdd:COG4181 89 ARHVGFVFQSFQLLPTlTALENVMLPLELAGRRDARARARALLE------------RVgLGHRLDhypaQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156105685 605 IARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGT 675
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
473-670 |
8.25e-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: 100.06 E-value: 8.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTLTLP---PGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDL----RTLD-PSWLRGqvVGFISQEPVLF 544
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINlPPQQRK--IGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 545 -GTTIMENIRFGKLEASDEEVYTAAREANAHEFITSfpegyntvVGERGT-TLSGGQKQRLAIARALIKQPTVLILDEAT 622
Cdd:cd03297 88 pHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDH--------LLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 156105685 623 SALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RGAHCIVVMADGRV 670
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRL 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
471-678 |
1.03e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.49 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlRGQVVGFISQEPVLF-GTTIM 549
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA---ENRHVNTVFQSYALFpHMTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 550 ENIRFG----KLEASD--EEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:PRK09452 105 ENVAFGlrmqKTPAAEitPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156105685 624 ALDAESERVVQ---EALDRaSAGRTVLVIAH----RLS-TVRgahcIVVMADGRVWEAGTHEE 678
Cdd:PRK09452 174 ALDYKLRKQMQnelKALQR-KLGITFVFVTHdqeeALTmSDR----IVVMRDGRIEQDGTPRE 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
454-677 |
1.06e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.47 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLERfydPTAGVVMLDGRDL---RTLDPS 527
Cdd:COG4161 2 SIQLKNINCFYG---SHQALFDINLECPSGETLVLLGPSGAGKSSllrVLNLLET---PDSGQLNIAGHQFdfsQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 528 WLRG--QVVGFISQE----PVLfgtTIMENI--------RFGKLEASDEEVYTAAReANAHEFITSFPegyntvvgergT 593
Cdd:COG4161 76 AIRLlrQKVGMVFQQynlwPHL---TVMENLieapckvlGLSKEQAREKAMKLLAR-LRLTDKADRFP-----------L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 594 TLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVW 671
Cdd:COG4161 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRII 220
|
....*.
gi 156105685 672 EAGTHE 677
Cdd:COG4161 221 EQGDAS 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
455-680 |
1.11e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 100.55 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGrdLRTLDPS----WLR 530
Cdd:PRK09493 2 IEFKNVSKHFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKvderLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 531 gQVVGFISQEPVLF-GTTIMENIRFGKLE---ASDEEVYTAAREANAHefitsfpegyntvVG--ERG----TTLSGGQK 600
Cdd:PRK09493 77 -QEAGMVFQQFYLFpHLTALENVMFGPLRvrgASKEEAEKQARELLAK-------------VGlaERAhhypSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 601 QRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEE 678
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222
|
..
gi 156105685 679 LL 680
Cdd:PRK09493 223 LI 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
388-672 |
1.54e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 105.27 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 388 QLTGGDLMsflvasQTVQrsmanlsvLFGQVVRGLS-------------AGA-RVFEYM-ALNPCIPLSGGCCVPKEQLR 452
Cdd:COG4178 295 EITLGGLM------QAAS--------AFGQVQGALSwfvdnyqslaewrATVdRLAGFEeALEAADALPEAASRIETSED 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 453 GSVTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLlerfYDPTAGVVMLDgRDLRTLdpsw 528
Cdd:COG4178 361 GALALEDLTLRTP--DGRPLLEDLSLSLKPGERLLITGPSGSGKSTllraIAGL----WPYGSGRIARP-AGARVL---- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 529 lrgqvvgFISQEPVLFGTTIMENIRF--GKLEASDEEVYTAAREANAHEFITSFPEGYNtvvgeRGTTLSGGQKQRLAIA 606
Cdd:COG4178 430 -------FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERLDEEAD-----WDQVLSLGEQQRLAFA 497
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 607 RALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWE 672
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQ 563
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
471-673 |
1.69e-23 |
|
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: 98.83 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWlrgQVVGFISQEPVLFGT-TIM 549
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL---RRIGALIEAPGFYPNlTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 550 ENIRFGKLeasdeevYTAAREANAHEFITsfpegyntVVGERGT------TLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:cd03268 91 ENLRLLAR-------LLGIRKKRIDEVLD--------VVGLKDSakkkvkGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 156105685 624 ALDAESERVVQEAL-DRASAGRTVLVIAHRLSTVRG-AHCIVVMADGR-VWEA 673
Cdd:cd03268 156 GLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKlIEEG 208
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
181-398 |
1.79e-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: 101.03 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:cd18546 45 YLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 261 TQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERY 340
Cdd:cd18546 125 LTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERF 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 341 GAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL 398
Cdd:cd18546 205 AELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFL 262
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
472-692 |
2.93e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.70 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGTTIMEN 551
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 552 IR---------FGKLEASDEEVYTAAREANahefitsfpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 622
Cdd:PRK11231 97 VAygrspwlslWGRLSAEDNARVNQAMEQT----------RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 623 SALD----AESERVVQEaldRASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKkgglyAELIRR 692
Cdd:PRK11231 167 TYLDinhqVELMRLMRE---LNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMT-----PGLLRT 233
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
456-651 |
3.52e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 99.55 E-value: 3.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 456 TFQNVCFSYP-CRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTldPSWLRGqVV 534
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADRG-VV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 gFisQEPVLFG-TTIMENIRFG-KLEAsdeeVYTAAREANAHEFITsfpegyntVVGERGT------TLSGGQKQRLAIA 606
Cdd:COG4525 82 -F--QKDALLPwLNVLDNVAFGlRLRG----VPKAERRARAEELLA--------LVGLADFarrriwQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 156105685 607 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH 651
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
453-690 |
4.23e-23 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 99.54 E-value: 4.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 453 GSVTFQNVCFSYpCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDpTAGVVMLDGRDLRTLDPSWLRgQ 532
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWR-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 533 VVGFISQEPVLFGTTIMENIR-FGKLeaSDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIK 611
Cdd:cd03289 78 AFGVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 612 QPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELI 690
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
470-670 |
4.41e-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: 4.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVVGFISQEPVLFG-TTI 548
Cdd:cd03266 18 VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEAR-RRLGFVSDSTGLYDrLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 549 MENIR-FGKLEASDEEVYTAAREANAHEFitsfpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDA 627
Cdd:cd03266 96 RENLEyFAGLYGLKGDELTARLEELADRL------GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 156105685 628 ESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRV 670
Cdd:cd03266 170 MATRALREFIRQlRALGKCILFSTHIMQEVeRLCDRVVVLHRGRV 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
455-699 |
6.51e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.39 E-value: 6.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPGFE---VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG 531
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 532 QVVGFISQEP--VLFGTTIMENIRFG--KLEASDEEVYTAAREA----NAHEFITSFPEgyntvvgergtTLSGGQKQRL 603
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGpeNLGIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 604 AIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLK 681
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
250
....*....|....*...
gi 156105685 682 KgglyAELIRRQALDAPR 699
Cdd:PRK13633 234 E----VEMMKKIGLDVPQ 247
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
473-685 |
9.39e-23 |
|
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: 100.57 E-value: 9.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTL----TLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRT------LDPSWLRgqvVGFISQEPV 542
Cdd:TIGR02142 9 LGDFSLdadfTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRR---IGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 LFG-TTIMENIRFGKLEASDEevYTAAREANAHEFItsfpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:TIGR02142 86 LFPhLSVRGNLRYGMKRARPS--ERRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 622 TSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKKGGL 685
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
454-699 |
1.44e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.58 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYPCRPGFE--VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDL--RTLDPSWL 529
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 530 RGQVvGFISQEP--VLFGTTIMENIRFG--KLEASDEEVYTAAREANAhefITSFPegYNTVVGERGTTLSGGQKQRLAI 605
Cdd:PRK13637 82 RKKV-GLVFQYPeyQLFEETIEKDIAFGpiNLGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 606 ARALIKQPTVLILDEATSALDAESErvvQEALDRASA-----GRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEEL 679
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGR---DEILNKIKElhkeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREV 232
|
250 260
....*....|....*....|
gi 156105685 680 LKKgglyAELIRRQALDAPR 699
Cdd:PRK13637 233 FKE----VETLESIGLAVPQ 248
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
458-670 |
1.50e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 102.88 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP---SWLRGQV 533
Cdd:PRK10535 8 KDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalAQLRREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 VGFISQE-PVLFGTTIMENIRFGKLEASDEevyTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQ 612
Cdd:PRK10535 88 FGFIFQRyHLLSHLTAAQNVEVPAVYAGLE---RKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 613 PTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRGAHCIVVMADGRV 670
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
472-669 |
1.51e-22 |
|
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: 96.73 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGR----DLRTLDPS---WLRGQVVGFISQ----- 539
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPReilALRRRTIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 540 ----------EPVLfgttimenirfgKLEASDEEVYTAAREANAHefitsfpegYNtvVGER-----GTTLSGGQKQRLA 604
Cdd:COG4778 106 prvsaldvvaEPLL------------ERGVDREEARARARELLAR---------LN--LPERlwdlpPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 605 IARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRG-AHCIVVMADGR 669
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
458-698 |
1.53e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 98.24 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrTLDPSWLRGQVVGFI 537
Cdd:PRK13642 8 ENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL-TAENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 538 SQEP--VLFGTTIMENIRFGKLEAS--DEEVYTAAREA----NAHEFITSFPegyntvvgergTTLSGGQKQRLAIARAL 609
Cdd:PRK13642 87 FQNPdnQFVGATVEDDVAFGMENQGipREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 610 IKQPTVLILDEATSALD----AESERVVQEALDRASAgrTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGL 685
Cdd:PRK13642 156 ALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSED 233
|
250
....*....|...
gi 156105685 686 YAELirrqALDAP 698
Cdd:PRK13642 234 MVEI----GLDVP 242
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
464-679 |
1.90e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 98.88 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 464 YPCRPGF-------EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRGQV 533
Cdd:PRK11308 15 YPVKRGLfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 ----------------VGFISQEPVLFGTtimenirfgKLEAsdeevytAAREANAHEFITSF---PEGYntvvGERGTT 594
Cdd:PRK11308 95 qivfqnpygslnprkkVGQILEEPLLINT---------SLSA-------AERREKALAMMAKVglrPEHY----DRYPHM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 595 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVV-------QEALdrasaGRTVLVIAHRLSTVRG-AHCIVVMA 666
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVlnlmmdlQQEL-----GLSYVFISHDLSVVEHiADEVMVMY 229
|
250
....*....|...
gi 156105685 667 DGRVWEAGTHEEL 679
Cdd:PRK11308 230 LGRCVEKGTKEQI 242
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
473-680 |
5.21e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.95 E-value: 5.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG---QVVGFISQEPVLF-GTTI 548
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrKKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 549 MENIRFG------KLEASDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIARALIKQPTVLILDEAT 622
Cdd:PRK10070 124 LDNTAFGmelagiNAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156105685 623 SALDAESERVVQEALDRASAG--RTVLVIAHRL-STVRGAHCIVVMADGRVWEAGTHEELL 680
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
469-680 |
5.76e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 95.59 E-value: 5.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVV-----MLDG-----------RDLRtldpswlrgQ 532
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTarslsqqkgliRQLR---------Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 533 VVGFISQEPVLF-GTTIMENIRFG----KLEASDEEVyTAAREANAHEFITSFPEGYNTvvgergtTLSGGQKQRLAIAR 607
Cdd:PRK11264 86 HVGFVFQNFNLFpHRTVLENIIEGpvivKGEPKEEAT-ARARELLAKVGLAGKETSYPR-------RLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 608 ALIKQPTVLILDEATSALDAEserVVQEALDR----ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELL 680
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
468-704 |
5.77e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.10 E-value: 5.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGT- 546
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGMVHQHFMLVPNl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 TIMENIRFGkLEASDEEVYTAAReanAHEFITSFPEGY------NTVVGErgttLSGGQKQRLAIARALIKQPTVLILDE 620
Cdd:COG3845 96 TVAENIVLG-LEPTKGGRLDRKA---ARARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 621 ATSAL-DAESERVVqEALDR-ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVweAGTH-------EELlkkgglyAELI 690
Cdd:COG3845 168 PTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVMAiADRVTVLRRGKV--VGTVdtaetseEEL-------AELM 237
|
250
....*....|....*.
gi 156105685 691 --RRQALDAPRTAAPP 704
Cdd:COG3845 238 vgREVLLRVEKAPAEP 253
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
471-718 |
7.39e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 101.39 E-value: 7.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDgrdlrtldpswlrgQVVGFISQEPVLFGTTIME 550
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--------------RSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 551 NIRFgkleaSDEEvyTAAREANA------HEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 624
Cdd:PTZ00243 740 NILF-----FDEE--DAARLADAvrvsqlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 625 LDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKK---GGLYAELIRRQAL---DA 697
Cdd:PTZ00243 813 LDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTslyATLAAELKENKDSkegDA 892
|
250 260
....*....|....*....|.
gi 156105685 698 PRTAAPPPKKPEGPRSHQHKS 718
Cdd:PTZ00243 893 DAEVAEVDAAPGGAVDHEPPV 913
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
455-680 |
8.37e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.15 E-value: 8.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP-------S 527
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelakrlA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 528 WLRgQVVGFIS----QEPVLFGttimeniRF----GKLEASDEEVYTAA-----REANAHEFITsfpegyntvvgergtT 594
Cdd:COG4604 79 ILR-QENHINSrltvRELVAFG-------RFpyskGRLTAEDREIIDEAiayldLEDLADRYLD---------------E 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 595 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAS--AGRTVLVIAHRLSTvrgAHC----IVVMADG 668
Cdd:COG4604 136 LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINF---ASCyadhIVAMKDG 212
|
250
....*....|..
gi 156105685 669 RVWEAGTHEELL 680
Cdd:COG4604 213 RVVAQGTPEEII 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
471-670 |
1.20e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.50 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSW---LRGQVVGFISQ-EPVLFGT 546
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQKLGFIYQfHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 TIMENIRFGKLEASdeeVYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 626
Cdd:PRK11629 103 TALENVAMPLLIGK---KKPAEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 156105685 627 AESERVVQEALDR--ASAGRTVLVIAHRLSTVRGAHCIVVMADGRV 670
Cdd:PRK11629 178 ARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
458-699 |
1.32e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.68 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrTLDPSW-----LRgQ 532
Cdd:PRK13636 9 EELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK---PIDYSRkglmkLR-E 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 533 VVGFISQEP--VLFGTTIMENIRFG--KLEASDEEVYTAAREANAHEFITSFPEgyntvvgERGTTLSGGQKQRLAIARA 608
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 609 LIKQPTVLILDEATSALD----AESERVVQEALDraSAGRTVLVIAHRLSTVrGAHC--IVVMADGRVWEAGTHEELLKK 682
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQK--ELGLTIIIATHDIDIV-PLYCdnVFVMKEGRVILQGNPKEVFAE 232
|
250
....*....|....*..
gi 156105685 683 gglyAELIRRQALDAPR 699
Cdd:PRK13636 233 ----KEMLRKVNLRLPR 245
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
456-651 |
1.39e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.77 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 456 TFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlRTLDPSWLRGQVvg 535
Cdd:PRK11248 3 QISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK--PVEGPGAERGVV-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 536 fISQEPVLFGTTIMENIRFGKLEASdeeVYTAAREANAHEFITSFP-EGYNTvvgERGTTLSGGQKQRLAIARALIKQPT 614
Cdd:PRK11248 76 -FQNEGLLPWRNVQDNVAFGLQLAG---VEKMQRLEIAHQMLKKVGlEGAEK---RYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 156105685 615 VLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH 651
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
467-694 |
1.50e-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: 96.71 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 467 RPGFEVlkDFTLTLPPGKIVALVGQSGGGKTTVASL---LERfydPTAGVVMLDGRDLrtLD-------PSWLRGqvVGF 536
Cdd:COG4148 11 RGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVL--QDsargiflPPHRRR--IGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 537 ISQEPVLFGT-TIMENIRFGkleasdeevYTAAREANAHEfitSFPEgyntVVG--------ERG-TTLSGGQKQRLAIA 606
Cdd:COG4148 82 VFQEARLFPHlSVRGNLLYG---------RKRAPRAERRI---SFDE----VVEllgighllDRRpATLSGGERQRVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 607 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKKG 683
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARKAEILPYLERlrDELDIPILYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLSRP 225
|
250
....*....|.
gi 156105685 684 GLYAELIRRQA 694
Cdd:COG4148 226 DLLPLAGGEEA 236
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
455-680 |
1.61e-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: 94.38 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAG-VVMLDGRDLRTLDPSWLRGQV 533
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 vGFIS---QEPVLFGTTIMENI---RFGKLEASDEevYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIAR 607
Cdd:COG1119 81 -GLVSpalQLRFPRDETVLDVVlsgFFDSIGLYRE--PTDEQRERARELLELL--GLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 608 ALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLV-IAHRLSTVrgAHCI---VVMADGRVWEAGTHEELL 680
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEI--PPGIthvLLLKDGRVVAAGPKEEVL 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
476-680 |
1.70e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.88 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 476 FTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlrGQVVGFISQEPVLFG-TTIMENIRF 554
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS---RRPVSMLFQENNLFShLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 555 G-----KLEASD-EEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALD-- 626
Cdd:PRK10771 95 GlnpglKLNAAQrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 627 --AESERVVQEALDRASAgrTVLVIAHRLSTvrgAHCI----VVMADGRVWEAGTHEELL 680
Cdd:PRK10771 164 lrQEMLTLVSQVCQERQL--TLLMVSHSLED---AARIaprsLVVADGRIAWDGPTDELL 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
455-670 |
2.36e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLdGRDLRtldpswlrgqvV 534
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVLF--GTTIMENIRfgkleasdeEVYTAAREANAHEFITSF---PEGYNTVVGergtTLSGGQKQRLAIARAL 609
Cdd:COG0488 381 GYFDQHQEELdpDKTVLDELR---------DGAPGGTEQEVRGYLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156105685 610 IKQPTVLILDEATSALDAESERVVQEALDrASAGrTVLVIAH-R--LSTVrgAHCIVVMADGRV 670
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGV 507
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
470-653 |
3.29e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.08 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD--PTA---GVVMLDGRDL--RTLDPSWLRGQVvGFISQEPV 542
Cdd:PRK14243 23 FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLyaPDVDPVEVRRRI-GMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 LFGTTIMENIRFG-KLEAS----DEEVYTAAREANAHEFITSfpegyntVVGERGTTLSGGQKQRLAIARALIKQPTVLI 617
Cdd:PRK14243 102 PFPKSIYDNIAYGaRINGYkgdmDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 156105685 618 LDEATSALDAESERVVQEALDRASAGRTVLVIAHRL 653
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
452-674 |
5.24e-21 |
|
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: 92.21 E-value: 5.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 452 RGSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldPSWLRG 531
Cdd:cd03220 17 SSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSLLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 532 QVVGFisqEPVLfgtTIMENIRF-----GKLEASDEEVYtaareanahEFITSFPEgyntvVGERGT----TLSGGQKQR 602
Cdd:cd03220 91 LGGGF---NPEL---TGRENIYLngrllGLSRKEIDEKI---------DEIIEFSE-----LGDFIDlpvkTYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 603 LAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRgAHC--IVVMADGRVWEAG 674
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIK-RLCdrALVLEKGKIRFDG 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
454-677 |
5.45e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 92.77 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYPCRpgfEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLE-----------RFYDPTAGVVMLDGR 519
Cdd:PRK11124 2 SIQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLEmprsgtlniagNHFDFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 520 DLRtldpswlrgQVVGFISQE----PVLfgtTIMENIrfgkLEA-------SDEEVYTAAREANAH----EFITSFPegy 584
Cdd:PRK11124 79 ELR---------RNVGMVFQQynlwPHL---TVQQNL----IEApcrvlglSKDQALARAEKLLERlrlkPYADRFP--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 585 ntvvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCI 662
Cdd:PRK11124 140 --------LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRV 211
|
250
....*....|....*
gi 156105685 663 VVMADGRVWEAGTHE 677
Cdd:PRK11124 212 VYMENGHIVEQGDAS 226
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
467-680 |
9.70e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 92.59 E-value: 9.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWlRGQVVGFISQEPvlfGT 546
Cdd:COG4167 23 RQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RCKHIRMIFQDP---NT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 TIMENIRFGK-LEA--------SDEEvytaaREANAHEFITS---FPEGYNTVVgergTTLSGGQKQRLAIARALIKQPT 614
Cdd:COG4167 99 SLNPRLNIGQiLEEplrlntdlTAEE-----REERIFATLRLvglLPEHANFYP----HMLSSGQKQRVALARALILQPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 615 VLILDEATSALDAeSERV--------VQEALdrasaGRTVLVIAHRLSTVRgaHC---IVVMADGRVWEAGTHEELL 680
Cdd:COG4167 170 IIIADEALAALDM-SVRSqiinlmleLQEKL-----GISYIYVSQHLGIVK--HIsdkVLVMHQGEVVEYGKTAEVF 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
457-651 |
1.03e-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: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 457 FQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDgrdlrtldpswlRGQVVGF 536
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------------KGLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 537 ISQEPVLF-GTTIMENI-----RFGKLEASDEEVYTA--------AREANAHEFITSFpEGYN------TVVGERG---- 592
Cdd:COG0488 66 LPQEPPLDdDLTVLDTVldgdaELRALEAELEELEAKlaepdedlERLAELQEEFEAL-GGWEaearaeEILSGLGfpee 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 593 ------TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAEServVQ--EALDRASAGrTVLVIAH 651
Cdd:COG0488 145 dldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSH 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
469-684 |
1.04e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.25 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlrgQVVGFISQEPVLF-GTT 547
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR-----RRIGYLPEERGLYpKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 IMENIR-FGKL---EASDeevytaAREaNAHEFITSFPegyntvVGERGT----TLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:COG4152 88 VGEQLVyLARLkglSKAE------AKR-RADEWLERLG------LGDRANkkveELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 620 EATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTVRgAHC--IVVMADGRVWEAGTHEELLKKGG 684
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVE-ELCdrIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
472-674 |
1.15e-20 |
|
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: 90.80 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDpswlrGQVVGFISQEPVLF-GTTIME 550
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRIGYLPEERGLYpKMKVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 551 NIR-FGKLEA-SDEEvytAAREANahEFITSFP-EGYNTVVGErgtTLSGGQKQRLAIARALIKQPTVLILDEATSALDA 627
Cdd:cd03269 90 QLVyLAQLKGlKKEE---ARRRID--EWLERLElSEYANKRVE---ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 156105685 628 ESERVVQEAL-DRASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAG 674
Cdd:cd03269 162 VNVELLKDVIrELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
469-679 |
1.33e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.52 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGqvVGFISQEPVLF-GTT 547
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-PPYQRP--INMMFQSYALFpHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 IMENIRFG-------KLEASD--EEVYTAAreaNAHEFITSFPEgyntvvgergtTLSGGQKQRLAIARALIKQPTVLIL 618
Cdd:PRK11607 108 VEQNIAFGlkqdklpKAEIASrvNEMLGLV---HMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156105685 619 DEATSALDAE-SERVVQEALD-RASAGRTVLVIAH-RLSTVRGAHCIVVMADGRVWEAGTHEEL 679
Cdd:PRK11607 174 DEPMGALDKKlRDRMQLEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
471-651 |
1.39e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.90 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD--PTA---GVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFG 545
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRRV-QMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 546 T-TIMENIRFG----KLEASDEEVYTAAREAnaHEFITSFPEGYNTVVGERGTtLSGGQKQRLAIARALIKQPTVLILDE 620
Cdd:PRK14247 96 NlSIFENVALGlklnRLVKSKKELQERVRWA--LEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190
....*....|....*....|....*....|.
gi 156105685 621 ATSALDAESERVVQEALDRASAGRTVLVIAH 651
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
458-680 |
1.49e-20 |
|
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: 91.07 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrTLDPSWLRGQV-VGF 536
Cdd:cd03218 4 ENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMHKRARLgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 537 ISQEPVLF-GTTIMENIR--FGKLEASDEEvytaaREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQP 613
Cdd:cd03218 80 LPQEASIFrKLTVEENILavLEIRGLSKKE-----REEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156105685 614 TVLILDEATSALD----AESERVVQEALDRasaGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEELL 680
Cdd:cd03218 153 KFLLLDEPFAGVDpiavQDIQKIIKILKDR---GIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
454-682 |
1.53e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.50 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYPCRPGFE--VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTL----DPS 527
Cdd:PRK13649 2 GINLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 528 WLRGQVvGFISQ--EPVLFGTTIMENIRFG--KLEASDEEVYTAAREANAHEFITsfpegyNTVVGERGTTLSGGQKQRL 603
Cdd:PRK13649 82 QIRKKV-GLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 604 AIARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLK 681
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQ 234
|
.
gi 156105685 682 K 682
Cdd:PRK13649 235 D 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
469-683 |
1.65e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 90.28 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF--YDPTAGVVMLDGRDLRTLDPS--WLRGQVVGFisQEPVLF 544
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEerARLGIFLAF--QYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 545 -GTTIMENIRFgkleasdeevytaareanahefitsfpegyntvVGErgtTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:cd03217 90 pGVKNADFLRY---------------------------------VNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 624 ALDAESERVVQEALDR-ASAGRTVLVIAHR---LSTVRG--AHcivVMADGRVWEAGTHE---ELLKKG 683
Cdd:cd03217 134 GLDIDALRLVAEVINKlREEGKSVLIITHYqrlLDYIKPdrVH---VLYDGRIVKSGDKElalEIEKKG 199
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
458-681 |
1.92e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 90.86 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVasllerFY------DPTAGVVMLDGRDLrTLDPSWLRG 531
Cdd:COG1137 7 ENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDI-THLPMHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 532 QV-VGFISQEPVLF-GTTIMENIRfGKLEASdeEVYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARAL 609
Cdd:COG1137 77 RLgIGYLPQEASIFrKLTVEDNIL-AVLELR--KLSKKEREERLEELLEEF--GITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 610 IKQPTVLILDEATSALD----AESERVVQEALDRasaGRTVLVIAHRlstVRGAHCIV----VMADGRVWEAGTHEELLK 681
Cdd:COG1137 152 ATNPKFILLDEPFAGVDpiavADIQKIIRHLKER---GIGVLITDHN---VRETLGICdrayIISEGKVLAEGTPEEILN 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
199-690 |
2.00e-20 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 96.90 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 199 LSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRL- 277
Cdd:TIGR01271 949 LVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIf 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 278 --TLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVAdeaLGNVRTVRAFAMEQREEERYGAELEACRCRAEELG 355
Cdd:TIGR01271 1029 iaAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITS---LKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYL 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 356 RGIALFQGLSNIAFNCMVLGTLFIG-GSLVAGQQLTGGDLMSFLVASQTVQRSMaNLSVLFGQVVRGLSagaRVFEYMAL 434
Cdd:TIGR01271 1106 STLRWFQMRIDIIFVFFFIAVTFIAiGTNQDGEGEVGIILTLAMNILSTLQWAV-NSSIDVDGLMRSVS---RVFKFIDL 1181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 435 NPCIPL---SGGCCVPKEQL-------------RGSVTFQNVCFSYpCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT 498
Cdd:TIGR01271 1182 PQEEPRpsgGGGKYQLSTVLvienphaqkcwpsGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKST 1260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 499 VASLLERFYDpTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRfGKLEASDEEVYTAAREANAHEFIT 578
Cdd:TIGR01271 1261 LLSALLRLLS-TEGEIQIDGVSWNSVTLQTWR-KAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIE 1337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 579 SFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRG 658
Cdd:TIGR01271 1338 QFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLE 1417
|
490 500 510
....*....|....*....|....*....|..
gi 156105685 659 AHCIVVMADGRVWEAGTHEELLKKGGLYAELI 690
Cdd:TIGR01271 1418 CQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
435-681 |
2.51e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.50 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 435 NPCIPLSGGCCVPKEQLrgsVTFQNVCFSyPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLErFYDPT---- 510
Cdd:TIGR00955 7 NSDVFGRVAQDGSWKQL---VSRLRGCFC-RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 511 AGVVMLDGRdlrTLDPSWLRgQVVGFISQEPVLFGT-TIMENIRFGKLEASDEEVYTAAREANAHEFIT--SFPEGYNTV 587
Cdd:TIGR00955 82 SGSVLLNGM---PIDAKEMR-AISAYVQQDDLFIPTlTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 588 VGERGTT--LSGGQKQRLAIARALIKQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLST--VRGAHCI 662
Cdd:TIGR00955 158 IGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKI 237
|
250
....*....|....*....
gi 156105685 663 VVMADGRVWEAGTHEELLK 681
Cdd:TIGR00955 238 ILMAEGRVAYLGSPDQAVP 256
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
473-651 |
3.80e-20 |
|
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: 89.83 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlRGQVVGFISQEPVLfgtTIMENI 552
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD--RMVVFQNYSLLPWL---TVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 553 RFGkLEASDEEVYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERV 632
Cdd:TIGR01184 76 ALA-VDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|.
gi 156105685 633 VQEALDR--ASAGRTVLVIAH 651
Cdd:TIGR01184 153 LQEELMQiwEEHRVTVLMVTH 173
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
472-682 |
3.98e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.48 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTldpSWLRGQVVGFISQEPVLF-GTTIME 550
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRDICMVFQSYALFpHMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 551 NIRFG--KLEASDEEVYTAAREANAHEFITSFPEGYntvVGErgttLSGGQKQRLAIARALIKQPTVLILDEATSALDAE 628
Cdd:PRK11432 98 NVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRY---VDQ----ISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 629 SERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLKK 682
Cdd:PRK11432 171 LRRSMREKIRelQQQFNITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
454-701 |
4.64e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.04 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYPCRPGFEV--LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrTLDPS---- 527
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI-TPETGnknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 528 -WLRGQVvGFISQ--EPVLFGTTIMENIRFGKLE--ASDEEvytaAREAnAHEFITSFpeGYNTVVGERGT-TLSGGQKQ 601
Cdd:PRK13641 81 kKLRKKV-SLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDE----AKEK-ALKWLKKV--GLSEDLISKSPfELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 602 RLAIARALIKQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEEL 679
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
250 260
....*....|....*....|..
gi 156105685 680 LKKgglyAELIRRQALDAPRTA 701
Cdd:PRK13641 233 FSD----KEWLKKHYLDEPATS 250
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
471-679 |
6.33e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.07 E-value: 6.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlRGQVVGFISQEPVLF-GTTIM 549
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDRKVGFVFQHYALFrHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 550 ENIRFG----------KLEASDEEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:PRK10851 93 DNIAFGltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 620 EATSALDAESE-------RVVQEALDRASagrtVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEEL 679
Cdd:PRK10851 162 EPFGALDAQVRkelrrwlRQLHEELKFTS----VFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
471-653 |
6.49e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.83 E-value: 6.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD-----PTAGVVMLDGRDL--RTLDPSWLRGQVvGFISQEPVL 543
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEI-GMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 544 FGTTIMENIRFG-------KLEASDEEVYTAAREANAHEFITSfpEGYNTVVGergttLSGGQKQRLAIARALIKQPTVL 616
Cdd:PRK14239 98 FPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVLATSPKII 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 156105685 617 ILDEATSALDAESERVVQEALDRASAGRTVLVIAHRL 653
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
454-683 |
6.95e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.61 E-value: 6.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYpcRPG----FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDL--RTLDpS 527
Cdd:PRK13646 2 TIRFDNVSYTY--QKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthKTKD-K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 528 WLRG--QVVGFISQ--EPVLFGTTIMENIRFG--KLEASDEEVytaarEANAHEFITSFpeGYN-TVVGERGTTLSGGQK 600
Cdd:PRK13646 79 YIRPvrKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEV-----KNYAHRLLMDL--GFSrDVMSQSPFQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 601 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHE 677
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPK 231
|
....*.
gi 156105685 678 ELLKKG 683
Cdd:PRK13646 232 ELFKDK 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
470-679 |
7.93e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.07 E-value: 7.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLdgRDLRTLDPSWLRGQV---------------- 533
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELItnpyskkiknfkelrr 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 -VGFISQEP--VLFGTTIMENIRFG-------KLEASDEEVYTAAREANAHEFITSFPEGyntvvgergttLSGGQKQRL 603
Cdd:PRK13631 117 rVSMVFQFPeyQLFKDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYLERSPFG-----------LSGGQKRRV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 604 AIARALIKQPTVLILDEATSALDAESER-VVQEALDRASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEEL 679
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
465-692 |
1.09e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 94.70 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 465 PC-RPGFEVLkdfTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRT-LDPswLRgQVVGFISQEPV 542
Cdd:TIGR01257 940 PSgRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETnLDA--VR-QSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 LFG-TTIMENIRF-GKLEASDEEVYTAAREANAHEfitsfpEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDE 620
Cdd:TIGR01257 1014 LFHhLTVAEHILFyAQLKGRSWEEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 621 ATSALDAESERVVQEALDRASAGRTVLVIAHRL--STVRGAHcIVVMADGRVWEAGTheELLKKG----GLYAELIRR 692
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdeADLLGDR-IAIISQGRLYCSGT--PLFLKNcfgtGFYLTLVRK 1162
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
473-648 |
1.09e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.92 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDP---TAGVVMLDGRDLRTLdPSWLRGqvVGFISQEPVLFG-TTI 548
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAL-PAEQRR--IGILFQDDLLFPhLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 549 MENIRFG-----KLEASDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:COG4136 94 GENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190
....*....|....*....|....*....|
gi 156105685 624 ALDAE-----SERVVQEAldRASAGRTVLV 648
Cdd:COG4136 163 KLDAAlraqfREFVFEQI--RQRGIPALLV 190
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
478-679 |
1.42e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.89 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 478 LTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWL---RGQVVGFisQEPVLFGT-TIMENIr 553
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQiarMGVVRTF--QHVRLFREmTVIENL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 554 fgkLEASDEEVYT----------AAR--EANAHEFITSFPE--GYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:PRK11300 102 ---LVAQHQQLKTglfsgllktpAFRraESEALDRAATWLErvGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156105685 620 EATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEEL 679
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
472-670 |
1.47e-19 |
|
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: 86.72 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEP----VLFGTT 547
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 IMENIRFGKLeasdeevytaareanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQPTVLILDEATSALDA 627
Cdd:cd03215 95 VAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 156105685 628 ESERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 670
Cdd:cd03215 138 GAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
463-665 |
1.80e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.90 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 463 SYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGrdlrtldpswlrGQVVGFISQ--- 539
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------------GARVAYVPQrse 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 540 EPVLFGTTIMENIRFG---------KLEASDEEVYTAAREAnahefitsfpEGYNTVVGERGTTLSGGQKQRLAIARALI 610
Cdd:NF040873 66 VPDSLPLTVRDLVAMGrwarrglwrRLTRDDRAAVDDALER----------VGLADLAGRQLGELSGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 611 KQPTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRGAHCIVVM 665
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
458-698 |
3.70e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 88.32 E-value: 3.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYpcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFI 537
Cdd:PRK13652 7 RDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR-KFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 538 SQEP--VLFGTTIMENIRFGKL------EASDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIARAL 609
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFGPInlgldeETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 610 IKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLkkggLY 686
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIF----LQ 228
|
250
....*....|..
gi 156105685 687 AELIRRQALDAP 698
Cdd:PRK13652 229 PDLLARVHLDLP 240
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
469-679 |
4.92e-19 |
|
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: 86.27 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVVGFISQEPVL-FGTT 547
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVR-RRIGIVFQDLSVdDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 IMENIR-FGKLEAsdeeVYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 626
Cdd:cd03265 90 GWENLYiHARLYG----VPGAERRERIDELLDFV--GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 627 AESERVVQEALDR--ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEEL 679
Cdd:cd03265 164 PQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
472-672 |
5.00e-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: 87.55 E-value: 5.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG-----QVVGFISQEPVLFGT 546
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrdvQLVFQDSPSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 TIMENIR--FGKLEASDEevytAAREANAHEFITSFpEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 624
Cdd:TIGR02769 106 TVRQIIGepLRHLTSLDE----SEQKARIAELLDMV-GLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 156105685 625 LDAESERVVQEALD--RASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWE 672
Cdd:TIGR02769 181 LDMVLQAVILELLRklQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
467-672 |
8.21e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.05 E-value: 8.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--QVVGFISQEPV-- 542
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrRDIQMVFQDSIsa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 -----LFGTTIMENIRfgKLEASDEevytAAREANAHEFITSFpEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLI 617
Cdd:PRK10419 102 vnprkTVREIIREPLR--HLLSLDK----AERLARASEMLRAV-DLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156105685 618 LDEATSALDaeseRVVQ-EALD-----RASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWE 672
Cdd:PRK10419 175 LDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
454-694 |
1.32e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.90 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYPCRPG-------------------FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVV 514
Cdd:COG1134 4 MIEVENVSKSYRLYHEpsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 515 MLDGRdlrtldPSWLRGQVVGFisqEPVLFGttiMENIRF-----GkleASDEEVytAAREanahEFITSFPEgyntvVG 589
Cdd:COG1134 84 EVNGR------VSALLELGAGF---HPELTG---RENIYLngrllG---LSRKEI--DEKF----DEIVEFAE-----LG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 590 E------RgtTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRgAHC- 661
Cdd:COG1134 138 DfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVR-RLCd 214
|
250 260 270
....*....|....*....|....*....|....
gi 156105685 662 -IVVMADGRVWEAGTHEELLKkggLYAELIRRQA 694
Cdd:COG1134 215 rAIWLEKGRLVMDGDPEEVIA---AYEALLAGRE 245
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
478-679 |
3.70e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.06 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 478 LTLPPGKIVALVGQSGGGKTTVASLLERFY--DPTAG--------VVMLDGRDLRTLDPSwlRGQVvGFISQEPVLFGT- 546
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGshiellgrTVQREGRLARDIRKS--RANT-GYIFQQFNLVNRl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 TIMENIRFGKLEASD-----EEVYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:PRK09984 102 SVLENVLIGALGSTPfwrtcFSWFTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156105685 622 TSALDAESERVVQEALD--RASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEEL 679
Cdd:PRK09984 180 IASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
458-674 |
4.04e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.22 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYPCRPGF--------EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYdPTAGVVMLDGRDLRTLDPSWL 529
Cdd:PRK15134 279 EQLQVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 530 -----RGQVVgFisQEP--VLFGTTIMENIRFGKLEASDEEVYTAAREAnahEFITSFPE-GYNTVVGER-GTTLSGGQK 600
Cdd:PRK15134 358 lpvrhRIQVV-F--QDPnsSLNPRLNVLQIIEEGLRVHQPTLSAAQREQ---QVIAVMEEvGLDPETRHRyPAEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 601 QRLAIARALIKQPTVLILDEATSALDaeseRVVQE---ALDRASAGR---TVLVIAHRLSTVRG-AHCIVVMADGRVWEA 673
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQ 507
|
.
gi 156105685 674 G 674
Cdd:PRK15134 508 G 508
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
455-651 |
4.30e-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: 81.34 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVmldgrdlrtldpSWLRGQVV 534
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------TWGSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQepvlfgttimenirfgkleasdeevytaareanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQPT 614
Cdd:cd03221 66 GYFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190
....*....|....*....|....*....|....*..
gi 156105685 615 VLILDEATSALDAESERVVQEALdRASAGrTVLVIAH 651
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
454-679 |
6.37e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 86.24 E-value: 6.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqv 533
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-ERG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 VGFISQEPVLF-GTTIMENIRFG-KLEAS-----DEEVYTAAREAN-AHefitsfpegyntVVGERGTTLSGGQKQRLAI 605
Cdd:PRK11000 77 VGMVFQSYALYpHLSVAENMSFGlKLAGAkkeeiNQRVNQVAEVLQlAH------------LLDRKPKALSGGQRQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 606 ARALIKQPTVLILDEATSALDAeSERV---VQEALDRASAGRTVLVIAH-RLSTVRGAHCIVVMADGRVWEAGTHEEL 679
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDA-ALRVqmrIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
472-680 |
6.51e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.94 E-value: 6.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF---YDP---TAGVVMLDGRDLRTLDPSWLRGQvVGFISQEPVLF- 544
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKE-VGMVFQQPNPFp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 545 GTTIMENIRFG-KLEASDEEVYTAAREANAHEFITSFPEGYNTvVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:PRK14246 104 HLSIYDNIAYPlKSHGIKEKREIKKIVEECLRKVGLWKEVYDR-LNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 624 ALDAESERVVQEALDRASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELL 680
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
469-680 |
7.97e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.38 E-value: 7.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGV-----VMLDGRDLRTLDPSWLRGQVVGFISQEPVL 543
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 544 FGTTIMENI----RFGKLEASDEevYTAAREANAHEfiTSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:PRK14271 113 FPMSIMDNVlagvRAHKLVPRKE--FRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156105685 620 EATSALDAESERVVQEALDRASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEELL 680
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
467-651 |
1.28e-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: 81.77 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGqvVGFISQEPVLFGT 546
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG--LLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 -TIMENIRFGKLEASDEEVYTAAREANAHEFiTSFPEGYntvvgergttLSGGQKQRLAIARALIKQPTVLILDEATSAL 625
Cdd:cd03231 88 lSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*..
gi 156105685 626 DAESERVVQEAL-DRASAGRTVLVIAH 651
Cdd:cd03231 157 DKAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
477-680 |
1.33e-17 |
|
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: 86.39 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 477 TLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML----DGRDLRTLDPSwLRGQV---VGFISQEPVLFG-TTI 548
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRAkryIGILHQEYDLYPhRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 549 MENIRFG-KLEASDEevyTAAREANAHEFITSFPEGYNTVVGERGT-TLSGGQKQRLAIARALIKQPTVLILDEATSALD 626
Cdd:TIGR03269 383 LDNLTEAiGLELPDE---LARMKAVITLKMVGFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 627 AESERVVQEAL--DRASAGRTVLVIAHRLSTVRGAhC--IVVMADGRVWEAGTHEELL 680
Cdd:TIGR03269 460 PITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDV-CdrAALMRDGKIVKIGDPEEIV 516
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
458-679 |
1.37e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.64 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlRGQVVG-- 535
Cdd:PRK15439 15 RSISKQYS---GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA--KAHQLGiy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 536 FISQEPVLFGT-TIMENIRFG--KLEASDEEVYTAAREANAHeFITSFPEGyntvvgergtTLSGGQKQRLAIARALIKQ 612
Cdd:PRK15439 90 LVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQ-LDLDSSAG----------SLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 613 PTVLILDEATSALD-AESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEEL 679
Cdd:PRK15439 159 SRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
447-674 |
1.43e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.83 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 447 PKEQLRGSVTfqnvcfSYPCRPGF------EV--LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDG 518
Cdd:PRK10261 312 PILQVRNLVT------RFPLRSGLlnrvtrEVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 519 RDLRTLDPSWLRG--QVVGFISQEPV-------LFGTTIMENIRFGKLEASDEevyTAAREANAHEFITSFPEGYNTVVG 589
Cdd:PRK10261 386 QRIDTLSPGKLQAlrRDIQFIFQDPYasldprqTVGDSIMEPLRVHGLLPGKA---AAARVAWLLERVGLLPEHAWRYPH 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 590 ErgttLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALD-RASAGRTVLVIAHRLSTV-RGAHCIVVMA 666
Cdd:PRK10261 463 E----FSGGQRQRICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDlQRDFGIAYLFISHDMAVVeRISHRVAVMY 538
|
....*...
gi 156105685 667 DGRVWEAG 674
Cdd:PRK10261 539 LGQIVEIG 546
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
453-699 |
1.73e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 453 GSVTFQNVCFSYPCRPGFE--VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF------------YDPTAGVVML-D 517
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEfkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetgqtivgdYAIPANLKKIkE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 518 GRDLRtldpswlrgQVVGFISQEP--VLFGTTIMENIRFG--KLEASDEEVYTAAREANAhefITSFPEGYntvVGERGT 593
Cdd:PRK13645 85 VKRLR---------KEIGLVFQFPeyQLFQETIEKDIAFGpvNLGENKQEAYKKVPELLK---LVQLPEDY---VKRSPF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 594 TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RGAHCIVVMADGRV 670
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKV 229
|
250 260
....*....|....*....|....*....
gi 156105685 671 WEAGTHEELLKKgglyAELIRRQALDAPR 699
Cdd:PRK13645 230 ISIGSPFEIFSN----QELLTKIEIDPPK 254
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
456-667 |
1.86e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.91 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 456 TFQNVCFSYPCRpgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVG 535
Cdd:PRK10575 13 ALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 536 FISQEPVLFGTTIMENI------------RFGKL--EASDEEVYTAAREANAHEFITSfpegyntvvgergttLSGGQKQ 601
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVaigrypwhgalgRFGAAdrEKVEEAISLVGLKPLAHRLVDS---------------LSGGERQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 602 RLAIARALIKQPTVLILDEATSALDaeservVQEALDrasagrtVLVIAHRLSTVRGAHCIVVMAD 667
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALD------IAHQVD-------VLALVHRLSQERGLTVIAVLHD 207
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
474-679 |
2.19e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.99 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 474 KDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--QVVGFISQEPV-------LF 544
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrSDIQMIFQDPLaslnprmTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 545 GTTIMENIRFGKLEASDEEVYTAAREANA-------------HEFitsfpegyntvvgergttlSGGQKQRLAIARALIK 611
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSRQEVKDRVKAMMLkvgllpnlinrypHEF-------------------SGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156105685 612 QPTVLILDEATSALDAESE-RVVQ--EALDRaSAGRTVLVIAHRLSTVRgaHC---IVVMADGRVWEAGTHEEL 679
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQaQVVNllQQLQR-EMGLSLIFIAHDLAVVK--HIsdrVLVMYLGHAVELGTYDEV 249
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
181-428 |
2.64e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 83.38 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:cd18565 60 TVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 261 TQVAGCLVSLSMLSTRLTLLLMVATPaLMGVGTLMGSG-LRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEER 339
Cdd:cd18565 140 VTVLGIGAILFYLNWQLALVALLPVP-LIIAGTYWFQRrIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERER 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 340 YGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLV------AGQQLTGGDLMSFLVASQTVQRSMANLSV 413
Cdd:cd18565 219 VADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVldgpplFTGTLTVGTLVTFLFYTQRLLWPLTRLGD 298
|
250
....*....|....*
gi 156105685 414 LFGQVVRGLSAGARV 428
Cdd:cd18565 299 LIDQYQRAMASAKRV 313
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
468-668 |
2.92e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.61 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQE-PVLFGT 546
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 TIMENIRFGKLEAsdEEV-------YTAARE-ANAHEFITSFPEGYNTVVGErgttLSGGQKQRLAIARALIKQPTVLIL 618
Cdd:PRK09700 96 TVLENLYIGRHLT--KKVcgvniidWREMRVrAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 156105685 619 DEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRgAHC--IVVMADG 668
Cdd:PRK09700 170 DEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIR-RICdrYTVMKDG 221
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
165-428 |
3.05e-17 |
|
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: 83.09 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 165 DHVGSFMTESQNLSTHLLILYGVQ-GLLTFGYL--VLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTD 241
Cdd:cd18558 46 SSAGPFEKLEEEMTLYAYYYLIIGaIVLITAYIqgSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 242 VQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEAL 321
Cdd:cd18558 126 VSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 322 GNVRTVRAFAMEQREEERYGAELEAcrcrAEELGRGIALFQGLSNIAFNCMVLGT----LFIGGSLVAGQQLTGGDlmsf 397
Cdd:cd18558 206 EAFRTVIAFGGQQKEETRYAQNLEI----AKRNGIKKAITFNISMGAAFLLIYASyalaFWYGTYLVTQQEYSIGE---- 277
|
250 260 270
....*....|....*....|....*....|.
gi 156105685 398 lvasqtvqrsmaNLSVLFGQVVRGLSAGARV 428
Cdd:cd18558 278 ------------VLTVFFSVLIGAFSAGQQV 296
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
455-652 |
4.10e-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: 79.12 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAG-VVMLDGRDLRtldpswlrgqv 533
Cdd:cd03223 1 IELENLSLATP--DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGrIGMPEGEDLL----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 vgFISQEPVLFGTTIMENIrfgkleasdeeVYTAAREanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQP 613
Cdd:cd03223 68 --FLPQRPYLPLGTLREQL-----------IYPWDDV------------------------LSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 156105685 614 TVLILDEATSALDAESERVVQEALDRASAgrTVLVIAHR 652
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
463-670 |
5.64e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.31 E-value: 5.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 463 SYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL--ERfyDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQE 540
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLGVAYIPED 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 541 PVLFGT----TIMENIrfgKLEASDEEVYT-------AAREANAHEFITSF---PEGYNTVVGergtTLSGGQKQRLAIA 606
Cdd:COG3845 342 RLGRGLvpdmSVAENL---ILGRYRRPPFSrggfldrKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 607 RALIKQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTVRgAHC--IVVMADGRV 670
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEIL-ALSdrIAVMYEGRI 480
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
471-680 |
7.20e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.17 E-value: 7.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlRGQVVGFISQEPVLFGT---- 546
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDK--DGQLKVADKNQLRLLRTrltm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 -----------TIMENIrfgkLEASDEEVYTAAREANAHEFITSFPEGYN-TVVGERGTTLSGGQKQRLAIARALIKQPT 614
Cdd:PRK10619 97 vfqhfnlwshmTVLENV----MEAPIQVLGLSKQEARERAVKYLAKVGIDeRAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156105685 615 VLILDEATSALD----AESERVVQEAldrASAGRTVLVIAHRLSTVR--GAHcIVVMADGRVWEAGTHEELL 680
Cdd:PRK10619 173 VLLFDEPTSALDpelvGEVLRIMQQL---AEEGKTMVVVTHEMGFARhvSSH-VIFLHQGKIEEEGAPEQLF 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
471-715 |
7.37e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 7.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVvMLDGR--------DLRTLdpswlrgqvvgFisQEPV 542
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTaplaeareDTRLM-----------F--QDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 LFG-TTIMENIRFGkLEASDEEvytAAREANAhefitsfPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:PRK11247 92 LLPwKKVIDNVGLG-LKGQWRD---AALQALA-------AVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 622 TSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVrgahciVVMADgRVweagtheeLLKKGG-----LYAELIRRQA 694
Cdd:PRK11247 161 LGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSEA------VAMAD-RV--------LLIEEGkigldLTVDLPRPRR 225
|
250 260 270
....*....|....*....|....*....|..
gi 156105685 695 LDAPRTAA-----------PPPKKPEGPRSHQ 715
Cdd:PRK11247 226 RGSARLAEleaevlqrvmsRGESEPTRLRWAG 257
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
467-626 |
7.86e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.99 E-value: 7.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWlRGQVVGFISQEPvlfGT 546
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-RSQRIRMIFQDP---ST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 TIMENIRFGKL-------------EASDEEVYTAAREANA-HEFITSFPEgyntvvgergtTLSGGQKQRLAIARALIKQ 612
Cdd:PRK15112 99 SLNPRQRISQIldfplrlntdlepEQREKQIIETLRQVGLlPDHASYYPH-----------MLAPGQKQRLGLARALILR 167
|
170
....*....|....
gi 156105685 613 PTVLILDEATSALD 626
Cdd:PRK15112 168 PKVIIADEALASLD 181
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
472-670 |
8.85e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.90 E-value: 8.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGQVVGFISQEPVLfGT----T 547
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRAKYIGRVFQDPMM-GTapsmT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 IMEN------------IRFGKleasdeevyTAAREANAHEFITSFPEGY----NTVVGergtTLSGGQKQRLAIARALIK 611
Cdd:COG1101 99 IEENlalayrrgkrrgLRRGL---------TKKRRELFRELLATLGLGLenrlDTKVG----LLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 612 QPTVLILDEATSALD---AE-----SERVVQEaldrasAGRTVLVIAHRLS-TVRGAHCIVVMADGRV 670
Cdd:COG1101 166 KPKLLLLDEHTAALDpktAAlvlelTEKIVEE------NNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
181-428 |
2.35e-16 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 80.18 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRL--TTDVQEFKSSfkLVISQGLR 258
Cdd:cd18570 48 LILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFndANKIREAISS--TTISLFLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 259 SCTQVAGcLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAME----Q 334
Cdd:cd18570 126 LLMVIIS-GIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEeqflK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 335 REEERYGAELEACRcraeELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVL 414
Cdd:cd18570 205 KIEKKFSKLLKKSF----KLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINL 280
|
250
....*....|....
gi 156105685 415 FGQVVRGLSAGARV 428
Cdd:cd18570 281 QPKIQEAKVAADRL 294
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
470-652 |
2.54e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.46 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFY--DPTAGVVMLDGRDlrtldpswlrgqvvgfISQEpvlfgTT 547
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ----------------FGRE-----AS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 IMENIrfGKLEASDE--EVYTAAREANAHEFITSFPEgyntvvgergttLSGGQKQRLAIARALIKQPTVLILDEATSAL 625
Cdd:COG2401 102 LIDAI--GRKGDFKDavELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180
....*....|....*....|....*....
gi 156105685 626 DAESERVVQEALDRAS--AGRTVLVIAHR 652
Cdd:COG2401 168 DRQTAKRVARNLQKLArrAGITLVVATHH 196
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
463-674 |
4.24e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.81 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 463 SYPCRPGFEvlkDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLD--------------PSW 528
Cdd:PRK11701 15 LYGPRKGCR---DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseaerrrllrTEW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 529 lrgqvvGFISQEP-------VLFGTTIMEnirfgKLEASDEEVYTAAREANAH---------EFITSFPegyntvvgerg 592
Cdd:PRK11701 92 ------GFVHQHPrdglrmqVSAGGNIGE-----RLMAVGARHYGDIRATAGDwlerveidaARIDDLP----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 593 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAEservVQ-EALD--R---ASAGRTVLVIAHRLSTVRG-AHCIVVM 665
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQaRLLDllRglvRELGLAVVIVTHDLAVARLlAHRLLVM 225
|
....*....
gi 156105685 666 ADGRVWEAG 674
Cdd:PRK11701 226 KQGRVVESG 234
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
453-656 |
4.50e-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: 76.90 E-value: 4.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 453 GSVTFQNVCFSYPCRPGF-EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL-ERfydPTAGVV----MLDGrdlRTLDP 526
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKrQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR---KTAGVItgeiLING---RPLDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 527 SWLRgqVVGFISQEPVLFGT-TIMENIRFgkleasdeevytaarEANAhefitsfpegyntvvgeRGttLSGGQKQRLAI 605
Cdd:cd03232 76 NFQR--STGYVEQQDVHSPNlTVREALRF---------------SALL-----------------RG--LSVEQRKRLTI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 156105685 606 ARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV 656
Cdd:cd03232 120 GVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSAS 171
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
471-651 |
5.35e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 78.35 E-value: 5.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD--PTA---GVVMLDGRDLRT--LDPSWLRGQVvGFISQEPVL 543
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSpdVDPIEVRREV-GMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 544 F-GTTIMENIRFG----KLEAS----DEEVYTAAREANAHEFITSFPEGYntvvgerGTTLSGGQKQRLAIARALIKQPT 614
Cdd:PRK14267 97 FpHLTIYDNVAIGvklnGLVKSkkelDERVEWALKKAALWDEVKDRLNDY-------PSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 156105685 615 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAH 651
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
472-692 |
7.91e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.10 E-value: 7.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGQVVGFISQEPVLFG-TTIME 550
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY-ASKEVARRIGLLAQNATTPGdITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 551 NIR---------FGKLEASDEEVYTAAREANahefitsfpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:PRK10253 101 LVArgryphqplFTRWRKEDEEAVTKAMQAT----------GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156105685 622 TSALDAESERVVQEALDRAS--AGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEELLKkgglyAELIRR 692
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNreKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT-----AELIER 239
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
467-650 |
8.40e-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: 76.63 E-value: 8.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWlrGQVVGFISQEPVLFGT 546
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 -TIMENIRFGK--LEASDEEVYTAAREANAHEFiTSFPEGYntvvgergttLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:TIGR01189 88 lSALENLHFWAaiHGGAQRTIEDALAAVGLTGF-EDLPAAQ----------LSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*..
gi 156105685 624 ALDAESERVVQEALdRASAGRTVLVIA 650
Cdd:TIGR01189 157 ALDKAGVALLAGLL-RAHLARGGIVLL 182
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
171-651 |
8.71e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 81.00 E-value: 8.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 171 MTESQNLSTHLLILYGVQGLLTF----GYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFk 246
Cdd:COG4615 40 LNATGAALARLLLLFAGLLVLLLlsrlASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 247 SSFKLVISQGLRSCTQVAGCLVSLSMLStrLTLLLMVAtpALMGVGTLMGsglRKLSRQCQEQIARAMGVADEALGNVRT 326
Cdd:COG4615 119 SQAFVRLPELLQSVALVLGCLAYLAWLS--PPLFLLTL--VLLGLGVAGY---RLLVRRARRHLRRAREAEDRLFKHFRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 327 V----RAFAM-EQREEERYGAELEACRCRAEEL-GRGIALFqgLSNIAF-NCMVLGtlFIGGSLVAGQQLTGGDLmsfLV 399
Cdd:COG4615 192 LlegfKELKLnRRRRRAFFDEDLQPTAERYRDLrIRADTIF--ALANNWgNLLFFA--LIGLILFLLPALGWADP---AV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 400 ASQTVqrsmanLSVLF-----GQVVRGLSA--GARVfeymALN---------PCIPLSGGCCVPKEQLRG--SVTFQNVC 461
Cdd:COG4615 265 LSGFV------LVLLFlrgplSQLVGALPTlsRANV----ALRkieelelalAAAEPAAADAAAPPAPADfqTLELRGVT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 462 FSYPC---RPGFEVlKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGqvvgfis 538
Cdd:COG4615 335 YRYPGedgDEGFTL-GPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ------- 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 539 qepvLFgTTImenirFgkleaSD----EEVY---TAAREANAHEFITSFP-EGYNTVVGERGTT--LSGGQKQRLAIARA 608
Cdd:COG4615 407 ----LF-SAV-----F-----SDfhlfDRLLgldGEADPARARELLERLElDHKVSVEDGRFSTtdLSQGQRKRLALLVA 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 156105685 609 LIKQPTVLILDEATSALDAESERVVQEAL--DRASAGRTVLVIAH 651
Cdd:COG4615 472 LLEDRPILVFDEWAADQDPEFRRVFYTELlpELKARGKTVIAISH 516
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
472-672 |
9.35e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.13 E-value: 9.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP---SWLRGQVVGFISQEPVLFGT-T 547
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAKHVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 IMENIRFGKLEASDEEvytAAREANAHEFITSFPegyntvVGER----GTTLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:PRK10584 105 ALENVELPALLRGESS---RQSRNGAKALLEQLG------LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 156105685 624 ALDAES-ERVVQE--ALDRASAGRTVLVIAHRLSTVRGAHCIVVMaDGRVWE 672
Cdd:PRK10584 176 NLDRQTgDKIADLlfSLNREHGTTLILVTHDLQLAARCDRRLRLV-NGQLQE 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
467-677 |
1.24e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.62 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdpswLRGQVVGFISQE------ 540
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNLVAYVPQSeevdws 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 541 -PVLFGTTIMENiRFGKL------EASDEEVYTAAREAnahefiTSFPEGYNTVVGErgttLSGGQKQRLAIARALIKQP 613
Cdd:PRK15056 93 fPVLVEDVVMMG-RYGHMgwlrraKKRDRQIVTAALAR------VDMVEFRHRQIGE----LSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 614 TVLILDEATSALDAESE-RVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHE 677
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
472-651 |
1.47e-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: 76.54 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLERFYDpTAGVVMLDGRDLRtldpswlRGQV---VGFISQEPVLF 544
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPRK-------PDQFqkcVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 545 -GTTIMENIRFGKLEASDEEVYTAAREANAHefITSFPEGYNTVVG-ERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 622
Cdd:cd03234 94 pGLTVRETLTYTAILRLPRKSSDAIRKKRVE--DVLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|
gi 156105685 623 SALDAESERVVQEALDR-ASAGRTVLVIAH 651
Cdd:cd03234 172 SGLDSFTALNLVSTLSQlARRNRIVILTIH 201
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
476-682 |
2.97e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 77.64 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 476 FTLTLPPGKIVALVGQSGGGKTTVASLLERFYDP----TAGVVMLDGRDLRTLDPSWLR---GQVVGFISQEP------- 541
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRkiiGREIAMIFQEPsscldps 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 542 VLFGTTIMENIRFGKLEASDEEVYTAAREANA----------HEFI-TSFPEgyntvvgergtTLSGGQKQRLAIARALI 610
Cdd:COG4170 106 AKIGDQLIEAIPSWTFKGKWWQRFKWRKKRAIellhrvgikdHKDImNSYPH-----------ELTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 611 KQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKK 682
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARlnQLQGTSILLISHDLESIsQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
455-699 |
3.33e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.70 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSY-PCRP-GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAG------VVMLDGRDLRTLDP 526
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 527 swLRGQV-VGFISQEPVLFGTTIMENIRFG--KLEASDEEVYTAAreANAHEFITSFPEGYNTVVGErgttLSGGQKQRL 603
Cdd:PRK13643 82 --VRKKVgVVFQFPESQLFEETVLKDVAFGpqNFGIPKEKAEKIA--AEKLEMVGLADEFWEKSPFE----LSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 604 AIARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLK 681
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
250
....*....|....*...
gi 156105685 682 KgglyAELIRRQALDAPR 699
Cdd:PRK13643 234 E----VDFLKAHELGVPK 247
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
469-670 |
4.15e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.91 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRGQVvGFISQEP-VLF 544
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQI-GMIFQDHhLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 545 GTTIMENIRFGKL--EASDEE----VYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPTVLIL 618
Cdd:PRK10908 93 DRTVYDNVAIPLIiaGASGDDirrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 619 DEATSALD-AESERVVQ--EALDRasAGRTVLVIAHRLSTV-RGAHCIVVMADGRV 670
Cdd:PRK10908 162 DEPTGNLDdALSEGILRlfEEFNR--VGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
468-679 |
7.45e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.64 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQE----PVL 543
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQElhlvPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 544 fgtTIMENIRFGKLEAS-----DEEVYTAAREANAHEFITSFPegyNTVVGErgttLSGGQKQRLAIARALIKQPTVLIL 618
Cdd:PRK11288 95 ---TVAENLYLGQLPHKggivnRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 619 DEATSALDA-ESE---RVVQEALDRasaGRTVLVIAHRLSTV-RGAHCIVVMADGRvwEAGTHEEL 679
Cdd:PRK11288 165 DEPTSSLSArEIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGR--YVATFDDM 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
471-670 |
1.12e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.37 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLerF--YDPTAGVVMLDGRDLRTLDPS--WLRGqvVGFIS----QEPV 542
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIRLDGKPVRIRSPRdaIRAG--IAYVPedrkGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 LFGTTIMENI---------RFGKLEASDEEvytaareANAHEFITSF---PEGYNTVVGergtTLSGGQKQRLAIARALI 610
Cdd:COG1129 342 VLDLSIRENItlasldrlsRGGLLDRRRER-------ALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 611 KQPTVLILDEATSALD--AESE--RVVQEAldrASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 670
Cdd:COG1129 411 TDPKVLILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVISSELPELLGlSDRILVMREGRI 472
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
454-656 |
1.19e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.69 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYPCRpgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDpTAGVVMLDGR--------DLRTLD 525
Cdd:PRK14258 7 AIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqniYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 526 PSWLRGQVvGFISQEPVLFGTTIMENIRFG--------KLEAsDEEVYTAAREANAHEFITSfpegyntVVGERGTTLSG 597
Cdd:PRK14258 83 LNRLRRQV-SMVHPKPNLFPMSVYDNVAYGvkivgwrpKLEI-DDIVESALKDADLWDEIKH-------KIHKSALDLSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156105685 598 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV 656
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
469-682 |
1.38e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.15 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF--YDPTAGVVMLDgrdlRTLDPSWLRGQVVGFISQE-PVLFG 545
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYH----VALCEKCGYVERPSKVGEPcPVCGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 546 TTIMENIRFGKLeasDEEVYTAAREANAHEF----------------ITSFPE-GYN--------------TVVGERGT- 593
Cdd:TIGR03269 88 TLEPEEVDFWNL---SDKLRRRIRKRIAIMLqrtfalygddtvldnvLEALEEiGYEgkeavgravdliemVQLSHRITh 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 594 ---TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAsagrtvlVIAHRLSTVRGAHCIVVMAD--- 667
Cdd:TIGR03269 165 iarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEA-------VKASGISMVLTSHWPEVIEDlsd 237
|
250 260
....*....|....*....|..
gi 156105685 668 -------GRVWEAGTHEELLKK 682
Cdd:TIGR03269 238 kaiwlenGEIKEEGTPDEVVAV 259
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
469-680 |
2.63e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.00 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRD--LRTLDPSWLRGqvVGFISQEPVLFGT 546
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisLLPLHARARRG--IGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 TIMENIRFGKLEASDEeVYTAAREANAHEFITSFPEGYntVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 626
Cdd:PRK10895 93 LSVYDNLMAVLQIRDD-LSAEQREDRANELMEEFHIEH--LRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 627 AES----ERVVQEALDRasaGRTVLVIAHRL-STVRGAHCIVVMADGRVWEAGTHEELL 680
Cdd:PRK10895 170 PISvidiKRIIEHLRDS---GLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
471-705 |
3.75e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.51 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVA-SLLERFYDP----TAGVVMLDGRDLRTLDPSWLR---GQVVGFISQEPV 542
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRgvrGNKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 lfgttimenIRFGKLEASDEEVYTA-------AREANAHEFITSFPEgyntvVGERGTT---------LSGGQKQRLAIA 606
Cdd:PRK15134 103 ---------VSLNPLHTLEKQLYEVlslhrgmRREAARGEILNCLDR-----VGIRQAAkrltdyphqLSGGERQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 607 RALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLKKG 683
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAP 248
|
250 260
....*....|....*....|..
gi 156105685 684 glyAELIRRQALDAPRTAAPPP 705
Cdd:PRK15134 249 ---THPYTQKLLNSEPSGDPVP 267
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
468-653 |
4.22e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGT- 546
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 TIMENI--------RFGKLEASdeEVYtaaREANAHEFITSFPEGYNTVVGErgttLSGGQKQRLAIARALIKQPTVLIL 618
Cdd:PRK10762 95 TIAENIflgrefvnRFGRIDWK--KMY---AEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 156105685 619 DEATSAL-DAESE---RVVQEALDRasaGRTVLVIAHRL 653
Cdd:PRK10762 166 DEPTDALtDTETEslfRVIRELKSQ---GRGIVYISHRL 201
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
470-679 |
4.78e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.58 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSW--------------------- 528
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKekekvleklviqktrfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 529 ---LRGQV-VGFISQEPVLFGTTIMENIRFGKLE--ASDEEVYTAAREanaHEFITSFPEGYNtvvgERGT-TLSGGQKQ 601
Cdd:PRK13651 100 ikeIRRRVgVVFQFAEYQLFEQTIEKDIIFGPVSmgVSKEEAKKRAAK---YIELVGLDESYL----QRSPfELSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 602 RLAIARALIKQPTVLILDEATSALDAEServVQEALD----RASAGRTVLVIAHRLSTV--RGAHCIVVmADGR-VWEAG 674
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQG---VKEILEifdnLNKQGKTIILVTHDLDNVleWTKRTIFF-KDGKiIKDGD 248
|
....*
gi 156105685 675 THEEL 679
Cdd:PRK13651 249 TYDIL 253
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
474-679 |
8.02e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.04 E-value: 8.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 474 KDFTLTLPPGKIVALVGQSGGGKT-TVASLLERF---YDPTAGVVMLDGRdlrTLDPSWLRGQVVGFISQEP-------V 542
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGK---PVAPCALRGRKIATIMQNPrsafnplH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 LFGTTIMENIR-FGKLeaSDEEVYTAAREA----NAHEFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPTVLI 617
Cdd:PRK10418 97 TMHTHARETCLaLGKP--ADDATLTAALEAvgleNAARVLKLYP-----------FEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 618 LDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEEL 679
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
467-681 |
1.26e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.12 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVV----MLDGR------DLRTLDPSWL---RGQV 533
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkMLLRRrsrqviELSEQSAAQMrhvRGAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 VGFISQEPVL-------FGTTIMENIRFGKlEASDEEvytAAREANAHEFITSFPEGyNTVVGERGTTLSGGQKQRLAIA 606
Cdd:PRK10261 106 MAMIFQEPMTslnpvftVGEQIAESIRLHQ-GASREE---AMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 607 RALIKQPTVLILDEATSALDAESE-------RVVQEALDRAsagrtVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEE 678
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQ 255
|
...
gi 156105685 679 LLK 681
Cdd:PRK10261 256 IFH 258
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
471-698 |
1.64e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrTLDPSwLRG-----QVVGFISQEP--VL 543
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYS-KRGllalrQQVATVFQDPeqQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 544 FGTTIMENIRFG--KLEASDEEVYTAAREANahefitsfpegynTVVGERG------TTLSGGQKQRLAIARALIKQPTV 615
Cdd:PRK13638 91 FYTDIDSDIAFSlrNLGVPEAEITRRVDEAL-------------TLVDAQHfrhqpiQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 616 LILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKKGglyaELIRRQ 693
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACT----EAMEQA 233
|
....*
gi 156105685 694 ALDAP 698
Cdd:PRK13638 234 GLTQP 238
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
472-680 |
1.68e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 71.76 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrtldPSWLR------GQVVGFISQEPVLfg 545
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARharqrvGVVPQFDNLDPDF-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 546 tTIMENIR-FGKleasdeevYTAAREANAHEFITSFPE------GYNTVVGErgttLSGGQKQRLAIARALIKQPTVLIL 618
Cdd:PRK13537 96 -TVRENLLvFGR--------YFGLSAAAARALVPPLLEfaklenKADAKVGE----LSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156105685 619 DEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELL 680
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
475-679 |
2.17e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.06 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 475 DFTLTLPPGKIVALVGQSGGGKTTVA----SLLERfYDPTAGVVMLDGRDLRTLDPSWL---RGQVVGFISQEPVL---- 543
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAfalmGLLAA-NGRIGGSATFNGREILNLPEKELnklRAEQISMIFQDPMTslnp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 544 ---FGTTIMENI----RFGKLEASDEEV--YTAAREANAHEFITSFPEGYntvvgergttlSGGQKQRLAIARALIKQPT 614
Cdd:PRK09473 113 ymrVGEQLMEVLmlhkGMSKAEAFEESVrmLDAVKMPEARKRMKMYPHEF-----------SGGMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 615 VLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGAhC--IVVMADGRVWEAGTHEEL 679
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLNelKREFNTAIIMITHDLGVVAGI-CdkVLVMYAGRTMEYGNARDV 249
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
467-670 |
2.35e-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: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLERFYDPTaGVVMLDGRDLRTlDPSWLRGQVVgFISQEPV 542
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKE-FAEKYPGEII-YVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 LFGT-TIMENIRFgkleasdeevytaAREANAHEFItsfpegyntvvgeRGttLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:cd03233 94 HFPTlTVRETLDF-------------ALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156105685 622 TSALDAEServvqeALDRASAGRTvlvIAHRLSTVRGAHC-------------IVVMADGRV 670
Cdd:cd03233 146 TRGLDSST------ALEILKCIRT---MADVLKTTTFVSLyqasdeiydlfdkVLVLYEGRQ 198
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
468-669 |
2.42e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.04 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYdPTA---GVVMLDGRDLR--TLDPSWLRGQVVgfISQEPV 542
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQasNIRDTERAGIAI--IHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 LF-GTTIMENI-------RFGKLEasDEEVYTAAREANAHEFITSFPegyNTVVGErgttLSGGQKQRLAIARALIKQPT 614
Cdd:PRK13549 93 LVkELSVLENIflgneitPGGIMD--YDAMYLRAQKLLAQLKLDINP---ATPVGN----LGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 615 VLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTVRG-AHCIVVMADGR 669
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIrDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
456-651 |
3.27e-13 |
|
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: 72.66 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 456 TFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLerfydptAGVvmldgrDLRTLDPSWLR-GQVV 534
Cdd:TIGR03719 6 TMNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGV------DKDFNGEARPQpGIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVLFGT-TIMENIRFGKLEASD-----EEVYTAARE---------------------ANAHEFITSF------- 580
Cdd:TIGR03719 71 GYLPQEPQLDPTkTVRENVEEGVAEIKDaldrfNEISAKYAEpdadfdklaaeqaelqeiidaADAWDLDSQLeiamdal 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 581 --PEGYNTVvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES----ERVVQEaldraSAGrTVLVIAH 651
Cdd:TIGR03719 151 rcPPWDADV-----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE-----YPG-TVVAVTH 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
455-656 |
5.07e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRpgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswLRgqvV 534
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR---I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVLFGTTIMENIRFGKLE--ASDEEVYTAAREANAHEFItSFPEgyntvvgergTTLSGGQKQRLAIARALIKQ 612
Cdd:PRK09544 70 GYVPQKLYLDTTLPLTVNRFLRLRpgTKKEDILPALKRVQAGHLI-DAPM----------QKLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 156105685 613 PTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV 656
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDLHLV 184
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
175-414 |
6.39e-13 |
|
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: 69.90 E-value: 6.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 175 QNLSTHLLILYGVQGLLTFGYLV------LLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRL--TTDVQEF- 245
Cdd:cd18568 36 KNISLLNLILIGLLIVGIFQILLsavrqyLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFqeNQKIRRFl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 246 -KSSFKLVisqgLRSCTQVAgCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNV 324
Cdd:cd18568 116 tRSALTTI----LDLLMVFI-YLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 325 RTVRAFAMEQ----REEERYGAELEAcRCRAEELGRGIALFQGLSNIAFNCMVlgtLFIGGSLVAGQQLTGGDLMSFLVA 400
Cdd:cd18568 191 ATIKALAAERpirwRWENKFAKALNT-RFRGQKLSIVLQLISSLINHLGTIAV---LWYGAYLVISGQLTIGQLVAFNML 266
|
250
....*....|....
gi 156105685 401 SQTVQRSMANLSVL 414
Cdd:cd18568 267 FGSVINPLLALVGL 280
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
471-625 |
6.64e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.75 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFG-TTIM 549
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSrMTVE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 550 ENIRFGKLEASDEEVYTaaREANAHEFitsFPEGYNTVVgERGTTLSGGQKQRLAIARALIKQPTVLILDEATSAL 625
Cdd:PRK11614 99 ENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
448-656 |
8.53e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.06 E-value: 8.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 448 KEQLRGSVTF--QNVCFSYPCRPGFEV-LKDFTLTLPPGKIVALVGQSGGGKTTVASLL-ERFydpTAGVVMLDGR--DL 521
Cdd:TIGR00956 751 MEKESGEDIFhwRNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERV---TTGVITGGDRlvNG 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 522 RTLDPSWLRgqVVGFISQEPVLFGT-TIMENIRFGKL-----EASDEEVYTAAREANAHEFITSFPEGyntVVGERGTTL 595
Cdd:TIGR00956 828 RPLDSSFQR--SIGYVQQQDLHLPTsTVRESLRFSAYlrqpkSVSKSEKMEYVEEVIKLLEMESYADA---VVGVPGEGL 902
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156105685 596 SGGQKQRLAIARALIKQPTVLI-LDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV 656
Cdd:TIGR00956 903 NVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSAI 965
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
467-703 |
8.90e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.09 E-value: 8.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT-VASLLERFYDPTA-------GVVMLDGRDLRTLDPSWL-RGQVV--- 534
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTlLKALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLaRLRAVlpq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 ------GFISQEPVLFGtTIMENIRFGKLEASDEEVYTAAREAnahefitsfpEGYNTVVGERGTTLSGGQKQRLAIARA 608
Cdd:PRK13547 91 aaqpafAFSAREIVLLG-RYPHARRAGALTHRDGEIAWQALAL----------AGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 609 L---------IKQPTVLILDEATSALD-AESERVVQEALDRASAGRT-VLVIAHRLS-TVRGAHCIVVMADGRVWEAGTH 676
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGAP 239
|
250 260 270
....*....|....*....|....*....|...
gi 156105685 677 EELLKkgglyAELIRR------QALDAPRTAAP 703
Cdd:PRK13547 240 ADVLT-----PAHIARcygfavRLVDAGDGVPP 267
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
471-670 |
9.75e-13 |
|
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: 68.51 E-value: 9.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLR--GQVVGFISQE----PVLF 544
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRriGVVFGQKTQLwwdlPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 545 GTTIMENI------RFGKL--EASD-----EEVYTAAREanahefitsfpegyntvvgergttLSGGQKQRLAIARALIK 611
Cdd:cd03267 115 SFYLLAAIydlppaRFKKRldELSElldleELLDTPVRQ------------------------LSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156105685 612 QPTVLILDEATSALDAESERVVQEALDRASAGR--TVLVIAHRLSTV-RGAHCIVVMADGRV 670
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRL 232
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
470-669 |
1.07e-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: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGQVVgFISQEPVLFG 545
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKH-YRGDVV-YNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 546 T-TIMENIRFG--------KLEASDEEVYtAAREANAHEFITSFPEGYNTVVGE---RGttLSGGQKQRLAIARALIKQP 613
Cdd:TIGR00956 152 HlTVGETLDFAarcktpqnRPDGVSREEY-AKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 614 TVLILDEATSALDAEServvqeALDRASAGRTVLVIAHRLSTVRGAHC----------IVVMADGR 669
Cdd:TIGR00956 229 KIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVAIYQCsqdayelfdkVIVLYEGY 288
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
467-651 |
2.01e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 467 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLErfydPTAGVVMLDGRDLRTLDPswlrGQVVGFISQ--- 539
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTllrlIAGLLP----PAAGTIKLDGGDIDDPDV----AEACHYLGHrna 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 540 -EPVLfgtTIMENIRF-GKLEASDEEVYTAAREANAHEFITSFPEGYntvvgergttLSGGQKQRLAIARALIKQPTVLI 617
Cdd:PRK13539 84 mKPAL---TVAENLEFwAAFLGGEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*
gi 156105685 618 LDEATSALDAESERVVQEAL-DRASAGRTVLVIAH 651
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIrAHLAQGGIVIAATH 185
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
471-693 |
3.77e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.74 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL--ERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPV------ 542
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVeipgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 --LFGTTIMENIR-FGKLEASDEEVYTAAREANAHefITSFPEGYNTVVGERGttLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:PRK09580 95 nqFFLQTALNAVRsYRGQEPLDRFDFQDLMEEKIA--LLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 620 EATSALDAESERVVQEALDRASAG-RTVLVIAHR---LSTVRGAHcIVVMADGRVWEAGTH---EELLKKGglYAELIRR 692
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHYqriLDYIKPDY-VHVLYQGRIVKSGDFtlvKQLEEQG--YGWLTEQ 247
|
.
gi 156105685 693 Q 693
Cdd:PRK09580 248 Q 248
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
472-669 |
4.61e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.52 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLE-RFYDPT-AGVVMLDGRDLRTldPSWLRgqvVGFISQEPVLF-GTTI 548
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTK--QILKR---TGFVTQDDILYpHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 549 MENIRFGKL----EASDEEVYTAAREANAHEFITSFPEgyNTVVGE---RGttLSGGQKQRLAIARALIKQPTVLILDEA 621
Cdd:PLN03211 158 RETLVFCSLlrlpKSLTKQEKILVAESVISELGLTKCE--NTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 156105685 622 TSALDAESE-RVVQEALDRASAGRTVLVIAHRLST--VRGAHCIVVMADGR 669
Cdd:PLN03211 234 TSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
447-678 |
4.63e-12 |
|
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: 69.19 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 447 PKEQLRGSVT-FQNVCFSYPCRPGFEvlkDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML--------- 516
Cdd:TIGR03719 314 PGPRLGDKVIeAENLTKAFGDKLLID---DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayv 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 517 -DGRDlrTLDPS---WlrgqvvgfisqEPVLFGTTImenIRFGKleasdeevytaaREANAHEFITSFpegyN------- 585
Cdd:TIGR03719 391 dQSRD--ALDPNktvW-----------EEISGGLDI---IKLGK------------REIPSRAYVGRF----Nfkgsdqq 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 586 TVVGErgttLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDrASAGrTVLVIAH------RLSTvrga 659
Cdd:TIGR03719 439 KKVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL-NFAG-CAVVISHdrwfldRIAT---- 508
|
250 260
....*....|....*....|
gi 156105685 660 HCIVVMADGRV-WEAGTHEE 678
Cdd:TIGR03719 509 HILAFEGDSHVeWFEGNFSE 528
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
482-659 |
5.45e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 63.93 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 482 PGKIVALVGQSGGGKTTVASLLERFYDPT-AGVVMLDGRDLRTLDPSWLRgqvvgfisqepvlfgttimenirfgkleas 560
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 561 deevytaareanahefitsfpegyNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD-- 638
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180
....*....|....*....|....*.
gi 156105685 639 -----RASAGRTVLVIAHRLSTVRGA 659
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPA 132
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
145-394 |
7.54e-12 |
|
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: 66.75 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 145 NVQIPLLLGQLVevvakytrDHVGSFMTESQNLSTHLLILYGVQGLLT--FGYL--VLLSHVGERMAVDMRRALFSSLLR 220
Cdd:cd18582 12 NVAVPFLLKYAV--------DALSAPASALLAVPLLLLLAYGLARILSslFNELrdALFARVSQRAVRRLALRVFRHLHS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 221 QDITFFDANKTGQLVSrlttdvqefkssfklVISQGLRSCTQVAG------------CLVSLSMLSTRLTL---LLMVAT 285
Cdd:cd18582 84 LSLRFHLSRKTGALSR---------------AIERGTRGIEFLLRfllfnilptileLLLVCGILWYLYGWsyaLITLVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 286 PALMGVGTLMGSGLR-KLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGL 364
Cdd:cd18582 149 VALYVAFTIKVTEWRtKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIG 228
|
250 260 270
....*....|....*....|....*....|
gi 156105685 365 SNIAFNCMVLGTLFIGGSLVAGQQLTGGDL 394
Cdd:cd18582 229 QALIISLGLTAIMLLAAQGVVAGTLTVGDF 258
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
457-672 |
9.36e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 9.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 457 FQNVCFSYPcRPGFEVlKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGqvvgf 536
Cdd:PRK10522 325 LRNVTFAYQ-DNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK----- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 537 isqepvLFGTTIMENIRFGKL-----EASDEEVYTA--AREANAHEFitsfpegynTVVGERGTT--LSGGQKQRLAIAR 607
Cdd:PRK10522 398 ------LFSAVFTDFHLFDQLlgpegKPANPALVEKwlERLKMAHKL---------ELEDGRISNlkLSKGQKKRLALLL 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 608 ALIKQPTVLILDEATSALDAESERVV-QEALDRASA-GRTVLVIAHRLSTVRGAHCIVVMADGRVWE 672
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
469-669 |
9.41e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.93 E-value: 9.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 469 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYdPTA---GVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLF- 544
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAGIVIIHQELTLVp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 545 GTTIMENIRFG-KLEASDEEVYTAAREANAHEFI--TSFPEGYNT-VVGERGttlsGGQKQRLAIARALIKQPTVLILDE 620
Cdd:TIGR02633 92 ELSVAENIFLGnEITLPGGRMAYNAMYLRAKNLLreLQLDADNVTrPVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 156105685 621 ATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRgAHC--IVVMADGR 669
Cdd:TIGR02633 168 PSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVK-AVCdtICVIRDGQ 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
454-669 |
1.22e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.78 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrtldPSWLR--- 530
Cdd:PRK13536 41 AIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARlar 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 531 ---GQVVGFISQEPVLfgtTIMENI----RFGKLEASD-EEVYTAAREANAHEfitsfpegynTVVGERGTTLSGGQKQR 602
Cdd:PRK13536 114 ariGVVPQFDNLDLEF---TVRENLlvfgRYFGMSTREiEAVIPSLLEFARLE----------SKADARVSDLSGGMKRR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 603 LAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAH----------RLSTVRGAHCIvvmADGR 669
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHfmeeaerlcdRLCVLEAGRKI---AEGR 255
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
483-681 |
1.42e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 66.30 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 483 GKIVALVGQSGGGKTtVASLLERFYDPTAGVVM-----LDGRDLRTLDPSWLR---GQVVGFISQEPVL-------FGTT 547
Cdd:PRK11022 33 GEVVGIVGESGSGKS-VSSLAIMGLIDYPGRVMaekleFNGQDLQRISEKERRnlvGAEVAMIFQDPMTslnpcytVGFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 IMENIRFGKLEASdeevytAAREANAHEFITSF----PEGYNTVVGERgttLSGGQKQRLAIARALIKQPTVLILDEATS 623
Cdd:PRK11022 112 IMEAIKVHQGGNK------KTRRQRAIDLLNQVgipdPASRLDVYPHQ---LSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156105685 624 ALDAESE-RVVQEALDRASAGRTVLV-IAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLK 681
Cdd:PRK11022 183 ALDVTIQaQIIELLLELQQKENMALVlITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
475-678 |
1.44e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.44 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 475 DFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDL-----RTLDPSWLRGqvVGFISQEPVLF-GTTI 548
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekGICLPPEKRR--IGYVFQDARLFpHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 549 MENIRFGKLEASDEE----VYTAAREAnaheFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSA 624
Cdd:PRK11144 94 RGNLRYGMAKSMVAQfdkiVALLGIEP----LLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 156105685 625 LDAESERVVQEALDRASagRTV----LVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEE 678
Cdd:PRK11144 159 LDLPRKRELLPYLERLA--REInipiLYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
470-683 |
2.00e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.66 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 470 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF--YDPTAGVVMLDGRDLRTLDPSwLRGQVVGFIS-QEPV-LFG 545
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIFLAfQYPIeIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 546 TTimeNIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNtVVGERGTTL--------SGGQKQRLAIARALIKQPTVLI 617
Cdd:CHL00131 99 VS---NADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156105685 618 LDEATSALDAESERVVQEALDR-ASAGRTVLVIAH--RLSTVRGAHCIVVMADGRVWEAGTHE---ELLKKG 683
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElakELEKKG 246
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
151-397 |
2.08e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 65.22 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 151 LLGQLVEVVAKYTRDHVgsFMTESQNLSTHLLI----LYGVQGLLTF--GYLVLlsHVGERMAVDMRRALFSSLLRQDIT 224
Cdd:cd18555 16 LLTLLIPILTQYVIDNV--IVPGNLNLLNVLGIgiliLFLLYGLFSFlrGYIII--KLQTKLDKSLMSDFFEHLLKLPYS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 225 FFDANKTGQLVSRLT--TDVQEFKSSfkLVISqGLRSCTQVAGCLVSLSMLSTRLTLLLMVATpALMGVGTLMGSG-LRK 301
Cdd:cd18555 92 FFENRSSGDLLFRANsnVYIRQILSN--QVIS-LIIDLLLLVIYLIYMLYYSPLLTLIVLLLG-LLIVLLLLLTRKkIKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 302 LSRQCQEQIARAMGVADEALGNVRTVRAFAMEQRE----EERYGAELEAcrcrAEELGRGIALFQGLSNIAFNCMVLGTL 377
Cdd:cd18555 168 LNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIykkwENLFKKQLKA----FKKKERLSNILNSISSSIQFIAPLLIL 243
|
250 260
....*....|....*....|
gi 156105685 378 FIGGSLVAGQQLTGGDLMSF 397
Cdd:cd18555 244 WIGAYLVINGELTLGELIAF 263
|
|
| 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 |
2.09e-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: 65.30 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLttdvQEFKSSFKLVISQGLRSC 260
Cdd:cd18566 48 VVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL----NSLEQIREFLTGQALLAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 261 TQVAGCLVSLSM---LSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREE 337
Cdd:cd18566 124 LDLPFVLIFLGLiwyLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQML 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 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 |
2.98e-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: 64.56 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTLTLPPGKIVALVGQSGGGKTT---------VASLLERFYDPTAGVVMLDGrdLRTLDpswlrgQVVgFISQEPVl 543
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSlindtlypaLARRLHLKKEQPGNHDRIEG--LEHID------KVI-VIDQSPI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 544 fGTT----------IMENIR--F-------------------GK-----LEASDEEvytaareanAHEFITSFPE----- 582
Cdd:cd03271 81 -GRTprsnpatytgVFDEIRelFcevckgkrynretlevrykGKsiadvLDMTVEE---------ALEFFENIPKiarkl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 583 --------GYNTVvGERGTTLSGGQKQRLAIARALIKQ---PTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIA 650
Cdd:cd03271 151 qtlcdvglGYIKL-GQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIE 229
|
250
....*....|...
gi 156105685 651 HRLSTVRGAHCIV 663
Cdd:cd03271 230 HNLDVIKCADWII 242
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
468-672 |
4.01e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.97 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 468 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYdPTA---GVVMLDG--RDLRTLDPSWLRGQVVgfISQE-- 540
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGevCRFKDIRDSEALGIVI--IHQEla 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 541 --PVLfgtTIMENIRFGKLEASD-----EEVYTAAREANAHEFITSFPEgynTVVGERGTtlsgGQKQRLAIARALIKQP 613
Cdd:NF040905 89 liPYL---SIAENIFLGNERAKRgvidwNETNRRARELLAKVGLDESPD---TLVTDIGV----GKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156105685 614 TVLILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWE 672
Cdd:NF040905 159 KLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
455-679 |
5.77e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 63.63 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPGFEvlkDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--Q 532
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFD---NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 533 VVGFISQEPVLF-GTTIMENIRFGKLEasdeevYTAAREANAHEFITSFPEGyntvVGERG------TTLSGGQKQRLAI 605
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAYPLRE------HTQLPAPLLHSTVMMKLEA----VGLRGaaklmpSELSGGMARRAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 606 ARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEEL 679
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISElnSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
453-651 |
1.29e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 453 GSVTF--QNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLdGRDLR-------- 522
Cdd:PRK11147 316 GKIVFemENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEvayfdqhr 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 523 -TLDPSwlrgqvvgfisqepvlfgTTIMENIRFGKleasdEEVYTAAREANAHEFITSF---PEGYNTVVgergTTLSGG 598
Cdd:PRK11147 392 aELDPE------------------KTVMDNLAEGK-----QEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGG 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 156105685 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 |
1.69e-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: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRlttdVQEFKSSFKLVISQGLRSC 260
Cdd:cd18588 48 LLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVAR----VRELESIRQFLTGSALTLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 261 TQVAGCLVSLSML---STRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREE 337
Cdd:cd18588 124 LDLVFSVVFLAVMfyySPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQ 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 338 ERYGAELeacrcrAEELGRGIALfQGLSNIAFN-------CMVLGTLFIGGSLVAGQQLTGGDLMSF-LVASQTVQ 405
Cdd:cd18588 204 RRWEELL------ARYVKASFKT-ANLSNLASQivqliqkLTTLAILWFGAYLVMDGELTIGQLIAFnMLAGQVSQ 272
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
473-651 |
1.93e-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: 64.04 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTLTLPPGKI-----VALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswlrgqvvgfISQEPvlfgtt 547
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-----------------ISYKP------ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 imenirfGKLEA-SDEEVYTAAREANAHEFITSFpegYNTVVGER----------GTTLSGGQKQRLAIARALIKQPTVL 616
Cdd:COG1245 408 -------QYISPdYDGTVEEFLRSANTDDFGSSY---YKTEIIKPlgleklldknVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190
....*....|....*....|....*....|....*...
gi 156105685 617 ILDEATSALDAEsERV-VQEALDR--ASAGRTVLVIAH 651
Cdd:COG1245 478 LLDEPSAHLDVE-QRLaVAKAIRRfaENRGKTAMVVDH 514
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
454-627 |
2.10e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.94 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 454 SVTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLlERFydpTAGVVMLDGRDLRTLDPSwL 529
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTllrmVAGL-ERI---TSGEIWIGGRVVNELEPA-D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 530 RGQVVGFisQEPVLF-GTTIMENI-------RFGKLEAsDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQ 601
Cdd:PRK11650 76 RDIAMVF--QNYALYpHMSVRENMayglkirGMPKAEI-EERVAEAARILELEPLLDRKPR-----------ELSGGQRQ 141
|
170 180
....*....|....*....|....*.
gi 156105685 602 RLAIARALIKQPTVLILDEATSALDA 627
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
467-651 |
2.88e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 467 RPGFEVLkDFTLTlpPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLR-----GQVVGFisqEP 541
Cdd:PRK13538 14 RILFSGL-SFTLN--AGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdllylGHQPGI---KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 542 VLfgtTIMENIRF-GKL--EASDEevytAAREANAHefitsfpegyntvVGERGT------TLSGGQKQRLAIARALIKQ 612
Cdd:PRK13538 88 EL---TALENLRFyQRLhgPGDDE----ALWEALAQ-------------VGLAGFedvpvrQLSAGQQRRVALARLWLTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 156105685 613 PTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAH 651
Cdd:PRK13538 148 APLWILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
179-398 |
2.90e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 62.11 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 179 THLLILYG----VQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVIS 254
Cdd:cd18540 42 TGFILLYLglilIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 255 QGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQ 334
Cdd:cd18540 122 DLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREE 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 335 REEERYGAELEACRCRAEELGRGIALF----QGLSNIAfncmVLGTLFIGGSLVAGQQLTGGDLMSFL 398
Cdd:cd18540 202 KNLREFKELTEEMRRASVRAARLSALFlpivLFLGSIA----TALVLWYGGILVLAGAITIGTLVAFI 265
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
181-412 |
4.35e-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: 61.45 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRL--TTDVQEFkssfklVISQGLR 258
Cdd:cd18782 48 MLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIseLDTIRGF------LTGTALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 259 SCTQVA---GCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAME-- 333
Cdd:cd18782 122 TLLDVLfsvIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAElk 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 334 --QREEERYGAELEAcrcrAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANL 411
Cdd:cd18782 202 arWRWQNRYARSLGE----GFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRL 277
|
.
gi 156105685 412 S 412
Cdd:cd18782 278 S 278
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
476-696 |
5.93e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 476 FTLTLPPGKIVALVGQSGGGKTT----VASLLerfydPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFgttIMEN 551
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTllarMAGLL-----PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPF---AMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 552 IRFGKLEASDEeVYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQR-------LAIARALIKQPTVLILDEATSA 624
Cdd:PRK03695 87 FQYLTLHQPDK-TRTEAVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 625 LDaeserVVQE-ALDR-----ASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEELLKKGGL---YAELIRRQA 694
Cdd:PRK03695 164 LD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENLaqvFGVNFRRLD 238
|
..
gi 156105685 695 LD 696
Cdd:PRK03695 239 VE 240
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
473-680 |
8.16e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 8.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS-WLRGQVVgFISQEP----VLFGTT 547
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIV-YISEDRkrdgLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 IMENI----------RFGKLEASDEevytaaREAnAHEFITSF----PeGYNTVVGErgttLSGGQKQRLAIARALIKQP 613
Cdd:PRK10762 347 VKENMsltalryfsrAGGSLKHADE------QQA-VSDFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156105685 614 TVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRG-AHCIVVMADGRV-----WEAGTHEELL 680
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
477-680 |
1.26e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.20 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 477 TLTLPPGKIVALVGQSGGGKTTVASLL----ERFYDPTAGVVMLDGRDLRTLDPSWLR---GQVVGFISQEP-------V 542
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRklvGHNVSMIFQEPqscldpsE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 LFGTTIMENI-----------RFGKLEASDEEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIARALIK 611
Cdd:PRK15093 107 RVGRQLMQNIpgwtykgrwwqRFGWRKRRAIELLHRVGIKDHKDAMRSFP-----------YELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156105685 612 QPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELL 680
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRlnQNNNTTILLISHDLQMLsQWADKINVLYCGQTVETAPSKELV 247
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
468-651 |
1.99e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 468 PGFEVLKDFTLTLPPG-KIvALVGQSGGGKTTVASLLerfydptAGVvmldgrdlrtlDPS-----WLR-GQVVGFISQE 540
Cdd:PRK11819 18 PKKQILKDISLSFFPGaKI-GVLGLNGAGKSTLLRIM-------AGV-----------DKEfegeaRPApGIKVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 541 PVLFGT-TIMENIRFGKLEASD-----EEVY------------TAAREA---------NAHEfITS----------FPEG 583
Cdd:PRK11819 79 PQLDPEkTVRENVEEGVAEVKAaldrfNEIYaayaepdadfdaLAAEQGelqeiidaaDAWD-LDSqleiamdalrCPPW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156105685 584 YNTVvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES----ERVVQEaldraSAGrTVLVIAH 651
Cdd:PRK11819 158 DAKV-----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlEQFLHD-----YPG-TVVAVTH 218
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
573-679 |
2.78e-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: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 573 AHEFITSFPE-------------GYNTVvGERGTTLSGGQKQRLAIARALIKQ---PTVLILDEATSALDAESERVVQEA 636
Cdd:TIGR00630 796 AYEFFEAVPSisrklqtlcdvglGYIRL-GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEV 874
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 156105685 637 LDR-ASAGRTVLVIAHRLSTVRGAHCIVVM------ADGRVWEAGTHEEL 679
Cdd:TIGR00630 875 LQRlVDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
473-684 |
5.39e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.75 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLerfydptAGV-------VMLDGRDLRtlDPSWlRGQVVGFISQEPV--- 542
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGArkiqqgrVEVLGGDMA--DARH-RRAVCPRIAYMPQglg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 --LFGT-TIMENIRF-GKLEASDEevytAAREANAHEFITS-----FPE---GyntvvgergtTLSGGQKQRLAIARALI 610
Cdd:NF033858 87 knLYPTlSVFENLDFfGRLFGQDA----AERRRRIDELLRAtglapFADrpaG----------KLSGGMKQKLGLCCALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 611 KQPTVLILDEATSALDAESERVVQEALDRASAGR---TVLViahrlSTV------RGAHCiVVMADGRVWEAGTHEELLK 681
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLV-----ATAymeeaeRFDWL-VAMDAGRVLATGTPAELLA 226
|
...
gi 156105685 682 KGG 684
Cdd:NF033858 227 RTG 229
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
148-428 |
7.30e-09 |
|
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: 57.81 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 148 IPLLLGQLVevvaKYTRDHV--GSFMTESQNLStHLLILYGVQGLLtfgYLVL----------LSH-VGERMAVDMRRAL 214
Cdd:cd18554 14 IPLLLPLIL----KYIVDDViqGSSLTLDEKVY-KLFTIIGIMFFI---FLILrppveyyrqyFAQwIANKILYDIRKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 215 FSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTL 294
Cdd:cd18554 86 FDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 295 MGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVL 374
Cdd:cd18554 166 FFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 156105685 375 GTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 428
Cdd:cd18554 246 LVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
473-651 |
9.52e-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: 56.65 E-value: 9.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTLTLPPG-----KIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDlrtldpswlrgqvVGFISQEPVLFGTT 547
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-------------VSYKPQYIKADYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 IMENIRFGKLEASDEEVYTAAREANahefitsfPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDA 627
Cdd:cd03237 77 TVRDLLSSITKDFYTHPYFKTEIAK--------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180
....*....|....*....|....*.
gi 156105685 628 ESERVVQEALDR--ASAGRTVLVIAH 651
Cdd:cd03237 149 EQRLMASKVIRRfaENNEKTAFVVEH 174
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
452-685 |
1.84e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.59 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 452 RGSVTFQNVCFSYPCRPGFevlKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVmldgrdlrtldpSWLRG 531
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLF---KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSEN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 532 QVVGFISQEPVL-F--GTTIMENIRFGKLEASDEEVYtaareanahefitsfpegyntvvgeRGT--------------- 593
Cdd:PRK15064 382 ANIGYYAQDHAYdFenDLTLFDWMSQWRQEGDDEQAV-------------------------RGTlgrllfsqddikksv 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 594 -TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAgrTVLVIAH------RLSTvrgaHCIVVMA 666
Cdd:PRK15064 437 kVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSHdrefvsSLAT----RIIEITP 510
|
250
....*....|....*....
gi 156105685 667 DGRVWEAGTHEELLKKGGL 685
Cdd:PRK15064 511 DGVVDFSGTYEEYLRSQGI 529
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
473-651 |
2.03e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTLTLPPGKI-----VALVGQSGGGKTTVASLLERFYDPTAGVVMLDgrdlrtLD----PSWLR----GQVVGFISQ 539
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKisykPQYIKpdydGTVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 540 EPVLFGTTIMEnirfgkleasdeevytaareanaHEFItsFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILD 619
Cdd:PRK13409 424 ITDDLGSSYYK-----------------------SEII--KPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLD 478
|
170 180 190
....*....|....*....|....*....|....
gi 156105685 620 EATSALDAESERVVQEALDRASAGR--TVLVIAH 651
Cdd:PRK13409 479 EPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
471-684 |
2.16e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.93 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERfyDPTAGVVMLDGRdlrtldpswlrgqVVGFISQEPV---LFGTT 547
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-------------ISGFPKKQETfarISGYC 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 548 IMENIRFGKLEASDEEVYTA----AREANAHE---FITSFPEGY------NTVVGERGTT-LSGGQKQRLAIARALIKQP 613
Cdd:PLN03140 959 EQNDIHSPQVTVRESLIYSAflrlPKEVSKEEkmmFVDEVMELVeldnlkDAIVGLPGVTgLSTEQRKRLTIAVELVANP 1038
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156105685 614 TVLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTvrgahcivvmadgRVWEAGTHEELLKKGG 684
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI-------------DIFEAFDELLLMKRGG 1097
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
473-668 |
3.57e-08 |
|
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: 53.87 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTLTLPPGKIVALVGQSGGGKTTVasLLERFYdpTAGVVMLDGrDLRTLDPSWLrgqvvgfisqepvlfgttimenI 552
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLIS-FLPKFSRNKL----------------------I 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 553 RFGKLEasdeevytaareanaheFITSFPEGYNTVvGERGTTLSGGQKQRLAIARALIKQP--TVLILDEATSALDAESE 630
Cdd:cd03238 64 FIDQLQ-----------------FLIDVGLGYLTL-GQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 156105685 631 RVVQEALDR-ASAGRTVLVIAHRLSTVRGAHCIVVMADG 668
Cdd:cd03238 126 NQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
471-670 |
3.61e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP-----------------------S 527
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlarglvylpedrqssglyldA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 528 WLRGQVVGFISQEPVLFGTTIMENIRFgkleasdeevytaareanahefitsfpEGYNTVVGERGT-------TLSGGQK 600
Cdd:PRK15439 357 PLAWNVCALTHNRRGFWIKPARENAVL---------------------------ERYRRALNIKFNhaeqaarTLSGGNQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156105685 601 QRLAIARALIKQPTVLILDEATSALDAeSER--VVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 670
Cdd:PRK15439 410 QKVLIAKCLEASPQLLIVDEPTRGVDV-SARndIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
471-690 |
3.91e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.48 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 471 EVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLErfydPTAGVVMLDGRDlrtldPSWLRGQVVGFISqepVLFGT 546
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILV----PTSGEVRVLGYV-----PFKRRKEFARRIG---VVFGQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 547 --------TIMENIRFGKleasdeEVY---TAAREANAHEF-----ITSFpegYNTVVgeRgtTLSGGQKQRLAIARALI 610
Cdd:COG4586 104 rsqlwwdlPAIDSFRLLK------AIYripDAEYKKRLDELvelldLGEL---LDTPV--R--QLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 611 KQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRgAHC--IVVMADGRVWEAGTHEELLKKGGLY 686
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIE-ALCdrVIVIDHGRIIYDGSLEELKERFGPY 249
|
....
gi 156105685 687 AELI 690
Cdd:COG4586 250 KTIV 253
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
455-651 |
4.83e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYpcrpGFEVL-KDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML----------DGRDlrT 523
Cdd:PRK11819 325 IEAENLSKSF----GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvklayvdQSRD--A 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 524 LDPSwlrgqvvgfisqepvlfgTTIMENIrfgkleaSD--EEVYTAAREANAHEFITSFpegyntvvGERGT-------T 594
Cdd:PRK11819 399 LDPN------------------KTVWEEI-------SGglDIIKVGNREIPSRAYVGRF--------NFKGGdqqkkvgV 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 156105685 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 ... |
181-411 |
8.78e-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: 8.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTF--GYLVLlsHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRL--TTDVQEFkssfklvISQG 256
Cdd:cd18567 48 FGLLLLLQALLSAlrSWLVL--YLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFgsLDEIQQT-------LTTG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 257 LrsctqVAG------CLVSLSML---STRLTLLLMVATPALMGVGTLMgsgLRKLSRQCQEQI---ARAMGVADEALGNV 324
Cdd:cd18567 119 F-----VEAlldglmAILTLVMMflySPKLALIVLAAVALYALLRLAL---YPPLRRATEEQIvasAKEQSHFLETIRGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 325 RTVRAFameQREEERYGAELEAcrcRAEELGRGI------ALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL 398
Cdd:cd18567 191 QTIKLF---GREAEREARWLNL---LVDAINADIrlqrlqILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFL 264
|
250
....*....|...
gi 156105685 399 VASQTVQRSMANL 411
Cdd:cd18567 265 AYKDQFSSRASSL 277
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
459-652 |
1.16e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 459 NVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRGQV--VGF 536
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLcfVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 537 ISQ-EPVLfgtTIMENIRFgkleasdeEVYTAAREANAHEFITSFPEGYntVVGERGTTLSGGQKQRLAIARALIKQPTV 615
Cdd:PRK13540 82 RSGiNPYL---TLRENCLY--------DIHFSPGAVGITELCRLFSLEH--LIDYPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 156105685 616 LILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHR 652
Cdd:PRK13540 149 WLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
480-655 |
2.43e-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: 54.02 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 480 LP---PGKIVALVGQSGGGKTTVASLLerfydptAGVVM-----LDGrdlrtlDPSWlrgqvvgfisqEPVL--FGTTIM 549
Cdd:COG1245 93 LPvpkKGKVTGILGPNGIGKSTALKIL-------SGELKpnlgdYDE------EPSW-----------DEVLkrFRGTEL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 550 ENiRFGKLeaSDEEVyTAAREANAHEFITSFPEGynTV------VGERG-------------------TTLSGGQKQRLA 604
Cdd:COG1245 149 QD-YFKKL--ANGEI-KVAHKPQYVDLIPKVFKG--TVrellekVDERGkldelaeklglenildrdiSELSGGELQRVA 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 605 IARALIKQPTVLILDEATSALD----AESERVVQEAldrASAGRTVLVIAHRLST 655
Cdd:COG1245 223 IAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAI 274
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
476-703 |
3.00e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 476 FTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlRGQVVGFI-------SQEPVLFGTTI 548
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSP---RDAIRAGImlcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 549 MENI---------RFGKLEASDEEvytaarEANAHEFITSF----PEGYNTVVgergtTLSGGQKQRLAIARALIKQPTV 615
Cdd:PRK11288 349 ADNInisarrhhlRAGCLINNRWE------AENADRFIRSLniktPSREQLIM-----NLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 616 LILDEATSALD--AESErVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVweAGtheELLKkgglyAELIRR 692
Cdd:PRK11288 418 ILLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRI--AG---ELAR-----EQATER 486
|
250
....*....|...
gi 156105685 693 QALDA--PRTAAP 703
Cdd:PRK11288 487 QALSLalPRTSAA 499
|
|
| 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 156105685 594 TLSGGQKQRLAIARALIKQPTVLILDEATSALDAEsERV-VQEALDRASAGRTVLVIAHRL 653
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
455-659 |
3.50e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.41 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRpgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLrgqvv 534
Cdd:PRK13541 2 LSLHQLQFNIEQK----NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GFISQEPVL-FGTTIMENIRF-GKLEASDEEVYTAAREANAHEFITsfpegyntvvgERGTTLSGGQKQRLAIARALIKQ 612
Cdd:PRK13541 73 TYIGHNLGLkLEMTVFENLKFwSEIYNSAETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQ 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 156105685 613 PTVLILDEATSALDAESERVVQEALD-RASAGRTVLVIAHRLSTVRGA 659
Cdd:PRK13541 142 SDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSA 189
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
175-395 |
4.17e-07 |
|
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: 52.22 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 175 QNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTdVQEFKSSFKLVis 254
Cdd:cd18586 42 LGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELPLESRPSGYWQQLLRDLDT-LRNFLTGPSLF-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 255 qGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQ 334
Cdd:cd18586 119 -AFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLG 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156105685 335 REEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLM 395
Cdd:cd18586 198 NLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGELTIGALI 258
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
552-684 |
5.72e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.43 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 552 IRFGKLEA--SDEEVYTAAR---------EANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDE 620
Cdd:NF000106 93 VR*GRRESfsGRENLYMIGR*ldlsrkdaRARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 621 ATSALDAESERVV-QEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLKKGG 684
Cdd:NF000106 171 PTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
583-686 |
1.00e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 583 GYNTVVGergtTLSGGQKQRLAIARALIKQPTVLILDEATSALD--AESErVVQEALDRASAGRTVLVIAHRLSTVRG-A 659
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKFE-IYQLIAELAKKDKGIIIISSEMPELLGiT 458
|
90 100 110
....*....|....*....|....*....|....
gi 156105685 660 HCIVVMADGRVweAG-------THEELLKKGGLY 686
Cdd:PRK10982 459 DRILVMSNGLV--AGivdtkttTQNEILRLASLH 490
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
150-340 |
1.29e-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: 50.58 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 150 LLLGQLVEVVAKYTRDHVGSFMTESQNLSTHLLILY------GVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDI 223
Cdd:cd18580 8 LLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVyaallvLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 224 TFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTrltlLLMVATPALMGVGTLMGSGLRKLS 303
Cdd:cd18580 88 SFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP----YFLIVLPPLLVVYYLLQRYYLRTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 156105685 304 RQCQ--EQIARA--MGVADEALGNVRTVRAFAMEQREEERY 340
Cdd:cd18580 164 RQLRrlESESRSplYSHFSETLSGLSTIRAFGWQERFIEEN 204
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
595-654 |
1.30e-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: 1.30e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 595 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRasAGRTVLVIAHRLS 654
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKS 640
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
455-670 |
1.58e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 455 VTFQNVCFSYPCRPgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMldgRDLRTLDPSWLRGQVV 534
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---RSAKVRMAVFSQHHVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 GF-ISQEPVLFgttiMENIRFGKLEasdeevytaaREANAHefITSFPEGYNTVVgERGTTLSGGQKQRLAIARALIKQP 613
Cdd:PLN03073 584 GLdLSSNPLLY----MMRCFPGVPE----------QKLRAH--LGSFGVTGNLAL-QPMYTLSGGQKSRVAFAKITFKKP 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 614 TVLILDEATSALDAESERVVQEALDRASAGrtVLVIAHRLSTVRGA-HCIVVMADGRV 670
Cdd:PLN03073 647 HILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKV 702
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
459-669 |
1.77e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 459 NVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGR--DLRTLDPSWLRGqvVGF 536
Cdd:PRK10982 3 NISKSFP---GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSKEALENG--ISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 537 ISQE-PVLFGTTIMENIRFGK-----LEASDEEVYTAAREANAHEFITSFPEgyntvvgERGTTLSGGQKQRLAIARALI 610
Cdd:PRK10982 78 VHQElNLVLQRSVMDNMWLGRyptkgMFVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 611 KQPTVLILDEATSALdAESE-----RVVQEALDRasaGRTVLVIAHRLSTVRgAHC--IVVMADGR 669
Cdd:PRK10982 151 YNAKIVIMDEPTSSL-TEKEvnhlfTIIRKLKER---GCGIVYISHKMEEIF-QLCdeITILRDGQ 211
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
595-656 |
1.96e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 1.96e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 595 LSGGQkQRLA-IARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLV------------IAHRLSTV 656
Cdd:PRK10938 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacITHRLEFV 476
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
475-626 |
2.10e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 475 DFT------LTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML-----DGRDLRTldpswlRgQVVGFISQEPVL 543
Cdd:NF033858 278 DFTavdhvsFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDIAT------R-RRVGYMSQAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 544 FGT-TIMENIrfgKLEASDEEVYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 622
Cdd:NF033858 351 YGElTVRQNL---ELHARLFHLPAAEIAARVAEMLERF--DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
....
gi 156105685 623 SALD 626
Cdd:NF033858 426 SGVD 429
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
482-684 |
2.24e-06 |
|
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: 51.55 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 482 PGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVVGFISQEPVLfgttimenirfGKLEASD 561
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVH-QNMGYCPQFDAI-----------DDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 562 EEVYTAAR---------EANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERV 632
Cdd:TIGR01257 2031 EHLYLYARlrgvpaeeiEKVANWSIQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 633 VQEAL-DRASAGRTVLVIAHRLSTVRgAHC--IVVMADGRVWEAGTHEELLKKGG 684
Cdd:TIGR01257 2109 LWNTIvSIIREGRAVVLTSHSMEECE-ALCtrLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
593-708 |
2.42e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 593 TTLSGGQKQRLAIARALI---KQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMA-- 666
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGpe 887
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 156105685 667 ----DGRVWEAGTHEELLKKGGLYAELIR---RQALDAPRTAAPPPKKP 708
Cdd:PRK00635 888 ggnlGGYLLASCSPEELIHLHTPTAKALRpylSSPQELPYLPDPSPKPP 936
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
467-654 |
2.58e-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: 49.29 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 467 RPGFEVLKDFTLTLP-PGKIVALVGQSGGGKTTVASLLE--------RFYDPTAGVVMLD---GRDLRTLDPSWLRGQV- 533
Cdd:cd03236 9 RYGPNSFKLHRLPVPrEGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 534 ----VGFISQEPVLFGTTIMENirfgkLEASDEEvytaareaNAHEFITSFPEgYNTVVGERGTTLSGGQKQRLAIARAL 609
Cdd:cd03236 89 vivkPQYVDLIPKAVKGKVGEL-----LKKKDER--------GKLDELVDQLE-LRHVLDRNIDQLSGGELQRVAIAAAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 156105685 610 IKQPTVLILDEATSALDAESE----RVVQEaldRASAGRTVLVIAHRLS 654
Cdd:cd03236 155 ARDADFYFFDEPSSYLDIKQRlnaaRLIRE---LAEDDNYVLVVEHDLA 200
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
530-653 |
3.26e-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: 47.95 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 530 RGQVVGFISqePVLFGTTIMENIRFGKLEASDEEvytaareanahefiTSFPeGYNTVVGERGTTLSGGQKQRLAIARAL 609
Cdd:cd03222 24 EGEVIGIVG--PNGTGKTTAVKILAGQLIPNGDN--------------DEWD-GITPVYKPQYIDLSGGELQRVAIAAAL 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 156105685 610 IKQPTVLILDEATSALDAESERVVQEALDRAS--AGRTVLVIAHRL 653
Cdd:cd03222 87 LRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDL 132
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
593-653 |
3.28e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.80 E-value: 3.28e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 593 TTLSGGQKQRLAIARALIK---QPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRL 653
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRlVDKGNTVVVIEHNL 889
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
477-651 |
3.74e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.47 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 477 TLTLPPGkIVALVGQSGGGKTTVASLLER-FYDPTAGVVMLDgRDLRTLDPS------------------WLRGQVVGFI 537
Cdd:COG0419 18 TIDFDDG-LNLIVGPNGAGKSTILEAIRYaLYGKARSRSKLR-SDLINVGSEeasvelefehggkryrieRRQGEFAEFL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 538 SQEP--------VLFGTTIMENI--RFGKLEASDEEVYTAAREAN-AHEFITSFPEGYNTVvgergTTLSGGQKQRLAIA 606
Cdd:COG0419 96 EAKPserkealkRLLGLEIYEELkeRLKELEEALESALEELAELQkLKQEILAQLSGLDPI-----ETLSGGERLRLALA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 156105685 607 RALikqptVLILDeaTSALDAESERVVQEALDRASagrtvlVIAH 651
Cdd:COG0419 171 DLL-----SLILD--FGSLDEERLERLLDALEELA------IITH 202
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
149-390 |
4.53e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 49.02 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 149 PLLLGQLVEVVAKYTRDHVgsfmtesqnlsTHLLILYGVQGLLTFGYLVLLSHV---GERMAVDMRRALFSSL----LRQ 221
Cdd:cd18579 17 PLLLGLLISYLSSYPDEPL-----------SEGYLLALALFLVSLLQSLLLHQYfflSFRLGMRVRSALSSLIyrkaLRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 222 DITFFDANKTGQLVSRLTTDVQEFKSSFkLVISQGLRSCTQVAGCLVSLSML---STRLTLLLMVatpALMGVGTLMGSG 298
Cdd:cd18579 86 SSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALYLLYRLlgwAALAGLGVLL---LLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 299 LRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMeqreEERYGAELEAcrCRAEELG--RGIALFQGLSNIAFNCM-VLG 375
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAW----EKPFLKRIEE--LRKKELKalRKFGYLRALNSFLFFSTpVLV 235
|
250
....*....|....*.
gi 156105685 376 TLFIGGSLVA-GQQLT 390
Cdd:cd18579 236 SLATFATYVLlGNPLT 251
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
458-670 |
4.69e-06 |
|
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: 49.82 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 458 QNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKT-TVASLLERFYDPTAGVVMLDGRDLRTLDPS-WLRGQVV- 534
Cdd:TIGR02633 261 RNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVDIRNPAqAIRAGIAm 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 535 --------GFISQEPVLFGTTIMENIRFGKLEASDE--EVYTAAREANAHEFITSFPEgynTVVGergtTLSGGQKQRLA 604
Cdd:TIGR02633 341 vpedrkrhGIVPILGVGKNITLSVLKSFCFKMRIDAaaELQIIGSAIQRLKVKTASPF---LPIG----RLSGGNQQKAV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156105685 605 IARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 670
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
453-670 |
5.22e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.54 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 453 GSVTFQ--NVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKT-TVASLLERFYDPTAGVVMLDGRDLRTLDPSWL 529
Cdd:PRK13549 256 GEVILEvrNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 530 RGQVVGFISQEPVLFG-TTIM---ENI------RFGKLEASDEevytAAREANAHEFI------TSFPEgyntvvgERGT 593
Cdd:PRK13549 336 IAQGIAMVPEDRKRDGiVPVMgvgKNItlaaldRFTGGSRIDD----AAELKTILESIqrlkvkTASPE-------LAIA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 594 TLSGGQKQRLAIARALIKQPTVLILDEATSALD----AESERVVQEAldrASAGRTVLVIAHRLSTVRG-AHCIVVMADG 668
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakYEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEG 481
|
..
gi 156105685 669 RV 670
Cdd:PRK13549 482 KL 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
465-670 |
5.56e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 465 PCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVA-SLLERFYDP-TAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPV 542
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 543 LFGTTIMENIRF-------GKLeaSDEEVYTAAREAN-AHEFITSF----PEGYNTVVgergtTLSGGQKQRLAIARALI 610
Cdd:NF040905 348 GYGLNLIDDIKRnitlanlGKV--SRRGVIDENEEIKvAEEYRKKMniktPSVFQKVG-----NLSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 611 KQPTVLILDEATSALD--AESE--RVVQEAldrASAGRTVLVIAHRLSTVRGAhC--IVVMADGRV 670
Cdd:NF040905 421 TDPDVLILDEPTRGIDvgAKYEiyTIINEL---AAEGKGVIVISSELPELLGM-CdrIYVMNEGRI 482
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
175-418 |
7.88e-06 |
|
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: 48.28 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 175 QNLSTHLLILYGVQGLLTF----GYL--VLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRL--TTDVQEFk 246
Cdd:cd18783 36 QSYSTLYVLTIGVVIALLFegilGYLrrYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMqqIERIRQF- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 247 ssfklvISQGLRSCTQVAGCLV----SLSMLSTRLTLLLMVATPALMG-VGTLMGSGLRKLSRQCQEQIAR-AMGVadEA 320
Cdd:cd18783 115 ------LTGQLFGTLLDATSLLvflpVLFFYSPTLALVVLAFSALIALiILAFLPPFRRRLQALYRAEGERqAFLV--ET 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 321 LGNVRTVRAFAMEQREEERYGAEL-EACRcRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLV 399
Cdd:cd18783 187 VHGIRTVKSLALEPRQRREWDERVaRAIR-ARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNM 265
|
250
....*....|....*....
gi 156105685 400 ASQTVQRSMANLSVLFGQV 418
Cdd:cd18783 266 LAGRVAGPLVQLAGLVQEY 284
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
478-704 |
8.24e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 478 LTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAG--------VVMLDGRDLRTL-DPSWLRGQVvGFISQEPVLFGTTI 548
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshITRLSFEQLQKLvSDEWQRNNT-DMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 549 MENIRfgkleasdEEVYTAAReanAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE 628
Cdd:PRK10938 103 AEIIQ--------DEVKDPAR---CEQLAQQF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 629 SERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLKKgGLYAELIRRQALDA---PRTAAP 703
Cdd:PRK10938 170 SRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ-ALVAQLAHSEQLEGvqlPEPDEP 248
|
.
gi 156105685 704 P 704
Cdd:PRK10938 249 S 249
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
472-637 |
1.83e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 472 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDgrdlrtldpswlRGQVVGFISQEPVLFgttimen 551
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------------KGIKLGYFAQHQLEF------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 552 irfgkLEASDEEVYTAAR------EANAHEFITSFpeGYN-TVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 624
Cdd:PRK10636 388 -----LRADESPLQHLARlapqelEQKLRDYLGGF--GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170
....*....|...
gi 156105685 625 LDAESERVVQEAL 637
Cdd:PRK10636 461 LDLDMRQALTEAL 473
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
188-356 |
3.27e-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: 46.44 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 188 QGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFkSSFKLVISQGLRSCTQVAGCL 267
Cdd:cd18559 51 QGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRV-DSMAPQVIKMWMGPLQNVIGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 268 VSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAmeqrEEERYGAELEAc 347
Cdd:cd18559 130 YLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFE----WEEAFIRQVDA- 204
|
....*....
gi 156105685 348 rCRAEELGR 356
Cdd:cd18559 205 -KRDNELAY 212
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
583-686 |
4.25e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 583 GYNTVvGERGTTLSGGQKQRLAIARALIKQPT---VLILDEATSALDAESER----VVQEALDRasaGRTVLVIAHRLST 655
Cdd:PRK00349 820 GYIKL-GQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRklleVLHRLVDK---GNTVVVIEHNLDV 895
|
90 100 110
....*....|....*....|....*....|....*..
gi 156105685 656 VRGAHCIVVM------ADGRVWEAGTHEELLKKGGLY 686
Cdd:PRK00349 896 IKTADWIIDLgpeggdGGGEIVATGTPEEVAKVEASY 932
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
145-422 |
6.75e-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: 45.29 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 145 NVQIPLLLGQLVEVVAKYTRDHVGSFMTesqnlsthLLILYGVQGLL--TFGYL--VLLSHVGERMAVDMRRALFSSLLR 220
Cdd:cd18560 12 NVLAPLFLGRAVNALTLAKVKDLESAVT--------LILLYALLRFSskLLKELrsLLYRRVQQNAYRELSLKTFAHLHS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 221 QDITFFDANKTGQLVS---RLTTDVQEFKSSFKLVISQGLRSCtqVAGCLVSLSMLSTRLTLLLMVATpALMGVGTLMGS 297
Cdd:cd18560 84 LSLDWHLSKKTGEVVRimdRGTESANTLLSYLVFYLVPTLLEL--IVVSVVFAFHFGAWLALIVFLSV-LLYGVFTIKVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 298 GLR-KLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEAcrcrAEELGRGIALFQGLSNIA----FNCM 372
Cdd:cd18560 161 EWRtKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKE----YQKSSVKVQASLSLLNVGqqliIQLG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 156105685 373 VLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGL 422
Cdd:cd18560 237 LTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
181-398 |
7.24e-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: 45.23 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRL--TTDVQEfkssfkLVISQGLR 258
Cdd:cd18779 48 LAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLssNATIRE------LLTSQTLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 259 SC---TQVAGCLVSLSMLSTRLTLLLMVAtpALMGVGTLMGSG--LRKLSRQCQEQIARAMGVADEALGNVRTVRAFAME 333
Cdd:cd18779 122 ALldgTLVLGYLALLFAQSPLLGLVVLGL--AALQVALLLATRrrVRELMARELAAQAEAQSYLVEALSGIETLKASGAE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 334 QREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL 398
Cdd:cd18779 200 DRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALN 264
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
150-424 |
8.98e-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: 44.96 E-value: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 150 LLLGQLVEVVakYTRDHVGSFMTesqnLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDAN 229
Cdd:cd18561 17 WLLARALARI--FAGGPWEDIMP----PLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 230 KTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQ 309
Cdd:cd18561 91 RTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 310 IARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQL 389
Cdd:cd18561 171 YGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQL 250
|
250 260 270
....*....|....*....|....*....|....*
gi 156105685 390 TGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSA 424
Cdd:cd18561 251 TLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISA 285
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
484-526 |
1.06e-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: 43.89 E-value: 1.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 156105685 484 KIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP 526
Cdd:pfam06414 12 KAILLGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELHP 54
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
593-681 |
1.44e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 593 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRgAHC--IVVMADGR 669
Cdd:PRK09700 408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEII-TVCdrIAVFCEGR 486
|
90
....*....|....*...
gi 156105685 670 V------WEAGTHEELLK 681
Cdd:PRK09700 487 LtqiltnRDDMSEEEIMA 504
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
593-629 |
2.63e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 2.63e-04
10 20 30
....*....|....*....|....*....|....*..
gi 156105685 593 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES 629
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
181-380 |
2.95e-04 |
|
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: 43.29 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 181 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 260
Cdd:cd18605 48 YGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 261 TQVAGCLVSLSMLSTRLTLLLMVatpaLMGVGTLMGSGLRKLSRqcqeQIARAMGVA--------DEALGNVRTVRAFAM 332
Cdd:cd18605 128 FGLLGYLVVICYQLPWLLLLLLP----LAFIYYRIQRYYRATSR----ELKRLNSVNlsplythfSETLKGLVTIRAFRK 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 156105685 333 EQREEERYGAELEACRcRAEELGRGIAL-----FQGLSniafNCMVLGTLFIG 380
Cdd:cd18605 200 QERFLKEYLEKLENNQ-RAQLASQAASQwlsirLQLLG----VLIVTFVALTA 247
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
473-676 |
3.38e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.63 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 473 LKDFTLTLPPGKIVALVGQSGGGKTTVAsllerfYDptagVVMLDG--RDLRTLdPSWLRgQVVGFISQEPV-----LFG 545
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLA------FD----TIYAEGqrRYVESL-SAYAR-QFLGQMDKPDVdsiegLSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 546 TTIMENIRFGKLEASD----EEVYTA-----AREA--NAHEFITSFPEGYNTVvGERGTTLSGGQKQRLAIARALIKQPT 614
Cdd:cd03270 79 AIAIDQKTTSRNPRSTvgtvTEIYDYlrllfARVGirERLGFLVDVGLGYLTL-SRSAPTLSGGEAQRIRLATQIGSGLT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156105685 615 --VLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRGAHCIVVMADGrvweAGTH 676
Cdd:cd03270 158 gvLYVLDEPSIGLHPRDNDRLIETLKRlRDLGNTVLVVEHDEDTIRAADHVIDIGPG----AGVH 218
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
594-626 |
3.51e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 3.51e-04
10 20 30
....*....|....*....|....*....|...
gi 156105685 594 TLSGGQKQRLAIARALIKQPTVLILDEATSALD 626
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
478-653 |
4.55e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.58 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 478 LTLPPGKIVALVGQSGGGKTTVasllerfydptagvvmldgrdLRTldpswlrgqvVGFIsqepvLFGTtiMENIRFGKL 557
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTI---------------------LDA----------IGLA-----LGGA--QSATRRRSG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 558 EASDEEVytAAREAnahEFITSFPegyntvvgergtTLSGGQKQRLAIARAL----IKQPTVLILDEATSALDAESERVV 633
Cdd:cd03227 58 VKAGCIV--AAVSA---ELIFTRL------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQAL 120
|
170 180
....*....|....*....|.
gi 156105685 634 QEAL-DRASAGRTVLVIAHRL 653
Cdd:cd03227 121 AEAIlEHLVKGAQVIVITHLP 141
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
480-651 |
4.76e-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: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 480 LPPGKIVALVGQSGGGKTTVASLLerfydptaGVVMLDGRdlrtldpSWLRGQVVGfiSQEPVLFGTTIMENIRFGK-LE 558
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDL--------AAAVATGK-------PWLGGPRVP--EQGKVLYVSAEGPADELRRrLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 559 ASdeevyTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSAL-----DAESERVV 633
Cdd:pfam13481 93 AA-----GADLDLPARLLFLSLVESLPLFFLDRGGPLLDADVDALEAALEEVEDPDLVVIDPLARALggdenSNSDVGRL 167
|
170 180
....*....|....*....|
gi 156105685 634 QEALDRASA--GRTVLVIAH 651
Cdd:pfam13481 168 VKALDRLARrtGATVLLVHH 187
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
590-651 |
6.58e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.44 E-value: 6.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156105685 590 ERGTtLSGGQKQ------RLAIARALIKQPTVLILDEATSALDAES-ERVVQEALD--RASAGRTVLVIAH 651
Cdd:cd03240 112 MRGR-CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEerKSQKNFQLIVITH 181
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
315-422 |
1.44e-03 |
|
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: 41.36 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 315 GVADEALGNVRTVRAFAMEQREEERYGAELEACRcRAE-ELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGD 393
Cdd:cd18583 177 SILTESLLNWETVKYFNREPYEKERYREAVKNYQ-KAErKYLFSLNLLNAVQSLILTLGLLAGCFLAAYQVSQGQATVGD 255
|
90 100
....*....|....*....|....*....
gi 156105685 394 LMSFLVASQTVQRSMANLSVLFGQVVRGL 422
Cdd:cd18583 256 FVTLLTYWAQLSGPLNFFATLYRSIQSDL 284
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
172-272 |
2.67e-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: 40.54 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 172 TESQNLSTHLLILYG----VQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKS 247
Cdd:cd18603 34 TQDTEQRDYRLGVYGalglGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDN 113
|
90 100
....*....|....*....|....*
gi 156105685 248 SFKLVISQGLRSCTQVAGCLVSLSM 272
Cdd:cd18603 114 TLPQNIRSFLNCLFQVISTLVVISI 138
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| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
593-707 |
2.75e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 593 TTLSGGQKQRLAIARALIKQPT-VL-ILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMA--- 666
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIGSGLTgVLyVLDEPSIGLhQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIGpga 566
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 156105685 667 ---DGRVWEAGTHEELLKKG----GLYaeLIRRQALDAPRTAAPPPKK 707
Cdd:TIGR00630 567 gehGGEVVASGTPEEILANPdsltGQY--LSGRKKIEVPAERRPGNGK 612
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|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
187-242 |
4.05e-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: 39.77 E-value: 4.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 156105685 187 VQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDV 242
Cdd:cd18606 47 LQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDT 102
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| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
149-394 |
5.32e-03 |
|
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: 39.54 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 149 PLLLGQLVevvAKYTRDHVGSfMTESQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDA 228
Cdd:cd18594 17 PLLLGRLV---AYFVPDSTVT-KTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALSK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 229 NKTGQLVSRLTTDVQEFKSSFK----LVISQGLRSCTQV-------AGCLVSLSMLstrLTLLLMVAtpalmgvgtLMGS 297
Cdd:cd18594 93 ITTGHIVNLLSNDVQKFDEVLVylhfLWIAPLQVIVLTGllwreigPSSLAGLGVL---LLLLPLQA---------YLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 298 GLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMeqreEERYGAELEACRCRAEELGRGIALFQGLsNIAFncMVLGTL 377
Cdd:cd18594 161 LFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTW----EESFAKLIENIRKKELKLIRKAAYIRAF-NMAF--FFFSPT 233
|
250
....*....|....*..
gi 156105685 378 FIGGSLVAGQQLTGGDL 394
Cdd:cd18594 234 LVSFATFVPYVLTGNTL 250
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|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
582-651 |
6.07e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 582 EGYNTVVGERGT-----TLSGGQKQ------RLAIARALIKQPTVLILDEATSALDAESER----VVQEALDRASAGRTV 646
Cdd:PRK01156 784 QDFNITVSRGGMvegidSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTnlkdIIEYSLKDSSDIPQV 863
|
....*
gi 156105685 647 LVIAH 651
Cdd:PRK01156 864 IMISH 868
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
227-390 |
7.38e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 39.01 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 227 DANKTGQLVSRLTTDVQEFkSSFKLVISQGLRSCTQVAGCLVSLSMLstrltlllmVATPALMGVGTLMGSG-----LRK 301
Cdd:cd18596 110 SSASVGKINNLMSVDANRI-SEFAAFLHLLVSAPLQIVIAIVFLYRL---------LGWSALVGLAVMVLLLplngyLAK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156105685 302 LSRQCQEQIARA----MGVADEALGNVRTVRAFAMEQREEERYgaeLEAcrcRAEELG--RGIALFQGLSNIAFNCM-VL 374
Cdd:cd18596 180 RYSRAQKELMKArdarVQLVTEVLQGIRMIKFFAWERKWEERI---LEA---REEELKwlRKRFLLDLLLSLLWFLIpIL 253
|
170
....*....|....*...
gi 156105685 375 GTLFIGGS--LVAGQQLT 390
Cdd:cd18596 254 VTVVTFATytLVMGQELT 271
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