|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
49-609 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 587.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 49 LALGAALVNVQIPLLLGQLV-EVVAKYTRDHVGSfmtesqnLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALF 127
Cdd:COG1132 29 LLLLSALLELLLPLLLGRIIdALLAGGDLSALLL-------LLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 128 SSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLM 207
Cdd:COG1132 102 EHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 208 GSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLG 287
Cdd:COG1132 182 GRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 288 TLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFEYMALNPCIPLSGGCcVPKEQLRGSV 367
Cdd:COG1132 262 VLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGA-VPLPPVRGEI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 368 TFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvG 447
Cdd:COG1132 341 EFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQI-G 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 448 FISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTV 527
Cdd:COG1132 418 VVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPI 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 528 LILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQAL 607
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFG 577
|
..
gi 533869216 608 DA 609
Cdd:COG1132 578 EE 579
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
50-340 |
5.21e-166 |
|
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: 475.50 E-value: 5.21e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 50 ALGAALVNVQIPLLLGQLVEVVAKYTRDHVGSFMTESQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSS 129
Cdd:cd18574 5 ALAAALVNIQIPLLLGDLVNVISRSLKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 130 LLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGS 209
Cdd:cd18574 85 LLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 210 GLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTL 289
Cdd:cd18574 165 FLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGLSNLALNGIVLGVL 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 533869216 290 FIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18574 245 YYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
49-605 |
6.43e-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: 460.71 E-value: 6.43e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 49 LALGAALVNVQIPLLLGQLVEVVAkytrDHvgSFMTESQNLSTH----LLILYGVQGLLTFGYLVLLSHVGERMAVDMRR 124
Cdd:TIGR02204 22 AALVALLITAAATLSLPYAVRLMI----DH--GFSKDSSGLLNRyfafLLVVALVLALGTAARFYLVTWLGERVVADIRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 125 ALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVG 204
Cdd:TIGR02204 96 AVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 205 TLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEAC------RCRAEELGRGIALFQGLSN 278
Cdd:TIGR02204 176 LLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAyeaarqRIRTRALLTAIVIVLVFGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 279 IAfncmvlGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFEYMALNPCIPLSGGCCV 358
Cdd:TIGR02204 256 IV------GVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 359 PKEQLRGSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP 438
Cdd:TIGR02204 330 LPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 439 SWLRgQVVGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIA 518
Cdd:TIGR02204 410 AELR-ARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIA 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 519 RALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLY 598
Cdd:TIGR02204 489 RAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLY 568
|
....*..
gi 533869216 599 AELIRRQ 605
Cdd:TIGR02204 569 ARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
53-602 |
8.13e-155 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 462.65 E-value: 8.13e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 53 AALVNVQIPLLLGQLVEVVakytrdhVGSFMTESQNLSTHLLILYGVQGLLTFG-----YLVLLSHVGERMavdmRRALF 127
Cdd:TIGR00958 173 SSLGEMFIPFYTGRVIDTL-------GGDKGPPALASAIFFMCLLSIASSVSAGlrggsFNYTMARINLRI----REDLF 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 128 SSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLM 207
Cdd:TIGR00958 242 RSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVF 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 208 GSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACR--CRAEELGRgiALFQGLSNIAFNCMV 285
Cdd:TIGR00958 322 GKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLqlNKRKALAY--AGYLWTTSVLGMLIQ 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 286 LGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFEYMALNPCIPLSGGccVPKEQLRG 365
Cdd:TIGR00958 400 VLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGT--LAPLNLEG 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQV 445
Cdd:TIGR00958 478 LIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQV 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 VgFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQP 525
Cdd:TIGR00958 558 A-LVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKP 636
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 526 TVLILDEATSALDAESERVVQEalDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELI 602
Cdd:TIGR00958 637 RVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
93-606 |
1.95e-147 |
|
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: 443.51 E-value: 1.95e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRlttdVQEFKSSFKLVISQGLRSC 172
Cdd:COG2274 202 LLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASR----FRDVESIREFLTGSLLTAL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 173 TQVAGCLVSLSML---STRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREE 249
Cdd:COG2274 278 LDLLFVLIFLIVLffySPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFR 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 250 ERYgAELEACRCRAEELGRGIALFQGLSNIAFNCMV-LGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFG 328
Cdd:COG2274 358 RRW-ENLLAKYLNARFKLRRLSNLLSTLSGLLQQLAtVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQ 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 329 QVVRGLSAGARVFEYMALnPCIPLSGGCCVPKEQLRGSVTFQNVCFSYPcRPGFEVLKDFTLTLPPGKIVALVGQSGGGK 408
Cdd:COG2274 437 RFQDAKIALERLDDILDL-PPEREEGRSKLSLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGK 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 409 TTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEF 488
Cdd:COG2274 515 STLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQI-GVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDF 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 489 ITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTV 568
Cdd:COG2274 594 IEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTI 673
|
490 500 510
....*....|....*....|....*....|....*...
gi 533869216 569 RGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQA 606
Cdd:COG2274 674 RLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
367-605 |
1.71e-142 |
|
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: 413.47 E-value: 1.71e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVv 446
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPT 526
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 527 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 605
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
93-605 |
7.16e-128 |
|
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: 388.31 E-value: 7.16e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSS----FKLVISQG 168
Cdd:TIGR02203 60 VIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAatdaFIVLVRET 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 169 LrsctQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQRE 248
Cdd:TIGR02203 140 L----TVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 249 EERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFG 328
Cdd:TIGR02203 216 TRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 329 QVVRGLSAGARVFEYMAlNPCIPLSGGccVPKEQLRGSVTFQNVCFSYPCRpGFEVLKDFTLTLPPGKIVALVGQSGGGK 408
Cdd:TIGR02203 296 PMQRGLAAAESLFTLLD-SPPEKDTGT--RAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGK 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 409 TTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKL-EASDEEVYTAAREANAHE 487
Cdd:TIGR02203 372 STLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQV-ALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQD 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 488 FITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLST 567
Cdd:TIGR02203 451 FVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLST 530
|
490 500 510
....*....|....*....|....*....|....*...
gi 533869216 568 VRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 605
Cdd:TIGR02203 531 IEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
367-601 |
2.01e-120 |
|
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: 356.93 E-value: 2.01e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPGFeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVv 446
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPT 526
Cdd:cd03251 79 GLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 527 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAEL 601
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
93-606 |
2.20e-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: 364.91 E-value: 2.20e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLT--FGYL--VLLSHVGERMavdMRR-AL--FSSLLRQDITFFDANKTGQLvSRlttdvqefkssfklVI 165
Cdd:COG5265 80 LLLAYGLLRLLSvlFGELrdALFARVTQRA---VRRlALevFRHLHALSLRFHLERQTGGL-SR--------------DI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 166 SQGLRSctqvAGCLVSLSMLSTRLTLL--LMVA-----------------TPALMGVGTLMGSGLR-KLSRQCQEQIARA 225
Cdd:COG5265 142 ERGTKG----IEFLLRFLLFNILPTLLeiALVAgillvkydwwfalitlvTVVLYIAFTVVVTEWRtKFRREMNEADSEA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 226 MGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGD 305
Cdd:COG5265 218 NTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGD 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 306 LMsfLVASQTVQRSMA--NLSVLFGQVVRGLSAGARVFEYMALNPCI-------PLSGGccvpkeqlRGSVTFQNVCFSY 376
Cdd:COG5265 298 FV--LVNAYLIQLYIPlnFLGFVYREIRQALADMERMFDLLDQPPEVadapdapPLVVG--------GGEVRFENVSFGY 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 377 pcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLF 456
Cdd:COG5265 368 --DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLR-AAIGIVPQDTVLF 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 457 GTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 536
Cdd:COG5265 445 NDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 537 LDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQA 606
Cdd:COG5265 525 LDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
367-605 |
4.51e-116 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 345.75 E-value: 4.51e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 446
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLR-RAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPT 526
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 527 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 605
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
93-596 |
4.29e-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: 331.72 E-value: 4.29e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 172
Cdd:COG4988 64 LLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 173 TQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARamgVADEALGNVR---TVRAFAMEQREE 249
Cdd:COG4988 144 LVPLLILVAVFPLDWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALAR---LSGHFLDRLRgltTLKLFGRAKAEA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 250 ERYGAELEACRCRAEELGRgIALfqgLSN-----IAFNCMVLGTLFIGGSLVAGQqLTGGDLMSFLVASQTVQRSMANLS 324
Cdd:COG4988 221 ERIAEASEDFRKRTMKVLR-VAF---LSSavlefFASLSIALVAVYIGFRLLGGS-LTLFAALFVLLLAPEFFLPLRDLG 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 325 VLFGQVVRGLSAGARVFEYMALNPCIPLSGGCCVPKEQlRGSVTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQS 404
Cdd:COG4988 296 SFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 405 GGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREAN 484
Cdd:COG4988 373 GAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQI-AWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAG 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 485 AHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHR 564
Cdd:COG4988 452 LDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHR 531
|
490 500 510
....*....|....*....|....*....|..
gi 533869216 565 LSTVRGAHCIVVMADGRVWEAGTHEELLKKGG 596
Cdd:COG4988 532 LALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
110-604 |
4.84e-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: 324.03 E-value: 4.84e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 110 LLSH-VGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTR 188
Cdd:COG4987 77 LVSHdATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 189 LTLLLMVAtpaLMGVGTLMGSGLRKLSRQCQEQIARAMG----VADEALGNVRTVRAFAMEQREEERYgAELEACRCRAE 264
Cdd:COG4987 157 LALVLALG---LLLAGLLLPLLAARLGRRAGRRLAAARAalraRLTDLLQGAAELAAYGALDRALARL-DAAEARLAAAQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 265 E-LGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFEY 343
Cdd:COG4987 233 RrLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 344 MALNPCIPLSGGCCVPKEQlrGSVTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTA 423
Cdd:COG4987 313 LDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 424 GVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGER 503
Cdd:COG4987 390 GSITLGGVDLRDLDEDDLR-RRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEG 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 504 GTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVW 583
Cdd:COG4987 469 GRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
490 500
....*....|....*....|.
gi 533869216 584 EAGTHEELLKKGGLYAELIRR 604
Cdd:COG4987 549 EQGTHEELLAQNGRYRQLYQR 569
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
365-596 |
1.61e-102 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 310.70 E-value: 1.61e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 365 GSVTFQNVCFSYpcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQ 444
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 445 VvGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQ 524
Cdd:cd03254 79 I-GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 525 PTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGG 596
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
93-605 |
3.37e-102 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 322.35 E-value: 3.37e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTfGYLvlLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 172
Cdd:PRK11176 74 LMILRGITSFIS-SYC--ISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 173 TQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERY 252
Cdd:PRK11176 151 ASIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRF 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 253 GAELEACRCRAEEL--GRGIA--LFQGLSNIAFNCMvlgtLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFG 328
Cdd:PRK11176 231 DKVSNRMRQQGMKMvsASSISdpIIQLIASLALAFV----LYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 329 QVVRGLSAGARVFEYMALNPCIPlSGGCCVpkEQLRGSVTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGK 408
Cdd:PRK11176 307 QFQRGMAACQTLFAILDLEQEKD-EGKRVI--ERAKGDIEFRNVTFTYPGKEV-PALRNINFKIPAGKTVALVGRSGSGK 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 409 TTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLEA-SDEEVYTAAREANAHE 487
Cdd:PRK11176 383 STIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQV-ALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMD 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 488 FITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLST 567
Cdd:PRK11176 462 FINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLST 541
|
490 500 510
....*....|....*....|....*....|....*...
gi 533869216 568 VRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 605
Cdd:PRK11176 542 IEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
179-617 |
1.37e-95 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 305.35 E-value: 1.37e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 179 LVSLSM-LSTRLTLLLMVatpaLMGVGTLMGS-GLRK---LSRQCQEQIARAMGVADEALGNVRTVRAFAmeqreeeRYG 253
Cdd:PRK13657 147 LLPLALfMNWRLSLVLVV----LGIVYTLITTlVMRKtkdGQAAVEEHYHDLFAHVSDAIGNVSVVQSYN-------RIE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 254 AELEACRCRAEELGRG-------IALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL-VASQTVQRsmanLSV 325
Cdd:PRK13657 216 AETQALRDIADNLLAAqmpvlswWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVgFATLLIGR----LDQ 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 326 LFGQVVRGLSAGARVFEYMALNPCIPLSG--GCCVPKEQLRGSVTFQNVCFSYP-CRPGfevLKDFTLTLPPGKIVALVG 402
Cdd:PRK13657 292 VVAFINQVFMAAPKLEEFFEVEDAVPDVRdpPGAIDLGRVKGAVEFDDVSFSYDnSRQG---VEDVSFEAKPGQTVAIVG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 403 QSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAARE 482
Cdd:PRK13657 369 PTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR-RNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAER 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 483 ANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIA 562
Cdd:PRK13657 448 AQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIA 527
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 563 HRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQALDAPRTAAPPP 617
Cdd:PRK13657 528 HRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGMLQEDERRKQP 582
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
367-605 |
2.04e-93 |
|
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: 287.46 E-value: 2.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYpcRP-GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQV 445
Cdd:cd03252 1 ITFEHVRFRY--KPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 vGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQP 525
Cdd:cd03252 79 -GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 526 TVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 605
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
363-582 |
1.66e-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: 274.35 E-value: 1.66e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 363 LRGSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLR 442
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 443 GQVVgFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALI 522
Cdd:cd03248 88 SKVS-LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 523 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRV 582
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
48-603 |
1.07e-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: 282.60 E-value: 1.07e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 48 QLALGAALVNVQIPLLL---GQLVEVVAKYTRDHVgsFMTESQNLSTHLLILYGV----QGLLTFGYLVLLSHVGERMAV 120
Cdd:TIGR03796 150 RGSRGALLYLLLAGLLLvlpGLVIPAFSQIFVDEI--LVQGRQDWLRPLLLGMGLtallQGVLTWLQLYYLRRLEIKLAV 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 121 DMRRALFSSLLRQDITFFDANKTGQLVSRLTTD--VQEFKSSfklvisqglrsctQVAGCLVSLSMLSTRLtLLLMVATP 198
Cdd:TIGR03796 228 GMSARFLWHILRLPVRFFAQRHAGDIASRVQLNdqVAEFLSG-------------QLATTALDAVMLVFYA-LLMLLYDP 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 199 ALMGVGTLMG----------SGLRK-LSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERY-GAELEACRCRaEEL 266
Cdd:TIGR03796 294 VLTLIGIAFAainvlalqlvSRRRVdANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSRWaGYQAKLLNAQ-QEL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 267 GRGIALFQGLSNI--AFNCMVLgtLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLsVLFGQVVRGLSAGARVFEYM 344
Cdd:TIGR03796 373 GVLTQILGVLPTLltSLNSALI--LVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNL-VGFGGTLQELEGDLNRLDDV 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 345 ALNPCIPL------SGGCCVPKEQLRGSVTFQNVCFSYPcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF 418
Cdd:TIGR03796 450 LRNPVDPLleepegSAATSEPPRRLSGYVELRNITFGYS-PLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 419 YDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNT 498
Cdd:TIGR03796 529 YQPWSGEILFDGIPREEIPREVLANSV-AMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDA 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 499 VVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAsaGRTVLVIAHRLSTVRGAHCIVVMA 578
Cdd:TIGR03796 608 ELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRR--GCTCIIVAHRLSTIRDCDEIIVLE 685
|
570 580
....*....|....*....|....*
gi 533869216 579 DGRVWEAGTHEELLKKGGLYAELIR 603
Cdd:TIGR03796 686 RGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
51-340 |
2.49e-85 |
|
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: 268.66 E-value: 2.49e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 51 LGAALVNVQIPLLLGQLVEVVAKYTRDHVgsfmteSQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSL 130
Cdd:cd18557 6 LISSAAQLLLPYLIGRLIDTIIKGGDLDV------LNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 131 LRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSG 210
Cdd:cd18557 80 LRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 211 LRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLF 290
Cdd:cd18557 160 IRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 533869216 291 IGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18557 240 YGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
367-581 |
3.29e-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: 250.76 E-value: 3.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVv 446
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVLFGTTIMENIrfgkleasdeevytaareanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQPT 526
Cdd:cd03228 79 AYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 527 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGR 581
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
102-619 |
3.81e-73 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 245.39 E-value: 3.81e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 102 LLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQefkssfKLVISQGLRSCT----QVAG 177
Cdd:PRK10789 51 LLRYVWRVLLFGASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVD------RVVFAAGEGVLTlvdsLVMG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 178 CLVSLSM---LSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGA 254
Cdd:PRK10789 125 CAVLIVMstqISWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 255 ELEACRCRAEELGRGIALFQ-------GLSNIafncmvlgtLFIGGS--LVAGQQLTGGDLMSFLVASQTVQRSMANLSV 325
Cdd:PRK10789 205 DAEDTGKKNMRVARIDARFDptiyiaiGMANL---------LAIGGGswMVVNGSLTLGQLTSFVMYLGLMIWPMLALAW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 326 LFGQVVRGLSAGARVFEYMALNPCIpLSGGCCVPKEqlRGSVTFQNVCFSYP--CRPgfeVLKDFTLTLPPGKIVALVGQ 403
Cdd:PRK10789 276 MFNIVERGSAAYSRIRAMLAEAPVV-KDGSEPVPEG--RGELDVNIRQFTYPqtDHP---ALENVNFTLKPGQMLGICGP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 404 SGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREA 483
Cdd:PRK10789 350 TGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRL-AVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLA 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 484 NAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAH 563
Cdd:PRK10789 429 SVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 564 RLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQALDAPRTAAPPPKK 619
Cdd:PRK10789 509 RLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAALDDAPEIRE 564
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
117-605 |
1.64e-72 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 246.79 E-value: 1.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 117 RMAVDMRRALFSSLLRQDITFFDANKTGQLVSRlttdVQEFKSSFKLVISQGLRSCTQVAGCLVSLSML---STRLTLLL 193
Cdd:TIGR03797 206 RMDASLQAAVWDRLLRLPVSFFRQYSTGDLASR----AMGISQIRRILSGSTLTTLLSGIFALLNLGLMfyySWKLALVA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 194 MVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYgAELEACRCRAEELGRGIALF 273
Cdd:TIGR03797 282 VALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARW-AKLFSRQRKLELSAQRIENL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 274 QGLSNIAFNCMVLGTLF-IGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGAR---VFEymalnpC 349
Cdd:TIGR03797 361 LTVFNAVLPVLTSAALFaAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERakpILE------A 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 350 IPLSGGCCVPKEQLRGSVTFQNVCFSYPCRpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLD 429
Cdd:TIGR03797 435 LPEVDEAKTDPGKLSGAIEVDRVTFRYRPD-GPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYD 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 430 GRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIrFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSG 509
Cdd:TIGR03797 514 GQDLAGLDVQAVRRQL-GVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSG 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 510 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRtvLVIAHRLSTVRGAHCIVVMADGRVWEAGTHE 589
Cdd:TIGR03797 592 GQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYD 669
|
490
....*....|....*.
gi 533869216 590 ELLKKGGLYAELIRRQ 605
Cdd:TIGR03797 670 ELMAREGLFAQLARRQ 685
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
53-605 |
1.65e-71 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 241.93 E-value: 1.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 53 AALVNVQIPLLLgqlvevvaKYTRDHVgsfmtesqnLSTHLLILYGVQGLLTfGYLVL-----LSHVGE-----RMAVD- 121
Cdd:PRK10790 35 AAAAEVSGPLLI--------SYFIDNM---------VAKGNLPLGLVAGLAA-AYVGLqllaaGLHYAQsllfnRAAVGv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 122 ---MRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATP 198
Cdd:PRK10790 97 vqqLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 199 ALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFameqREEERYGAELEACRcRAEELGR-------GIA 271
Cdd:PRK10790 177 AVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQF----RQQARFGERMGEAS-RSHYMARmqtlrldGFL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 272 LFQGLSniAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL---------VASQTVQRSMANLSVLfgqvvrglsAGARVFE 342
Cdd:PRK10790 252 LRPLLS--LFSALILCGLLMLFGFSASGTIEVGVLYAFIsylgrlnepLIELTTQQSMLQQAVV---------AGERVFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 343 YMAL------NPCIPLSGGccvpkeqlrgSVTFQNVCFSYpcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLE 416
Cdd:PRK10790 321 LMDGprqqygNDDRPLQSG----------RIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 417 RFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKlEASDEEVYTAAREANAHEFITSFPEGY 496
Cdd:PRK10790 389 GYYPLTEGEIRLDGRPLSSLSHSVLR-QGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 497 NTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVV 576
Cdd:PRK10790 467 YTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILV 546
|
570 580
....*....|....*....|....*....
gi 533869216 577 MADGRVWEAGTHEELLKKGGLYAELIRRQ 605
Cdd:PRK10790 547 LHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
86-594 |
2.94e-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: 237.72 E-value: 2.94e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 86 SQNLSTHL------LILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANkTGQLVSRLTTdVQEFKS 159
Cdd:COG4618 53 SRSVDTLLmltllaLGLYAVMGLLDAVRSRILVRVGARLDRRLGPRVFDAAFRAALRGGGGA-AAQALRDLDT-LRQFLT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 160 SfklvisQGLrsctqVAGC--------LVSLSMLSTRLTLLlmvatpALMGVGTLMGSGL------RKLSRQCQEQIARA 225
Cdd:COG4618 131 G------PGL-----FALFdlpwapifLAVLFLFHPLLGLL------ALVGALVLVALALlnerltRKPLKEANEAAIRA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 226 MGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLS---NIAFNCMVLGTlfiGGSLVAGQQLT 302
Cdd:COG4618 194 NAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAGGFSALSkflRLLLQSAVLGL---GAYLVIQGEIT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 303 GGDLM--SFLVAsqtvqRSMANLSVLFG---QVVRGLSAGARVFEYMALNPCIPlsggccvPKEQL---RGSVTFQNVCF 374
Cdd:COG4618 271 PGAMIaaSILMG-----RALAPIEQAIGgwkQFVSARQAYRRLNELLAAVPAEP-------ERMPLprpKGRLSVENLTV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 375 SYPC--RPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLrGQVVGFISQE 452
Cdd:COG4618 339 VPPGskRP---ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL-GRHIGYLPQD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 453 PVLFGTTIMENI-RFGklEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILD 531
Cdd:COG4618 415 VELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLD 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 533869216 532 EATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKK 594
Cdd:COG4618 493 EPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
51-340 |
4.68e-68 |
|
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: 4.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 51 LGAALVNVQIPLLLGQLVEVVAKYTRDHVGSFMTESQnLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSL 130
Cdd:cd18573 6 LVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKT-FALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 131 LRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSG 210
Cdd:cd18573 85 LRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 211 LRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLF 290
Cdd:cd18573 165 VRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLY 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 533869216 291 IGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18573 245 YGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
365-582 |
7.91e-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: 217.84 E-value: 7.91e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 365 GSVTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQ 444
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 445 VVGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQ 524
Cdd:cd03245 79 NIGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 525 PTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRV 582
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
48-577 |
7.53e-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: 224.86 E-value: 7.53e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 48 QLALGAALVNVQIPLLLGQ---LVEVVAKYTRDhvGSFMTESQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRR 124
Cdd:TIGR02857 4 ALALLALLGVLGALLIIAQawlLARVVDGLISA--GEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 125 ALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVG 204
Cdd:TIGR02857 82 RLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 205 TLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRgIALfqgLSNIAFNcm 284
Cdd:TIGR02857 162 ILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLR-IAF---LSSAVLE-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 285 VLGTL-------FIGGSLVAGQQLTGGDLMSFLVASQTVQrSMANLSVLFGQVVRGLSAGARVFEYMALNPcIPLSGGCC 357
Cdd:TIGR02857 236 LFATLsvalvavYIGFRLLAGDLDLATGLFVLLLAPEFYL-PLRQLGAQYHARADGVAAAEALFAVLDAAP-RPLAGKAP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 358 VPKEQLRgSVTFQNVCFSYPCRPgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLD 437
Cdd:TIGR02857 314 VTAAPAS-SLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 438 PSWLRGQVvGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAI 517
Cdd:TIGR02857 391 ADSWRDQI-AWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLAL 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 518 ARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVM 577
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
86-594 |
2.15e-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: 221.45 E-value: 2.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 86 SQNLSTHLLI------LYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDAnKTGQLVSRLTTdVQEFKS 159
Cdd:TIGR01842 39 SGSVPTLLMLtvlalgLYLFLGLLDALRSFVLVRIGEKLDGALNQPIFAASFSATLRRGSG-DGLQALRDLDQ-LRQFLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 160 SfklvisQGLrsctqVAGC--------LVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADE 231
Cdd:TIGR01842 117 G------PGL-----FAFFdapwmpiyLLVCFLLHPWIGILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 232 ALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGdlmSFLV 311
Cdd:TIGR01842 186 ALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPG---MMIA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 312 ASQTVQRSMANLSVLFG---QVVRGLSAGARVFEYMALNPciplSGGCCVPKEQLRGSVTFQNVCFSYPcRPGFEVLKDF 388
Cdd:TIGR01842 263 GSILVGRALAPIDGAIGgwkQFSGARQAYKRLNELLANYP----SRDPAMPLPEPEGHLSVENVTIVPP-GGKKPTLRGI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 389 TLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLrGQVVGFISQEPVLFGTTIMENI-RFG 467
Cdd:TIGR01842 338 SFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETF-GKHIGYLPQDVELFPGTVAENIaRFG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 468 KlEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQE 547
Cdd:TIGR01842 417 E-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALAN 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 533869216 548 ALDRASA-GRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKK 594
Cdd:TIGR01842 496 AIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
365-587 |
3.13e-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: 210.81 E-value: 3.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 365 GSVTFQNVCFSYpcRPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG 443
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 444 QVvGFISQEPVLFGTTIMENIR-FGklEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALI 522
Cdd:cd03244 79 RI-SIIPQDPVLFSGTIRSNLDpFG--EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 523 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGT 587
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
89-602 |
5.44e-64 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 223.85 E-value: 5.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 89 LSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTtDVQEFKSSFKLVISQG 168
Cdd:TIGR01193 198 ISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 169 LRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAME--- 245
Cdd:TIGR01193 277 FLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEaer 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 246 -QREEERYGAELE-ACRCRAEELGRGiaLFQGLSNIAFNCMVLgtlFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANL 323
Cdd:TIGR01193 357 ySKIDSEFGDYLNkSFKYQKADQGQQ--AIKAVTKLILNVVIL---WTGAYLVMRGKLTLGQLITFNALLSYFLTPLENI 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 324 SVLFGQVVRGLSAGARVFEyMALNPCIPLSGGCCVPKEQLRGSVTFQNVCFSYpcrpGF--EVLKDFTLTLPPGKIVALV 401
Cdd:TIGR01193 432 INLQPKLQAARVANNRLNE-VYLVDSEFINKKKRTELNNLNGDIVINDVSYSY----GYgsNILSDISLTIKMNSKTTIV 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 402 GQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFG-KLEASDEEVYTAA 480
Cdd:TIGR01193 507 GMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR-QFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAAC 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 481 REANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAgRTVLV 560
Cdd:TIGR01193 586 EIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIF 664
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 533869216 561 IAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELI 602
Cdd:TIGR01193 665 VAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
110-565 |
3.42e-63 |
|
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: 218.00 E-value: 3.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 110 LLSH-VGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFklvisqgLRSCTQVAGCLVsLSMLSTR 188
Cdd:TIGR02868 75 LVGHdAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLY-------VRVIVPAGVALV-VGAAAVA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 189 LTLLLMVATPALMGVGTLMGSGL-----RKLSRQCQEQIARAMG----VADEALGNVRTVRAF-AMEQ--REEERYGAEL 256
Cdd:TIGR02868 147 AIAVLSVPAALILAAGLLLAGFVaplvsLRAARAAEQALARLRGelaaQLTDALDGAAELVASgALPAalAQVEEADREL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 257 EACRCRAeelGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSA 336
Cdd:TIGR02868 227 TRAERRA---AAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 337 GARVFEYMALNPCI-----PLSGGCCVPKEQLRgsvtFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTV 411
Cdd:TIGR02868 304 AERIVEVLDAAGPVaegsaPAAGAVGLGKPTLE----LRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 412 ASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITS 491
Cdd:TIGR02868 378 LATLAGLLDPLQGEVTLDGVPVSSLDQDEVR-RRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRA 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 533869216 492 FPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRL 565
Cdd:TIGR02868 457 LPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
51-340 |
1.79e-59 |
|
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: 200.85 E-value: 1.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 51 LGAALVNVQIPLLLGQLVEVVAkytrdHVGSFMTESQNLsTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSL 130
Cdd:cd18572 6 VVAALSELAIPHYTGAVIDAVV-----ADGSREAFYRAV-LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 131 LRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSG 210
Cdd:cd18572 80 LRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 211 LRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLF 290
Cdd:cd18572 160 YRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 533869216 291 IGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18572 240 YGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
49-340 |
5.11e-59 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 199.63 E-value: 5.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 49 LALGAALVNVQIPLLLGQLVEVVakytrdHVGSFMTESQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFS 128
Cdd:cd18576 4 LLLLSSAIGLVFPLLAGQLIDAA------LGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 129 SLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMG 208
Cdd:cd18576 78 HLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 209 SGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGT 288
Cdd:cd18576 158 RRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 533869216 289 LFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18576 238 LWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
389-605 |
4.57e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 205.46 E-value: 4.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 389 TLTLPPGKIVALVGQSGGGKTTVASLLERFYdPTAGVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFGK 468
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHL-SWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 469 LEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEA 548
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 549 LDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 605
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
249-605 |
3.04e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 200.05 E-value: 3.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 249 EERYGAELEACRCRAEELGRGIALFQGLSN---IAFNCM-VLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLS 324
Cdd:PRK11160 219 EDRYRQQLEQTEQQWLAAQRRQANLTGLSQalmILANGLtVVLMLWLAAGGVGGNAQPGALIALFVFAALAAFEALMPVA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 325 VLF---GQVVrglSAGARVFEYMALNPCIPLSGGCCVPKEQlrGSVTFQNVCFSYPCRPgFEVLKDFTLTLPPGKIVALV 401
Cdd:PRK11160 299 GAFqhlGQVI---ASARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQP-QPVLKGLSLQIKAGEKVALL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 402 GQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAR 481
Cdd:PRK11160 373 GRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR-QAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQ 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 482 EANAHEFITSfPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVI 561
Cdd:PRK11160 452 QVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMI 530
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 533869216 562 AHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELIRRQ 605
Cdd:PRK11160 531 THRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
44-340 |
6.94e-55 |
|
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: 188.84 E-value: 6.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 44 ILSCQLALGAALVNVQIPLLLGQLVEVVAKYTRDHVGS--FMTESQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVD 121
Cdd:cd18577 2 IIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPdeFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 122 MRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQ-VAGCLVSLSMlSTRLTLLLMVATPAL 200
Cdd:cd18577 82 IRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTfIAGFIIAFIY-SWKLTLVLLATLPLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 201 MGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEacrcRAEELGRGIALFQGLSNIA 280
Cdd:cd18577 161 AIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALE----KARKAGIKKGLVSGLGLGL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 281 FNCMVLGT----LFIGGSLVAGQQLTGGD----LMSFLVASQTVQRSMANLSVLfgqvVRGLSAGARV 340
Cdd:cd18577 237 LFFIIFAMyalaFWYGSRLVRDGEISPGDvltvFFAVLIGAFSLGQIAPNLQAF----AKARAAAAKI 300
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
54-340 |
5.34e-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: 186.30 E-value: 5.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 54 ALVNVQIPLLLGQLVEVVAKYTRDHVGSFMTESQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQ 133
Cdd:cd18780 9 SGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 134 DITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRK 213
Cdd:cd18780 89 EIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 214 LSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGG 293
Cdd:cd18780 169 LSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 533869216 294 SLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18780 249 RLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
94-579 |
1.10e-51 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 192.94 E-value: 1.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 94 LILYG-VQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTgqlvSRLTTDVQEFKSSFKLVISQGLRSC 172
Cdd:PTZ00265 103 LVLIGiFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQVNAGIGTKFITI 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 173 TQVAGCLVSLSMLS----TRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQR- 247
Cdd:PTZ00265 179 FTYASAFLGLYIWSlfknARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTi 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 248 ------EEERYGA-ELEACRCRAEELGrgiaLFQG--LSNIAFNcMVLGTLFIGGSLVAGQ---QLTGGDLMSFLVAsqt 315
Cdd:PTZ00265 259 lkkfnlSEKLYSKyILKANFMESLHIG----MINGfiLASYAFG-FWYGTRIIISDLSNQQpnnDFHGGSVISILLG--- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 316 VQRSMANLSVLFGQV---VRGLSAGARVFEYMALNPCIPLSGGccvpKEQLRG--SVTFQNVCFSYPCRPGFEVLKDFTL 390
Cdd:PTZ00265 331 VLISMFMLTIILPNIteyMKSLEATNSLYEIINRKPLVENNDD----GKKLKDikKIQFKNVRFHYDTRKDVEIYKDLNF 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 391 TLPPGKIVALVGQSGGGKTTVASLLERFYDPTAG-VVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFGTTIMENIRFG-- 467
Cdd:PTZ00265 407 TLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdIIINDSHNLKDINLKWWRSKI-GVVSQDPLLFSNSIKNNIKYSly 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 468 ---KLEA----------------------------------------------------SDEEVYTAAREANAHEFITSF 492
Cdd:PTZ00265 486 slkDLEAlsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtiKDSEVVDVSKKVLIHDFVSAL 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 493 PEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG 570
Cdd:PTZ00265 566 PDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRY 645
|
....*....
gi 533869216 571 AHCIVVMAD 579
Cdd:PTZ00265 646 ANTIFVLSN 654
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
114-603 |
1.76e-49 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 186.39 E-value: 1.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 114 VGERMAVDMRRALFSSLLRQDITFFD--ANKTGQLVSRLTTDVQEFKSS--------------FKLVISQGLRSCTQVAG 177
Cdd:PTZ00265 893 IGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGlvnnivifthfivlFLVSMVMSFYFCPIVAA 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 178 CLVSLSMLSTRLTLLL--MVATPALMGVGTLMGSGLRKLSRQcQEQIARAMGVADEALGNVRTVRAFAMEQreeerYGAE 255
Cdd:PTZ00265 973 VLTGTYFIFMRVFAIRarLTANKDVEKKEINQPGTVFAYNSD-DEIFKDPSFLIQEAFYNMNTVIIYGLED-----YFCN 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 256 L--EACRCRAEELGRGI---ALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLM----SFLVASQTVQRSMAnlsvl 326
Cdd:PTZ00265 1047 LieKAIDYSNKGQKRKTlvnSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMkslfTFLFTGSYAGKLMS----- 1121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 327 fgqvVRGLSAGARV-FE-YMAL-----NPCIPLSGGCCVP-KEQLRGSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIV 398
Cdd:PTZ00265 1122 ----LKGDSENAKLsFEkYYPLiirksNIDVRDNGGIRIKnKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTT 1197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 399 ALVGQSGGGKTTVASLLERFYD------------------------------------------------------PTAG 424
Cdd:PTZ00265 1198 AIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSG 1277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 425 VVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERG 504
Cdd:PTZ00265 1278 KILLDGVDICDYNLKDLR-NLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYG 1356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 505 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEAL--DRASAGRTVLVIAHRLSTVRGAHCIVVMAD--- 579
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIVVFNNpdr 1436
|
570 580
....*....|....*....|....*..
gi 533869216 580 --GRVWEAGTHEELLK-KGGLYAELIR 603
Cdd:PTZ00265 1437 tgSFVQAHGTHEELLSvQDGVYKKYVK 1463
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
44-320 |
2.41e-49 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 173.21 E-value: 2.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 44 ILSCQLALGAALVNVQIPLLLGQLVEVVAKYTRDHvgsfmTESQNL-STHLLILYGVQGLLTFGYLVLLSHVGERMAVDM 122
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPE-----TQALNVySLALLLLGLAQFILSFLQSYLLNHTGERLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 123 RRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRS-CTQVAGCLVSLSmLSTRLTLLLMVATPALM 201
Cdd:pfam00664 77 RRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSlATIVGGIIVMFY-YGWKLTLVLLAVLPLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 202 GVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAF 281
Cdd:pfam00664 156 LVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIG 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 533869216 282 NCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSM 320
Cdd:pfam00664 236 YLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
44-340 |
6.19e-49 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 172.35 E-value: 6.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 44 ILSCQLALGAALVNVQIPLLLGQLV-EVVAKYTRDHVGSFMTEsqnlsthLLILYGVQGLLTFGYLVLLSHVGERMAVDM 122
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIdDVIPAGDLSLLLWIALL-------LLLLALLRALLSYLRRYLAARLGQRVVFDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 123 RRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMG 202
Cdd:cd07346 75 RRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 203 VGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFN 282
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 283 CMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd07346 235 LGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
93-340 |
3.54e-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: 170.30 E-value: 3.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 172
Cdd:cd18552 45 IIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 173 TQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERY 252
Cdd:cd18552 125 LTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 253 GAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVR 332
Cdd:cd18552 205 RKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQR 284
|
....*...
gi 533869216 333 GLSAGARV 340
Cdd:cd18552 285 GLAAAERI 292
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
50-607 |
1.05e-47 |
|
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: 180.91 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 50 ALGAALVNVQIPLLLGQLVEVVAK------YTRDHVGSFMTESQNLSthlLILYG----VQGLLTFGYLVLLSHVGERMA 119
Cdd:TIGR00957 961 AIGLFITFLSIFLFVCNHVSALASnywlslWTDDPMVNGTQNNTSLR---LSVYGalgiLQGFAVFGYSMAVSIGGIQAS 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 120 VDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLsMLSTRLtllLMVATPA 199
Cdd:TIGR00957 1038 RVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVI-LLATPI---AAVIIPP 1113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 200 LMGVGTLMGSGLRKLSRQCQ--EQIARAMGVA--DEALGNVRTVRAFAMEQREEERYGAELEACR--------------C 261
Cdd:TIGR00957 1114 LGLLYFFVQRFYVASSRQLKrlESVSRSPVYShfNETLLGVSVIRAFEEQERFIHQSDLKVDENQkayypsivanrwlaV 1193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 262 RAEELGRGIALFQGL-SNIAFNCMVLGtlFIGGSLVAGQQLTGgdLMSFLVasqtvqRSMANLSVlfgqvvrGLSAGARV 340
Cdd:TIGR00957 1194 RLECVGNCIVLFAALfAVISRHSLSAG--LVGLSVSYSLQVTF--YLNWLV------RMSSEMET-------NIVAVERL 1256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 341 FEYMALNPCIPLSGGCCVPKEQL--RGSVTFQNVCFSYpcRPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLER 417
Cdd:TIGR00957 1257 KEYSETEKEAPWQIQETAPPSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFR 1334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 418 FYDPTAGVVMLDGRDLRTLDPSWLRGQVVgFISQEPVLFGTTIMENIR-FGKLeaSDEEVYTAAREANAHEFITSFPEGY 496
Cdd:TIGR00957 1335 INESAEGEIIIDGLNIAKIGLHDLRFKIT-IIPQDPVLFSGSLRMNLDpFSQY--SDEEVWWALELAHLKTFVSALPDKL 1411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 497 NTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVV 576
Cdd:TIGR00957 1412 DHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIV 1491
|
570 580 590
....*....|....*....|....*....|.
gi 533869216 577 MADGRVWEAGTHEELLKKGGLYAELIRRQAL 607
Cdd:TIGR00957 1492 LDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
367-594 |
8.89e-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: 164.43 E-value: 8.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 446
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELR-RKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPV--LFGTTIMENIRFGkLEA---SDEEVYTAAREA----NAHEFITSFPegyntvvgergTTLSGGQKQRLAI 517
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEDVAFG-PENlglPREEIRERVEEAlelvGLEHLADRPP-----------HELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 518 ARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLKK 594
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
370-582 |
4.17e-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: 158.15 E-value: 4.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYP--CRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvG 447
Cdd:cd03246 4 ENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHV-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 448 FISQEPVLFGTTIMENIrfgkleasdeevytaareanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQPTV 527
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 528 LILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLSTVRGAHCIVVMADGRV 582
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
368-563 |
7.24e-45 |
|
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: 7.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 368 TFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVg 447
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 448 FISQEPVLFGTTIMENIRFGKLEASDEEVYTAAREAnAHEFitSFPEGYntvVGERGTTLSGGQKQRLAIARALIKQPTV 527
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLRERKFDRERALEL-LERL--GLPPDI---LDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 533869216 528 LILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH 563
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
369-591 |
4.90e-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: 156.96 E-value: 4.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 369 FQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD-----PTAGVVMLDGRDLRTLD--PSWL 441
Cdd:cd03260 3 LRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDvdVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 442 RGQVvGFISQEPVLFGTTIMENIRFG-KL------EASDEEVYTAAREANAHEFitsfpegyntvVGER--GTTLSGGQK 512
Cdd:cd03260 80 RRRV-GMVFQKPNPFPGSIYDNVAYGlRLhgiklkEELDERVEEALRKAALWDE-----------VKDRlhALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 513 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEEL 591
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
49-340 |
1.08e-43 |
|
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: 157.98 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 49 LALGAALVNVQIPLLLGQLVEVVAKyTRDHVGSFMTesqnlsthLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFS 128
Cdd:cd18551 7 LSLLGTAASLAQPLLVKNLIDALSA-GGSSGGLLAL--------LVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 129 SLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMG 208
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 209 SGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGT 288
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 533869216 289 LFIGGSLVAGQQLTGGDLMSFLV-ASQTVQrSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18551 238 LGVGGARVASGALTVGTLVAFLLyLFQLIT-PLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
49-340 |
4.09e-43 |
|
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: 156.44 E-value: 4.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 49 LALGAALVNVQIPLLLGQLV-EVVAKYTRDHVGsfmtesqNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALF 127
Cdd:cd18542 7 ALLLATALNLLIPLLIRRIIdSVIGGGLRELLW-------LLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 128 SSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLM 207
Cdd:cd18542 80 DHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 208 GSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLG 287
Cdd:cd18542 160 FKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 533869216 288 TLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18542 240 VLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
367-592 |
4.41e-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: 161.99 E-value: 4.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPG--FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLR-- 442
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 443 GQVVGFISQEPV--LF-----GTTIMENIRFGKLeASDEEVYTAAREANAH-----EFITSFPegyntvvgergTTLSGG 510
Cdd:COG1123 341 RRRVQMVFQDPYssLNprmtvGDIIAEPLRLHGL-LSRAERRERVAELLERvglppDLADRYP-----------HELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 511 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGT 587
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
....*
gi 533869216 588 HEELL 592
Cdd:COG1123 489 TEEVF 493
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
365-587 |
8.89e-43 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 152.95 E-value: 8.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 365 GSVTFQNVCFSY-PCRPgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG 443
Cdd:cd03369 5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 444 QVvGFISQEPVLFGTTIMENI-RFGklEASDEEVYTAAReanahefitsfpegyntvVGERGTTLSGGQKQRLAIARALI 522
Cdd:cd03369 83 SL-TIIPQDPTLFSGTIRSNLdPFD--EYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 523 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGT 587
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
49-338 |
9.42e-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: 155.33 E-value: 9.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 49 LALGAALVnvqipLLLGQLVevvaKYTRDHvGSFMTESQNLSTHLLILYGVQGLLTFG-----YLVllSHVGERMAVDMR 123
Cdd:cd18575 5 LLIAAAAT-----LALGQGL----RLLIDQ-GFAAGNTALLNRAFLLLLAVALVLALAsalrfYLV--SWLGERVVADLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 124 RALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGV 203
Cdd:cd18575 73 KAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 204 GTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEAC------RCRAEELGRGIALFQGLS 277
Cdd:cd18575 153 IILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAfaaalrRIRARALLTALVIFLVFG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 533869216 278 NIAFncmvlgTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRglSAGA 338
Cdd:cd18575 233 AIVF------VLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQR--AAGA 285
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
367-606 |
1.15e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.68 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgqVV 446
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR--RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVLFGT-TIMENIRF-GKLEASDEEVytaaREANAHEFITSF--PEGYNTVVGergtTLSGGQKQRLAIARALI 522
Cdd:COG1131 76 GYVPQEPALYPDlTVRENLRFfARLYGLPRKE----ARERIDELLELFglTDAADRKVG----TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 523 KQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKKG--GLY 598
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARLleDVF 227
|
....*...
gi 533869216 599 AELIRRQA 606
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 ... |
369-581 |
3.22e-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: 151.47 E-value: 3.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 369 FQNVCFSYPcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPsWLRGQVVGF 448
Cdd:cd03225 2 LKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSL-KELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 449 ISQEP--VLFGTTIMENIRFG--KLEASDEEVYTAAREANAHEFITSFPEgyntvvgERGTTLSGGQKQRLAIARALIKQ 524
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALELVGLEGLRD-------RSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 525 PTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHCIVVMADGR 581
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
367-582 |
4.26e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 151.73 E-value: 4.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLERfydPTAGVVMLDGRDLRTLDP---S 439
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSErelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 440 WLRGQVVGFISQEPVLFGT-TIMENIRFGKLEASdeeVYTAAREANAHEFITSFpeGyntvVGERG----TTLSGGQKQR 514
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVALPLLLAG---VSRKERRERARELLERV--G----LGDRLdhrpSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 515 LAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRGAHCIVVMADGRV 582
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
385-535 |
9.19e-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: 148.18 E-value: 9.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQvVGFISQEPVLF-GTTIMEN 463
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE-IGYVFQDPQLFpRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 533869216 464 IRFGkleASDEEVYTAAREANAHEFITSFPEGY--NTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 535
Cdd:pfam00005 80 LRLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
367-582 |
1.32e-41 |
|
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: 149.95 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLERfydPTAGVVMLDGRDLRTLDPSWL- 441
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 442 --RGQVVGFISQEPVLFGT-TIMENIRFGKLEASDEevyTAAREANAHEFITSF--PEGYNTVVGErgttLSGGQKQRLA 516
Cdd:cd03255 78 afRRRHIGFVFQSFNLLPDlTALENVELPLLLAGVP---KKERRERAEELLERVglGDRLNHYPSE----LSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 517 IARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRGAHCIVVMADGRV 582
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
51-340 |
4.77e-41 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 150.92 E-value: 4.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 51 LGAALVNVQIPLLLGQLVEVVAKytrdhvgsfmTESQNLSTHLLIlygVQGLLTFGYLV-------LLSHVGERMAVDMR 123
Cdd:cd18784 6 LAAAVGEIFIPYYTGQVIDGIVI----------EKSQDKFSRAII---IMGLLAIASSVaagirggLFTLAMARLNIRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 124 RALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGV 203
Cdd:cd18784 73 NLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 204 GTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEacrcRAEELGRGIALFQG----LSNI 279
Cdd:cd18784 153 SKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLK----DTYKLKIKEALAYGgyvwSNEL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 533869216 280 AFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18784 229 TELALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
367-581 |
6.13e-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: 147.62 E-value: 6.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRP--GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL--ErfYDPTAGVVMLDGRdlrtldpswlr 442
Cdd:cd03250 1 ISVEDASFTWDSGEqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 443 gqvVGFISQEPVLFGTTIMENIRFGKLEasDEEVYTAAREANA-HEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARAL 521
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENILFGKPF--DEERYEKVIKACAlEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 522 IKQPTVLILDEATSALDAES-----ERVVQEALdraSAGRTVLVIAHRLSTVRGAHCIVVMADGR 581
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
367-623 |
1.34e-40 |
|
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: 155.06 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPgFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTA---GVVMLDGRDLRTLDPsWLRG 443
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSE-ALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 444 QVVGFISQEP--VLFGTTIMENIRFG--KLEASDEEVYTAAREANAHEFITSFPEGYNTvvgergtTLSGGQKQRLAIAR 519
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 520 ALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKKgg 596
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA-- 233
|
250 260
....*....|....*....|....*..
gi 533869216 597 lYAELIRRQALDAPRTAAPPPKKPEGP 623
Cdd:COG1123 234 -PQALAAVPRLGAARGRAAPAAAAAEP 259
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
375-586 |
8.62e-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: 145.34 E-value: 8.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 375 SYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWL--RGQVVGFISQ 451
Cdd:cd03257 10 SFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkiRRKEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 452 EPVL-------FGTTIMENIRFGKLEASDEEVYTAAREA-----NAHEFITSFPegyntvvgergTTLSGGQKQRLAIAR 519
Cdd:cd03257 90 DPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYP-----------HELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 520 ALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAG 586
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
367-610 |
2.47e-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: 145.27 E-value: 2.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGrdLRTLDPS--WLRG 443
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEEnlWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 444 QVVGFISQEP--VLFGTTIMENIRFGkLE----ASDE---EVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQR 514
Cdd:TIGR04520 77 KKVGMVFQNPdnQFVGATVEDDVAFG-LEnlgvPREEmrkRVDEALKLVGMEDFRDREPH-----------LLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 515 LAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELL 592
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRklNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIF 224
|
250
....*....|....*...
gi 533869216 593 KKGglyaELIRRQALDAP 610
Cdd:TIGR04520 225 SQV----ELLKEIGLDVP 238
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
367-604 |
1.70e-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: 142.49 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 446
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-RRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVL-FGTTIMENI---------RFGKLEASDEE-VYTAAREANAHEFItsfpegyntvvgERG-TTLSGGQKQR 514
Cdd:COG1120 78 AYVPQEPPApFGLTVRELValgryphlgLFGRPSAEDREaVEEALERTGLEHLA------------DRPvDELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 515 LAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEEL 591
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
250
....*....|...
gi 533869216 592 LKkgglyAELIRR 604
Cdd:COG1120 226 LT-----PELLEE 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
368-603 |
2.09e-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: 141.92 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 368 TFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRGQVvG 447
Cdd:COG4555 3 EVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQI-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 448 FISQEPVLF-GTTIMENIR-FGKLEASDEEVYTAAREANAHEFItsFPEGYNTVVGErgttLSGGQKQRLAIARALIKQP 525
Cdd:COG4555 78 VLPDERGLYdRLTVRENIRyFAELYGLFDEELKKRIEELIELLG--LEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 526 TVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVrGAHC--IVVMADGRVWEAGTHEELLKKGG---LYA 599
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEV-EALCdrVVILHKGKVVAQGSLDELREEIGeenLED 230
|
....
gi 533869216 600 ELIR 603
Cdd:COG4555 231 AFVA 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
367-594 |
3.01e-38 |
|
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: 141.18 E-value: 3.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVA---SLLERfydPTAGVVMLDGRDLRTLDPSWLR 442
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIrciNGLER---PTSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 443 G--QVVGFISQEPVLFGT-TIMENIRFgKLE---ASDEEVYTAARE----ANAHEFITSFPegyntvvgergTTLSGGQK 512
Cdd:cd03258 79 KarRRIGMIFQHFNLLSSrTVFENVAL-PLEiagVPKAEIEERVLEllelVGLEDKADAYP-----------AQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 513 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHE 589
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
....*
gi 533869216 590 ELLKK 594
Cdd:cd03258 227 EVFAN 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
50-596 |
3.11e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 152.05 E-value: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 50 ALGAALVnVQIpLLLGQLVEVVAKYTRDHVGSFMTE---SQNLSTHLLILygVQGLLTFG----------YLVLLS-HVG 115
Cdd:PLN03232 907 AVGGLWV-VMI-LLVCYLTTEVLRVSSSTWLSIWTDqstPKSYSPGFYIV--VYALLGFGqvavtftnsfWLISSSlHAA 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 116 ERMavdmRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTR-----LT 190
Cdd:PLN03232 983 KRL----HDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTIslwaiMP 1058
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 191 LLLMVATPALMGVGTlmGSGLRKLSRQCQEQIARAMGvadEALGNVRTVRAFAMEQREEERYGAELEacrcraeelgrgi 270
Cdd:PLN03232 1059 LLILFYAAYLYYQST--SREVRRLDSVTRSPIYAQFG---EALNGLSSIRAYKAYDRMAKINGKSMD------------- 1120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 271 alfqglSNIAFNcmvLGTLFIGGSLVAGQQLTGGdLMSFLVASQTVQRS-------------------MANLSVLFGQVV 331
Cdd:PLN03232 1121 ------NNIRFT---LANTSSNRWLTIRLETLGG-VMIWLTATFAVLRNgnaenqagfastmglllsyTLNITTLLSGVL 1190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 332 R-------GLSAGARVFEYMAL---NPCI-----PLSGGccvpkeQLRGSVTFQNVCFSYpcRPGFE-VLKDFTLTLPPG 395
Cdd:PLN03232 1191 RqaskaenSLNSVERVGNYIDLpseATAIiennrPVSGW------PSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPS 1262
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 396 KIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIR-FGklEASDE 474
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLR-RVLSIIPQSPVLFSGTVRFNIDpFS--EHNDA 1339
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 475 EVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA 554
Cdd:PLN03232 1340 DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFK 1419
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 533869216 555 GRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGG 596
Cdd:PLN03232 1420 SCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
51-350 |
3.41e-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: 3.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 51 LGAALVNVQIPL---LLGQLVEVVAKYTRDHVgsfMTESQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALF 127
Cdd:cd18578 16 IGAIIAGAVFPVfaiLFSKLISVFSLPDDDEL---RSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 128 SSLLRQDITFFD--ANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVsLSM-LSTRLTLLLMVATPALMGVG 204
Cdd:cd18578 93 RAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLI-IAFvYGWKLALVGLATVPLLLLAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 205 TLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSN-IAFNC 283
Cdd:cd18578 172 YLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQsLTFFA 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 533869216 284 MVLGtLFIGGSLVAGQQLTGGD----LMSFLVASQTVQRSMAnlsvLFGQVVRGLSAGARVFEYMALNPCI 350
Cdd:cd18578 252 YALA-FWYGGRLVANGEYTFEQffivFMALIFGAQSAGQAFS----FAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
367-586 |
4.84e-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: 138.99 E-value: 4.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlRGQVV 446
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA--LSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVLFGTTIMENIrfgkleasdeevytaareanahefitsfpegyntvvgerGTTLSGGQKQRLAIARALIKQPT 526
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 527 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAG 586
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
367-582 |
5.60e-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: 137.22 E-value: 5.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYP-CRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlrgqv 445
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 VGFISQEPVLFG-TTIMENIRFGkLEASDeeVYTAAREANAHEFITsfpegyntVVGERGT------TLSGGQKQRLAIA 518
Cdd:cd03293 75 RGYVFQQDALLPwLTVLDNVALG-LELQG--VPKAEARERAEELLE--------LVGLSGFenayphQLSGGMRQRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 519 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHCIVVMA--DGRV 582
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSarPGRI 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
370-582 |
5.80e-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: 135.60 E-value: 5.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRGQVvGFI 449
Cdd:cd03230 4 RNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRI-GYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 450 SQEPVLFGT-TIMENIRfgkleasdeevytaareanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQPTVL 528
Cdd:cd03230 79 PEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 529 ILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRV 582
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
367-592 |
7.68e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 140.60 E-value: 7.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVA---SLLERfydPTAGVVMLDGRDLRTLDPSWLR 442
Cdd:COG1135 2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 443 G--QVVGFISQEPVLFGT-TIMENIRFGkLEASDeeVYTAAREANAHEFITsfpegyntVVG--ERGTT----LSGGQKQ 513
Cdd:COG1135 79 AarRKIGMIFQHFNLLSSrTVAENVALP-LEIAG--VPKAEIRKRVAELLE--------LVGlsDKADAypsqLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 514 RLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEE 590
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLD 227
|
..
gi 533869216 591 LL 592
Cdd:COG1135 228 VF 229
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
50-603 |
8.36e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 147.96 E-value: 8.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 50 ALGAALVnVQIPLLLGQLVEVVaKYTRDHVGSFMTESQNLSTHLLILY-GVQGLLTFG---------YLVLLSHVgeRMA 119
Cdd:PLN03130 910 ALGGAWV-VMILFLCYVLTEVF-RVSSSTWLSEWTDQGTPKTHGPLFYnLIYALLSFGqvlvtllnsYWLIMSSL--YAA 985
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 120 VDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPA 199
Cdd:PLN03130 986 KRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVL 1065
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 200 LMGVGTLMGSGLRKLSRQcqEQIARAMGVAD--EALGNVRTVRAFAMEQREEERYGAELEacrcraeelgrgialfqglS 277
Cdd:PLN03130 1066 FYGAYLYYQSTAREVKRL--DSITRSPVYAQfgEALNGLSTIRAYKAYDRMAEINGRSMD-------------------N 1124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 278 NIAFNCMVLGtlfiGGSLVAGQQLTGGDLMSFLVASQTV--------QRSMA-----------NLSVLFGQVVR------ 332
Cdd:PLN03130 1125 NIRFTLVNMS----SNRWLAIRLETLGGLMIWLTASFAVmqngraenQAAFAstmglllsyalNITSLLTAVLRlaslae 1200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 333 -GLSAGARVFEYMALNPCIPL--SGGCCVPKEQLRGSVTFQNVCFSYpcRPGFE-VLKDFTLTLPPGKIVALVGQSGGGK 408
Cdd:PLN03130 1201 nSLNAVERVGTYIDLPSEAPLviENNRPPPGWPSSGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGK 1278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 409 TTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIR-FGklEASDEEVYTAAREANAHE 487
Cdd:PLN03130 1279 SSMLNALFRIVELERGRILIDGCDISKFGLMDLR-KVLGIIPQAPVLFSGTVRFNLDpFN--EHNDADLWESLERAHLKD 1355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 488 FITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLST 567
Cdd:PLN03130 1356 VIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNT 1435
|
570 580 590
....*....|....*....|....*....|....*..
gi 533869216 568 VRGAHCIVVMADGRVWEAGTHEELL-KKGGLYAELIR 603
Cdd:PLN03130 1436 IIDCDRILVLDAGRVVEFDTPENLLsNEGSAFSKMVQ 1472
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
367-582 |
8.99e-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: 137.91 E-value: 8.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlrgqv 445
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 VGFISQEPVLFG-TTIMENIRFGkLEASDeeVYTAAREANAHEFI---------TSFPegyntvvgergTTLSGGQKQRL 515
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALG-LELRG--VPKAERRERARELLelvglagfeDAYP-----------HQLSGGMRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 516 AIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH------RLSTvRgahcIVVMAD--GRV 582
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFLAD-R----VVVLSArpGRI 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
370-593 |
9.32e-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: 137.63 E-value: 9.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYP-CRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGF 448
Cdd:COG1124 5 RNLSVSYGqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV-QM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 449 ISQEPVL-------FGTTIMENIRFGKLEASDEEVYTAAREAN-AHEFITSFPEgyntvvgergtTLSGGQKQRLAIARA 520
Cdd:COG1124 84 VFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 521 LIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTVrgAH-C--IVVMADGRVWEAGTHEEL 591
Cdd:COG1124 153 LILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVV--AHlCdrVAVMQNGRIVEELTVADL 226
|
..
gi 533869216 592 LK 593
Cdd:COG1124 227 LA 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
367-586 |
1.32e-36 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 136.11 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPsWLRGqvV 446
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP-ERRN--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVLFGT-TIMENIRFG------KLEASDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIAR 519
Cdd:cd03259 75 GMVFQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 520 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAG 586
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
368-581 |
4.55e-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: 132.75 E-value: 4.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 368 TFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvG 447
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 448 FISQepvlfgttimenirfgkleasdeevytaareanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQPTV 527
Cdd:cd00267 77 YVPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 528 LILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTV-RGAHCIVVMADGR 581
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
363-603 |
7.14e-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: 135.42 E-value: 7.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 363 LRGSVTFQNVCFSYP--CRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSW 440
Cdd:cd03288 16 LGGEIKIHDLCVRYEnnLKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 441 LRGQVvGFISQEPVLFGTTIMENIRfGKLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARA 520
Cdd:cd03288 93 LRSRL-SIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 521 LIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELL-KKGGLYA 599
Cdd:cd03288 171 FVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFA 250
|
....
gi 533869216 600 ELIR 603
Cdd:cd03288 251 SLVR 254
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
370-593 |
5.37e-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: 134.80 E-value: 5.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDP---TAGVVMLDGRDLRTLDPS---WLR 442
Cdd:COG0444 5 RNLKVYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKelrKIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 443 GQVVGFISQEP---------VlfGTTIMENIRFGKLeASDEEVYTAAREA-------NAHEFITSFP-Egyntvvgergt 505
Cdd:COG0444 85 GREIQMIFQDPmtslnpvmtV--GDQIAEPLRIHGG-LSKAEARERAIELlervglpDPERRLDRYPhE----------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 506 tLSGGQKQRLAIARALIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTVRG-AHCIVVMA 578
Cdd:COG0444 151 -LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVAEiADRVAVMY 225
|
250
....*....|....*
gi 533869216 579 DGRVWEAGTHEELLK 593
Cdd:COG0444 226 AGRIVEEGPVEELFE 240
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
370-610 |
6.85e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.22 E-value: 6.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYP--CRPGfevLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrTLDPSW-LRGQVv 446
Cdd:PRK13635 9 EHISFRYPdaATYA---LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-SEETVWdVRRQV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEP--VLFGTTIMENIRFGkLEASD-------EEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAI 517
Cdd:PRK13635 84 GMVFQNPdnQFVGATVQDDVAFG-LENIGvpreemvERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 518 ARALIKQPTVLILDEATSALDAESErvvQEALD-----RASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELL 592
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
250
....*....|....*...
gi 533869216 593 KKGglyaELIRRQALDAP 610
Cdd:PRK13635 229 KSG----HMLQEIGLDVP 242
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
367-581 |
2.48e-34 |
|
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: 128.46 E-value: 2.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWL-RGQV 445
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPpLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 VGFISQEPVLF-GTTIMENIRFGkleasdeevytaareanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQ 524
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 525 PTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHCIVVMADGR 581
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
366-591 |
4.75e-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: 132.91 E-value: 4.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGqv 445
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-PPEKRN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 VGFISQEPVLFG-TTIMENIRFGkLEASDeeVYTAAREANAHEF-----ITSFpegyntvvGERG-TTLSGGQKQRLAIA 518
Cdd:COG3842 79 VGMVFQDYALFPhLTVAENVAFG-LRMRG--VPKAEIRARVAELlelvgLEGL--------ADRYpHQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 519 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH------RLSTVrgahcIVVMADGRVWEAGTHEE 590
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHdqeealALADR-----IAVMNDGRIEQVGTPEE 222
|
.
gi 533869216 591 L 591
Cdd:COG3842 223 I 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
371-563 |
5.63e-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: 128.53 E-value: 5.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 371 NVCFSYpcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrtldPSWLRGQVVGFIS 450
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 451 QEP--VLFGTTIMENIRFGKLEASD--EEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPT 526
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAgnEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 533869216 527 VLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAH 563
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITH 184
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
93-602 |
6.32e-34 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 138.96 E-value: 6.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVqgllTFGYLV---LLSHVGeRMAVDMRRALFSSLLRQDITF-FDANK---TGQLVSRLTTDVQEFKSsfklvI 165
Cdd:PLN03232 345 FLIFFGV----TFGVLCesqYFQNVG-RVGFRLRSTLVAAIFHKSLRLtHEARKnfaSGKVTNMITTDANALQQ-----I 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 166 SQGLRSCTQVAGCL-VSLSMLSTRL-------TLLLMVATPalmgVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVR 237
Cdd:PLN03232 415 AEQLHGLWSAPFRIiVSMVLLYQQLgvaslfgSLILFLLIP----LQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMD 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 238 TVRAFAMEQREEERYGAeleacrCRAEELgrgiALF---QGLSniAFNCMVLGTLFIGGSLVAGQQ--LTGGDL-----M 307
Cdd:PLN03232 491 TVKCYAWEKSFESRIQG------IRNEEL----SWFrkaQLLS--AFNSFILNSIPVVVTLVSFGVfvLLGGDLtparaF 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 308 SFLVASQTVQRSMANLSVLFGQVVRGLSAGARVFEY-------MALNPciPLSGGccVPkeqlrgSVTFQNVCFSYPCRP 380
Cdd:PLN03232 559 TSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELllseeriLAQNP--PLQPG--AP------AISIKNGYFSWDSKT 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVAS--LLERFYDPTAGVVmldgrdlrtldpswLRGQVvGFISQEPVLFGT 458
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISamLGELSHAETSSVV--------------IRGSV-AYVPQVSWIFNA 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 TIMENIRFGklEASDEEVYTAAREANA--HEfITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 536
Cdd:PLN03232 694 TVRENILFG--SDFESERYWRAIDVTAlqHD-LDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 537 LDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELI 602
Cdd:PLN03232 771 LDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
44-340 |
9.62e-34 |
|
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: 130.60 E-value: 9.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 44 ILSCQLALGAALVNVQIPLLLGQLVEVVAKYTRDHVGSFMTESQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMR 123
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 124 RALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGV 203
Cdd:cd18547 82 KDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 204 GTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGA---ELEACRCRAEELGrGIA--LFQGLSN 278
Cdd:cd18547 162 TKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEineELYKASFKAQFYS-GLLmpIMNFINN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 279 IAFncmvLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18547 241 LGY----VLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
367-590 |
2.20e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 127.48 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRg 443
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 444 QVVGFISQE-PVLFGTTIMENIRFGkLEA---SDEEVYTAAREA----NAHEFITSFPEgyntvvgergtTLSGGQKQRL 515
Cdd:COG2884 79 RRIGVVFQDfRLLPDRTVYENVALP-LRVtgkSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 516 AIARALIKQPTVLILDEATSALDAE-SERVVqEALDRASA-GRTVLVIAHRLSTVRGAHC-IVVMADGRVWEAGTHEE 590
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRrGTTVLIATHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
367-582 |
5.24e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 127.10 E-value: 5.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--Q 444
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 445 VVGFISQEPVLFG-TTIMENIRFGKLEA-----------SDEEVytaareANAHEFITSfpegyntvVG------ERGTT 506
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVLAGRLGRtstwrsllglfPPEDR------ERALEALER--------VGladkayQRADQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 507 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRgAHC--IVVMADGRV 582
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLAR-RYAdrIIGLRDGRV 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
367-593 |
1.07e-32 |
|
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: 125.86 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRG 443
Cdd:COG1127 6 IEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 444 QVvGFISQEPVLFGT-TIMENIRF-----GKLeaSDEEVYTAAREA----NAHEFITSFPegyntvvGErgttLSGGQKQ 513
Cdd:COG1127 83 RI-GMLFQGGALFDSlTVFENVAFplrehTDL--SEAEIRELVLEKlelvGLPGAADKMP-------SE----LSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 514 RLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEE 590
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRelRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
...
gi 533869216 591 LLK 593
Cdd:COG1127 229 LLA 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
370-586 |
1.78e-32 |
|
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: 123.31 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFI 449
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA-RKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 450 SQepvlfgttIMENIRFGKLeasdeevytaareanAHEFITsfpegyntvvgergtTLSGGQKQRLAIARALIKQPTVLI 529
Cdd:cd03214 79 PQ--------ALELLGLAHL---------------ADRPFN---------------ELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 530 LDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAG 586
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
367-592 |
1.85e-32 |
|
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: 125.49 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 446
Cdd:cd03295 1 IEFENVTKRYG--GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR-RKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVLF-GTTIMENIRF-GKLEASDEEvytaAREANAHEFITSF---PEGYntvvGER-GTTLSGGQKQRLAIARA 520
Cdd:cd03295 78 GYVIQQIGLFpHMTVEENIALvPKLLKWPKE----KIRERADELLALVgldPAEF----ADRyPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 521 LIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRL-STVRGAHCIVVMADGRVWEAGTHEELL 592
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRlqQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
367-592 |
2.72e-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: 124.72 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTV---ASLLERfydPTAGVVMLDGRDL--RTLDPSWL 441
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLtdSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 442 RGQVvGFISQEPVLFG-TTIMENIrfgkLEA-------SDEEVYTAAREANAH----EFITSFPEgyntvvgergtTLSG 509
Cdd:COG1126 76 RRKV-GMVFQQFNLFPhLTVLENV----TLApikvkkmSKAEAEERAMELLERvglaDKADAYPA-----------QLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 510 GQKQRLAIARALIKQPTVLILDEATSALDAEserVVQEALD--R--ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWE 584
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVE 216
|
....*...
gi 533869216 585 AGTHEELL 592
Cdd:COG1126 217 EGPPEEFF 224
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
117-340 |
3.80e-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: 125.91 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 117 RMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVA 196
Cdd:cd18590 66 RLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 197 TPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGL 276
Cdd:cd18590 146 MPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLV 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 533869216 277 SNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18590 226 RRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
368-591 |
7.12e-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: 123.83 E-value: 7.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 368 TFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQV-- 445
Cdd:cd03256 2 EVENLSKTYP--NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 VGFISQEPVLFG-TTIMENIRFGKLeasdeevytaareaNAHEFITS----FPE-------------GYNTVVGERGTTL 507
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRL--------------GRRSTWRSlfglFPKeekqralaalervGLLDKAYQRADQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 508 SGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRgAHC--IVVMADGRVW 583
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAR-EYAdrIVGLKDGRIV 224
|
....*...
gi 533869216 584 EAGTHEEL 591
Cdd:cd03256 225 FDGPPAEL 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
369-610 |
9.99e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 124.33 E-value: 9.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 369 FQNVCFSYPcrPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvG 447
Cdd:PRK13632 10 VENVSFSYP--NSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKI-G 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 448 FISQEP--VLFGTTIMENIRFGkLEAS-------DEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIA 518
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFG-LENKkvppkkmKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 519 RALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKgg 596
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN-- 232
|
250
....*....|....
gi 533869216 597 lyAELIRRQALDAP 610
Cdd:PRK13632 233 --KEILEKAKIDSP 244
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
381-593 |
1.25e-31 |
|
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: 122.93 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS--WLRGQVVGFisQEPVLFGT 458
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHeiARLGIGRTF--QIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 -TIMENIR--------FGKLEASDEEVYTAAREAnAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLI 529
Cdd:cd03219 90 lTVLENVMvaaqartgSGLLLARARREEREARER-AEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 530 LDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLK 593
Cdd:cd03219 167 LDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
367-591 |
1.68e-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: 121.84 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPgFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVV 446
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAAR-QSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVLFGT-TIMENIRF-GKLEASDEEvyTAAREANAHEFITSFPEGYNTVVGergtTLSGGQKQRLAIARALIKQ 524
Cdd:cd03263 78 GYCPQFDALFDElTVREHLRFyARLKGLPKS--EIKEEVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 533869216 525 PTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAH------RLSTvRgahcIVVMADGRVWEAGTHEEL 591
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdeaeALCD-R----IAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
367-593 |
7.40e-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: 120.68 E-value: 7.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--Q 444
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 445 VVGFISQEPVLFGT-TIMENIRFG---KLEASDEEVYTAARE----ANAHEFITSFPegyntvvGErgttLSGGQKQRLA 516
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLEkleaVGLRGAEDLYP-------AE----LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 517 IARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLK 593
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
44-340 |
1.25e-30 |
|
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: 121.44 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 44 ILSCQLALGAALVNVQIPLLLGQLV-EVVAKYTRDHVGSFMTEsqnlsthLLILYGVQGLLTFGYLVLLSHVGERMAVDM 122
Cdd:cd18543 2 ILALLAALLATLAGLAIPLLTRRAIdGPIAHGDRSALWPLVLL-------LLALGVAEAVLSFLRRYLAGRLSLGVEHDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 123 RRALFSSLLRQDITFFDANKTGQLVSRLTTD---VQEFKSSFKLVISQGLrsctQVAGCLVSLSMLSTRLTLLLMVATPA 199
Cdd:cd18543 75 RTDLFAHLQRLDGAFHDRWQSGQLLSRATSDlslVQRFLAFGPFLLGNLL----TLVVGLVVMLVLSPPLALVALASLPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 200 LMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEER--------YGAELEACRCRAeelgRGIA 271
Cdd:cd18543 151 LVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRfeaaarrlRATRLRAARLRA----RFWP 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 272 LFQGLSNIAfncmVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18543 227 LLEALPELG----LAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
367-592 |
1.76e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.81 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRtldpswLRGQVV 446
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR------RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVL---FGTTIMENIR---------FGKLEASDEEvytAAREA----NAHEFItsfpegyNTVVGErgttLSGG 510
Cdd:COG1121 78 GYVPQRAEVdwdFPITVRDVVLmgrygrrglFRRPSRADRE---AVDEAlervGLEDLA-------DRPIGE----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 511 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRgAHC--IVVMADGRVwEAGT 587
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVR-EYFdrVLLLNRGLV-AHGP 221
|
....*
gi 533869216 588 HEELL 592
Cdd:COG1121 222 PEEVL 226
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
49-311 |
2.37e-30 |
|
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: 120.98 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 49 LALGAALVNVQIPLLLGQLVevvakytrDHVgsfmtESQNLSTHLLILYG--------VQGLLTFGYLVLLSHVGERMAV 120
Cdd:cd18541 7 FLILVDLLQLLIPRIIGRAI--------DAL-----TAGTLTASQLLRYAllilllalLIGIFRFLWRYLIFGASRRIEY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 121 DMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPAL 200
Cdd:cd18541 74 DLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 201 MGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIA 280
Cdd:cd18541 154 ALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLL 233
|
250 260 270
....*....|....*....|....*....|.
gi 533869216 281 FNCMVLGTLFIGGSLVAGQQLTGGDLMSFLV 311
Cdd:cd18541 234 IGLSFLIVLWYGGRLVIRGTITLGDLVAFNS 264
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
366-593 |
2.91e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 122.18 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASL---LERfydPTAGVVMLDGRDLRTLDPSWLR 442
Cdd:COG1118 2 SIEVRNISKRFG---SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 443 GqvVGFISQEPVLFG-TTIMENIRFG--KLEASDEEvytaaREANAHEFITSFP-EGYntvvGER-GTTLSGGQKQRLAI 517
Cdd:COG1118 76 R--VGFVFQHYALFPhMTVAENIAFGlrVRPPSKAE-----IRARVEELLELVQlEGL----ADRyPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 518 ARALIKQPTVLILDEATSALDA----ESERVVQEALDRaSAGRTVLV---------IAHRlstvrgahcIVVMADGRVWE 584
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDE-LGGTTVFVthdqeealeLADR---------VVVMNQGRIEQ 214
|
....*....
gi 533869216 585 AGTHEELLK 593
Cdd:COG1118 215 VGTPDEVYD 223
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
90-591 |
3.09e-30 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 127.59 E-value: 3.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 90 STHLLILYGVQGLLTFGY---LVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVIS 166
Cdd:PTZ00243 998 ATYLYVYLGIVLLGTFSVplrFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYL 1077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 167 QgLRSCTqvAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMG---SGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFA 243
Cdd:PTZ00243 1078 Y-LLQCL--FSICSSILVTSASQPFVLVALVPCGYLYYRLMQfynSANREIRRIKSVAKSPVFTLLEEALQGSATITAYG 1154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 244 MEQ---REEERYGAELEACRCRAEELGRGIAL-FQGLSNIAFNCMVLgTLFIGGSLVAGQQLTGGDLMSFLVASQT---- 315
Cdd:PTZ00243 1155 KAHlvmQEALRRLDVVYSCSYLENVANRWLGVrVEFLSNIVVTVIAL-IGVIGTMLRATSQEIGLVSLSLTMAMQTtatl 1233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 316 ----------------VQR-----------SMANLSVLFGQVVRGLSAGARVFEYMALNPCIPLSGGccvPKEQLRGSVT 368
Cdd:PTZ00243 1234 nwlvrqvatveadmnsVERllyytdevpheDMPELDEEVDALERRTGMAADVTGTVVIEPASPTSAA---PHPVQAGSLV 1310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 369 FQNVCFSYpcRPGFE-VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvG 447
Cdd:PTZ00243 1311 FEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF-S 1387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 448 FISQEPVLFGTTIMENIR-FgkLEASDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPT 526
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNVDpF--LEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGS 1465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 527 VLIL-DEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEEL 591
Cdd:PTZ00243 1466 GFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
370-592 |
6.11e-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: 124.41 E-value: 6.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYPCRPG--------FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFyDPTAGVVMLDGRDLRTLDPSWL 441
Cdd:COG4172 279 RDLKVWFPIKRGlfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 442 RG-----QVVgFisQEPvlFGT---------TIMENIRFGKLEASDEEVYTAAREANA-------------HEFitsfpe 494
Cdd:COG4172 358 RPlrrrmQVV-F--QDP--FGSlsprmtvgqIIAEGLRVHGPGLSAAERRARVAEALEevgldpaarhrypHEF------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 495 gyntvvgergttlSGGQKQRLAIARALIKQPTVLILDEATSALDaeseRVVQ-EALD-----RASAGRTVLVIAHRLSTV 568
Cdd:COG4172 427 -------------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVV 489
|
250 260
....*....|....*....|....*
gi 533869216 569 RG-AHCIVVMADGRVWEAGTHEELL 592
Cdd:COG4172 490 RAlAHRVMVMKDGKVVEQGPTEQVF 514
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
384-594 |
8.34e-30 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 117.82 E-value: 8.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqvVGFISQEPVLF-GTTIME 462
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-KRD--ISYVPQNYALFpHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 463 NIRFG-------KLEAsDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIARALIKQPTVLILDEATS 535
Cdd:cd03299 91 NIAYGlkkrkvdKKEI-ERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 536 ALDAESERVVQEALDRA--SAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLKK 594
Cdd:cd03299 159 ALDVRTKEKLREELKKIrkEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
381-582 |
1.05e-29 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 116.48 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSW--LRgQVVGFISQEPVLFG- 457
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLR-QKVGMVFQQFNLFPh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 458 TTIMENIRFGKLEA---SDEEVYTAAREANAH----EFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPTVLIL 530
Cdd:cd03262 91 LTVLENITLAPIKVkgmSKAEAEERALELLEKvglaDKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 531 DEATSALDAEserVVQEALD----RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 582
Cdd:cd03262 160 DEPTSALDPE---LVGEVLDvmkdLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
370-591 |
1.07e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.83 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGV-----VMLDGRDL--RTLDPSWLR 442
Cdd:COG1117 15 RNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 443 GQVvGFISQEPVLFGTTIMENIRFG--------KLEAsDEEVYTAAREANAhefitsfpegYNTV---VGERGTTLSGGQ 511
Cdd:COG1117 92 RRV-GMVFQKPNPFPKSIYDNVAYGlrlhgiksKSEL-DEIVEESLRKAAL----------WDEVkdrLKKSALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 512 KQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEE 590
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEFGPTEQ 239
|
.
gi 533869216 591 L 591
Cdd:COG1117 240 I 240
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
368-592 |
1.08e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 117.16 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 368 TFQNVCFSYPcrpgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqvVG 447
Cdd:COG3840 3 RLDDLTYRYG-----DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERP--VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 448 FISQEPVLFG-TTIMENIRFG-----KLEASD-EEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIARA 520
Cdd:COG3840 75 MLFQENNLFPhLTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 521 LIKQPTVLILDEATSALD----AESERVVQEAldRASAGRTVLVIAHRLSTVR--GAHCIVVmADGRVWEAGTHEELL 592
Cdd:COG3840 144 LVRKRPILLLDEPFSALDpalrQEMLDLVDEL--CRERGLTVLMVTHDPEDAAriADRVLLV-ADGRIAADGPTAALL 218
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
93-340 |
1.67e-29 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 118.77 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 172
Cdd:cd18564 60 LVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 173 TQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERY 252
Cdd:cd18564 140 LTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 253 GAE----LEAcRCRAEELGrgiALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFG 328
Cdd:cd18564 220 AREnrksLRA-GLRAARLQ---ALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTG 295
|
250
....*....|..
gi 533869216 329 QVVRGLSAGARV 340
Cdd:cd18564 296 RIAKASASAERV 307
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
385-592 |
2.05e-29 |
|
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: 117.36 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWL---RGQVVGFISQEPVLF-GTTI 460
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelRRKKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 461 MENIRFGkLE---ASDEEVYTAAREA----NAHEFITSFPegyntvvGErgttLSGGQKQRLAIARALIKQPTVLILDEA 533
Cdd:cd03294 120 LENVAFG-LEvqgVPRAEREERAAEAlelvGLEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 534 TSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEELL 592
Cdd:cd03294 188 FSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
44-340 |
7.14e-29 |
|
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: 116.73 E-value: 7.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 44 ILSCQLALGAALVNVQIPLLLGQLV-EVVAKYTRDHV---GSFMtesqnlsthlLILYGVQGLLTFGYLVLLSHVGERMA 119
Cdd:cd18548 2 ILAPLFKLLEVLLELLLPTLMADIIdEGIANGDLSYIlrtGLLM----------LLLALLGLIAGILAGYFAAKASQGFG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 120 VDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPA 199
Cdd:cd18548 72 RDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 200 LMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNI 279
Cdd:cd18548 152 LALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMML 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 280 AFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL-VASQTVQrSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18548 232 IMNLAIVAILWFGGHLINAGSLQVGDLVAFInYLMQILM-SLMMLSMVFVMLPRASASAKRI 292
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
367-582 |
1.13e-28 |
|
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: 112.14 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlrgqvv 446
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 gfisqepvlfgttimenirfgkleasdeevytaaREANAHefitsfpeGYNTVvgergTTLSGGQKQRLAIARALIKQPT 526
Cdd:cd03216 70 ----------------------------------RDARRA--------GIAMV-----YQLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 527 VLILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 582
Cdd:cd03216 103 LLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
367-591 |
1.46e-28 |
|
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: 113.87 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqvV 446
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-KRP--V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVLF-GTTIMENIRFG----KLEASD--EEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIAR 519
Cdd:cd03300 75 NTVFQNYALFpHLTVFENIAFGlrlkKLPKAEikERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 520 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS---TVrgAHCIVVMADGRVWEAGTHEEL 591
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEI 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
376-591 |
1.89e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 116.37 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 376 YPCRPGF-----EVLK---DFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG---- 443
Cdd:COG4608 17 FPVRGGLfgrtvGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 444 -QVVgFisQEP---------VlfGTTIMENIRFGKLeASDEEVYTAAREA-------------NAHEFitsfpegyntvv 500
Cdd:COG4608 97 mQMV-F--QDPyaslnprmtV--GDIIAEPLRIHGL-ASKAERRERVAELlelvglrpehadrYPHEF------------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 501 gergttlSGGQKQRLAIARALIKQPTVLILDEATSALD----AEserVV------QEALdrasaGRTVLVIAHRLSTVRG 570
Cdd:COG4608 159 -------SGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQ---VLnlledlQDEL-----GLTYLFISHDLSVVRH 223
|
250 260
....*....|....*....|..
gi 533869216 571 -AHCIVVMADGRVWEAGTHEEL 591
Cdd:COG4608 224 iSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
49-340 |
2.90e-28 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 114.91 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 49 LALGAALVNVQIPLLLGQLVevvakytrDHVgsFMTESQNLSTHLLILY-----GVQGLLTF-----GYLvlLSHVGERM 118
Cdd:cd18563 7 LMLLGTALGLVPPYLTKILI--------DDV--LIQLGPGGNTSLLLLLvlglaGAYVLSALlgilrGRL--LARLGERI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 119 AVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATP 198
Cdd:cd18563 75 TADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 199 ALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSN 278
Cdd:cd18563 155 LVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLT 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 279 IafnCMVLGTLFI---GGSLVAGQQLTGGDLMSFLV-ASQTVQRsMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18563 235 F---LTSLGTLIVwyfGGRQVLSGTMTLGTLVAFLSyLGMFYGP-LQWLSRLNNWITRALTSAERI 296
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
381-592 |
3.36e-28 |
|
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: 112.53 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGQV-VGFISQEPVLFGT- 458
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGL-PPHERARAgIGYVPEGRRIFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 TIMENIRFG-------KLEASDEEVYTAareanahefitsFPegyntVVGER----GTTLSGGQKQRLAIARALIKQPTV 527
Cdd:cd03224 91 TVEENLLLGayarrraKRKARLERVYEL------------FP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 528 LILDEATSALdaeSERVVQEALDR----ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELL 592
Cdd:cd03224 154 LLLDEPSEGL---APKIVEEIFEAirelRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
369-582 |
5.23e-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: 111.86 E-value: 5.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 369 FQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTldpSWLRgqvVGF 448
Cdd:cd03235 2 VEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKR---IGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 449 ISQEPVL---FGTTIMENIR---------FGKLEASDEEvytAAREAnaHEFItsfpeGYNTVVGERGTTLSGGQKQRLA 516
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLmglyghkglFRRLSKADKA---KVDEA--LERV-----GLSELADRQIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 517 IARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRgAHC-IVVMADGRV 582
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVL-EYFdRVLLLNRTV 209
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
107-310 |
7.50e-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: 7.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 107 YLVLLSHVGERMavdmRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLS 186
Cdd:cd18589 60 YNITMSRIHSRL----QGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 187 TRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRC--RAE 264
Cdd:cd18589 136 PKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRlnKKE 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 533869216 265 ELGRGIALF-QGLSNIAfncMVLGTLFIGGSLVAGQQLTGGDLMSFL 310
Cdd:cd18589 216 AAAYAVSMWtSSFSGLA---LKVGILYYGGQLVTAGTVSSGDLVTFV 259
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
367-587 |
1.29e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.13 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPC-RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLERfydPTAGVVMLDGRDLRTLDPSWLR 442
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 443 G--QVVGFISQE-PVLFGTTIMENIRFgKLEA---SDEEVYTAARE-------ANAHEFitsFPegyntvvgergTTLSG 509
Cdd:PRK11153 79 KarRQIGMIFQHfNLLSSRTVFDNVAL-PLELagtPKAEIKARVTEllelvglSDKADR---YP-----------AQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 510 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAG 586
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
.
gi 533869216 587 T 587
Cdd:PRK11153 224 T 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
366-608 |
1.61e-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: 118.89 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYpCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswlrgqv 445
Cdd:TIGR00957 636 SITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 VGFISQEPVLFGTTIMENIRFGKleASDEEVYTAAREANAH-EFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQ 524
Cdd:TIGR00957 701 VAYVPQQAWIQNDSLRENILFGK--ALNEKYYQQVLEACALlPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 525 PTVLILDEATSALDAESERVVQEAL---DRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAEL 601
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
....*..
gi 533869216 602 IRRQALD 608
Cdd:TIGR00957 859 LRTYAPD 865
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
380-582 |
1.86e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.27 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 380 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP--SWLRGqvVGFISQEPVLFG 457
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdAQAAG--IAIIHQELNLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 458 T-TIMENIRFGKLEAS-----DEEVYTAAREAnAHEFITSFPEgyNTVVGErgttLSGGQKQRLAIARALIKQPTVLILD 531
Cdd:COG1129 93 NlSVAENIFLGREPRRgglidWRAMRRRAREL-LARLGLDIDP--DTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 532 EATSAL-DAESER---VVQEaLdrASAGRTVLVIAHRLSTVRgAHC--IVVMADGRV 582
Cdd:COG1129 166 EPTASLtEREVERlfrIIRR-L--KAQGVAIIYISHRLDEVF-EIAdrVTVLRDGRL 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
365-591 |
3.00e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 113.24 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 365 GSVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLerfyDPTAGVVMLDGRDLRTLDPSw 440
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrmIAGLE----DPTSGEILIGGRDVTDLPPK- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 441 LRGqvVGFISQEPVLFGT-TIMENIRFG----KLEAS--DEEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQ 513
Cdd:COG3839 74 DRN--IAMVFQSYALYPHmTVYENIAFPlklrKVPKAeiDRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 514 RLAIARALIKQPTVLILDEATSALDAESeRV--------VQEALDRAsagrTVLV---------IAHRlstvrgahcIVV 576
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRLGTT----TIYVthdqveamtLADR---------IAV 206
|
250
....*....|....*
gi 533869216 577 MADGRVWEAGTHEEL 591
Cdd:COG3839 207 MNDGRIQQVGTPEEL 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
366-591 |
4.41e-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: 110.12 E-value: 4.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlRGQV 445
Cdd:cd03296 2 SIEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 VGFISQEPVLFG-TTIMENIRFG-KLEASDEEVYTAAREANAHEFI-----TSFPEGYNTvvgergtTLSGGQKQRLAIA 518
Cdd:cd03296 76 VGFVFQHYALFRhMTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYPA-------QLSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 519 RALIKQPTVLILDEATSALDA----ESERVVQEALDRASAgRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEEL 591
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHV-TTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
49-340 |
4.67e-27 |
|
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: 111.47 E-value: 4.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 49 LALGAALVNVQIPLLLGQLVEVVAKYTRDHVGSFmtesqNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFS 128
Cdd:cd18778 7 CALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLL-----GLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 129 SLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMG 208
Cdd:cd18778 82 KLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 209 SGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAelEACRCRAEELGrgiALFqgLSNIAFNCMV--- 285
Cdd:cd18778 162 KKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEA--LSRRYRKAQLR---AMK--LWAIFHPLMEflt 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 286 -LGT---LFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18778 235 sLGTvlvLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
381-582 |
6.38e-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: 110.13 E-value: 6.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWL--RGQVVGFisQEPVLFGT 458
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarLGIARTF--QNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 -TIMENI-----------------RFGKLEASDEEVYTAAREAnAHEFitsfpeGYNTVVGERGTTLSGGQKQRLAIARA 520
Cdd:COG0411 94 lTVLENVlvaaharlgrgllaallRLPRARREEREARERAEEL-LERV------GLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 521 LIKQPTVLILDEATSAL-DAESERVVQ--EALdRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 582
Cdd:COG0411 167 LATEPKLLLLDEPAAGLnPEETEELAEliRRL-RDERGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
366-582 |
2.06e-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: 106.48 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPCRPG---FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL--ERFYDPTAGVVMLDGRDLrtlDPSW 440
Cdd:cd03213 3 TLSFRNLTVTVKSSPSksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 441 LRGQVvGFISQEPVLFGT-TIMENIRFgkleasdeevytAAREanahefitsfpegyntvvgeRGttLSGGQKQRLAIAR 519
Cdd:cd03213 80 FRKII-GYVPQDDILHPTlTVRETLMF------------AAKL--------------------RG--LSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 520 ALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRGAHC--IVVMADGRV 582
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSEIFELFdkLLLLSQGRV 190
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
367-610 |
4.46e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.91 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPGFeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVV 446
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR-KHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEP--VLFGTTIMENIRFG------KLEASDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIA 518
Cdd:PRK13648 86 GIVFQNPdnQFVGSIVKYDVAFGlenhavPYDEMHRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 519 RALIKQPTVLILDEATSALDAESERVVQEALDRASAGR--TVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGG 596
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
250
....*....|....
gi 533869216 597 LYAELirrqALDAP 610
Cdd:PRK13648 235 ELTRI----GLDLP 244
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
44-340 |
4.55e-26 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 108.32 E-value: 4.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 44 ILSCQLALGAALVNVQIPLLLGQLVEvvaKYTRDHVGSFMTEsqnLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMR 123
Cdd:cd18545 3 LLALLLMLLSTAASLAGPYLIKIAID---EYIPNGDLSGLLI---IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 124 RALFSSLLRQDITFFDANKTGQLVSRLTTDVqefkSSFKLVISQGL----RSCTQVAGCLVSLSMLSTRLTLLLMVATPA 199
Cdd:cd18545 77 QDLFSHLQKLSFSFFDSRPVGKILSRVINDV----NSLSDLLSNGLinliPDLLTLVGIVIIMFSLNVRLALVTLAVLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 200 LMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEER--------YGAELEACRcraeelgrgia 271
Cdd:cd18545 153 LVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIfdelnrenRKANMRAVR----------- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 272 LFQGLSNIAFNCMVLGT---LFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18545 222 LNALFWPLVELISALGTalvYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
44-340 |
4.67e-26 |
|
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: 108.63 E-value: 4.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 44 ILSCQLALGAALVNVQIPLLLGQLV-EVVAKYTRDHVGSFMtesqnLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDM 122
Cdd:cd18544 2 ILALLLLLLATALELLGPLLIKRAIdDYIVPGQGDLQGLLL-----LALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 123 RRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMG 202
Cdd:cd18544 77 RRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 203 VGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGA---ELEACRCRAEELGrgiALF----QG 275
Cdd:cd18544 157 ATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEinqEYRKANLKSIKLF---ALFrplvEL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 276 LSNIAfncmVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18544 234 LSSLA----LALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
381-592 |
6.32e-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: 106.60 E-value: 6.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGT-T 459
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 460 IMENIRFG--------KLEASDEEVYTAareanahefitsFPegyntVVGER----GTTLSGGQKQRLAIARALIKQPTV 527
Cdd:COG0410 95 VEENLLLGayarrdraEVRADLERVYEL------------FP-----RLKERrrqrAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 528 LILDEATSALdaeSERVVQE---ALDR-ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELL 592
Cdd:COG0410 158 LLLDEPSLGL---APLIVEEifeIIRRlNREGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELL 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
367-613 |
7.75e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.80 E-value: 7.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPGFE--VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML------DGRDLRTLDP 438
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 439 swLRgQVVGFISQ--EPVLFGTTIMENIRFGKLE--ASDEEVYTAAREANA-----HEFITSFPegyntvvgergTTLSG 509
Cdd:PRK13634 83 --LR-KKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIElvglpEELLARSP-----------FELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 510 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAG 586
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQG 228
|
250 260
....*....|....*....|....*..
gi 533869216 587 THEELLKKGglyAELIRRQaLDAPRTA 613
Cdd:PRK13634 229 TPREIFADP---DELEAIG-LDLPETV 251
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
93-310 |
8.01e-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: 107.92 E-value: 8.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFgYLVLLSHV-GERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQE------------FKS 159
Cdd:cd18549 48 LLALYILRTLLNY-FVTYWGHVmGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDiselahhgpedlFIS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 160 SFKLVisqglrsctqvaGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTV 239
Cdd:cd18549 127 IITII------------GSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVV 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 240 RAFAMEQREEERYGAELEACRcRAEELG-RGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL 310
Cdd:cd18549 195 KAFANEEYEIEKFDEGNDRFL-ESKKKAyKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFL 265
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
189-602 |
1.03e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 113.29 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 189 LTLLLMVATPalmgvgTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAeleacrCRAEELG- 267
Cdd:PLN03130 448 LMLVLMFPIQ------TFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQT------VRDDELSw 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 268 -RGIALFQGLSNIAFNCM-VLGTL-------FIGGSLVAGQQLTGGDLMS------FLVASQTVQRSMANLSVLFGQVVr 332
Cdd:PLN03130 516 fRKAQLLSAFNSFILNSIpVLVTVvsfgvftLLGGDLTPARAFTSLSLFAvlrfplFMLPNLITQAVNANVSLKRLEEL- 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 333 gLSAGARVfeyMALNPciPLSGGccVPkeqlrgSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVA 412
Cdd:PLN03130 595 -LLAEERV---LLPNP--PLEPG--LP------AISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLI 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 413 SLLERFYDPTAGVVMLdgrdlrtldpswLRGQVvGFISQEPVLFGTTIMENIRFGkLEASDEEVYTAAREANAHEFITSF 492
Cdd:PLN03130 661 SAMLGELPPRSDASVV------------IRGTV-AYVPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLL 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 493 PEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESER-VVQEALDRASAGRT-VLVI--AHRLSTV 568
Cdd:PLN03130 727 PGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRqVFDKCIKDELRGKTrVLVTnqLHFLSQV 806
|
410 420 430
....*....|....*....|....*....|....
gi 533869216 569 RGahcIVVMADGRVWEAGTHEELLKKGGLYAELI 602
Cdd:PLN03130 807 DR---IILVHEGMIKEEGTYEELSNNGPLFQKLM 837
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
49-591 |
1.27e-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: 113.08 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 49 LALGAALVNVQiPLLLGQlveVVAKYTRDHvgsfmTESQNLSTHLLI----LYGVQGLLTFGYLVLLSHVGERMAVDMRR 124
Cdd:TIGR01271 89 LYFGEATKAVQ-PLLLGR---IIASYDPFN-----APEREIAYYLALglclLFIVRTLLLHPAIFGLHHLGMQMRIALFS 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 125 ALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFklvisqGLRSCTQVA--GCLVSLSMLSTRLTLLLMVATPALMG 202
Cdd:TIGR01271 160 LIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGL------ALAHFVWIAplQVILLMGLIWELLEVNGFCGLGFLIL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 203 VGtLMGSGLRKLSRQCQEQ----IARAMGVADEALGNVRTVRAF----AMEQREEERYGAELEACR----CR-------- 262
Cdd:TIGR01271 234 LA-LFQACLGQKMMPYRDKragkISERLAITSEIIENIQSVKAYcweeAMEKIIKNIRQDELKLTRkiayLRyfyssaff 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 263 ------------AEELGRGIALFQGLSNIAFnCMVLgtlfiggSLVAGQQLTGG------------DLMSFLVASQ--TV 316
Cdd:TIGR01271 313 fsgffvvflsvvPYALIKGIILRRIFTTISY-CIVL-------RMTVTRQFPGAiqtwydslgaitKIQDFLCKEEykTL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 317 QRSMANLSVLFGQVVRGLSAG-ARVFEYMALNPCiplsggccvPKEQLRG--SVTFQNvcFSYPCRPgfeVLKDFTLTLP 393
Cdd:TIGR01271 385 EYNLTTTEVEMVNVTASWDEGiGELFEKIKQNNK---------ARKQPNGddGLFFSN--FSLYVTP---VLKNISFKLE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 394 PGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswlrgqvVGFISQEPVLFGTTIMENIRFGKleASD 473
Cdd:TIGR01271 451 KGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPGTIKDNIIFGL--SYD 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 474 EEVYTAAREA-NAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESER-VVQEALDR 551
Cdd:TIGR01271 515 EYRYTSVIKAcQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKeIFESCLCK 594
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 533869216 552 ASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEEL 591
Cdd:TIGR01271 595 LMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
367-576 |
1.28e-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: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLErfydPTAGVVMLDGRDLRTLDPSWLR 442
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 443 gqVVGFISQEPVLFGT-TIMENIRF----GKLEASDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAI 517
Cdd:COG4133 76 --RLAYLGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 518 ARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRGAHCIVV 576
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
387-586 |
1.93e-25 |
|
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: 104.50 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 387 DFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlrGQVVGFISQEPVLFG-TTIMENIR 465
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRPVSMLFQENNLFAhLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 466 FG-----KLEASDEE-VYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIARALIKQPTVLILDEATSALD- 538
Cdd:cd03298 93 LGlspglKLTAEDRQaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDp 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 533869216 539 AESERVVQEALD-RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAG 586
Cdd:cd03298 162 ALRAEMLDLVLDlHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
383-606 |
5.46e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 103.99 E-value: 5.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL---ERfYDPTAGVVMLDGRDLRTLDPS--WLRGQVVGFisQEPV--- 454
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPDerARAGIFLAF--QYPVeip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 -----LFGTTIMENIRFGKLEASD--EEVYTAAREAN-AHEFITSfpeGYNtvVGergttLSGGQKQRLAIARALIKQPT 526
Cdd:COG0396 91 gvsvsNFLRTALNARRGEELSAREflKLLKEKMKELGlDEDFLDR---YVN--EG-----FSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 527 VLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAH--RLSTVRGAHCIVVMADGRVWEAGTHE---ELLKKGglYAE 600
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKElalELEEEG--YDW 238
|
....*.
gi 533869216 601 LIRRQA 606
Cdd:COG0396 239 LKEEAA 244
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
367-610 |
7.11e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.88 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPGfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTA---GVVMLDGRDLrTLDPSWLRG 443
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITL-TAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 444 QVVGFISQEP--VLFGTTIMENIRFGkLE---ASDEEVYTAAREANAH----EFITSFPEgyntvvgergtTLSGGQKQR 514
Cdd:PRK13640 84 EKVGIVFQNPdnQFVGATVGDDVAFG-LEnraVPRPEMIKIVRDVLADvgmlDYIDSEPA-----------NLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 515 LAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELL 592
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231
|
250
....*....|....*...
gi 533869216 593 KKgglyAELIRRQALDAP 610
Cdd:PRK13640 232 SK----VEMLKEIGLDIP 245
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
367-592 |
7.85e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.68 E-value: 7.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDlrTLDPSWLRG--Q 444
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGirK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 445 VVGFISQEP--VLFGTTIMENIRFGK----LEASD--EEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLA 516
Cdd:PRK13644 78 LVGIVFQNPetQFVGRTVEEDLAFGPenlcLPPIEirKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 517 IARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELL 592
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
371-582 |
7.92e-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: 102.66 E-value: 7.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 371 NVCFSYPCRpgfEVLKDFTLTLPPGkIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVVGFIS 450
Cdd:cd03264 5 NLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLR-RRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 451 QEPvlfgtTIMENIRfgkleaSDEEVYTAAR-----EANAHEFITSFPE--GYNTVVGERGTTLSGGQKQRLAIARALIK 523
Cdd:cd03264 79 QEF-----GVYPNFT------VREFLDYIAWlkgipSKEVKARVDEVLElvNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 524 QPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 582
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKL 207
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
384-551 |
8.27e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.87 E-value: 8.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLErfydPTAGVVMLDGRDLRTLDPSWLRGQvVGFISQEPVLFGTT 459
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTllkiVASLIS----PTSGTLLFEGEDISTLKPEIYRQQ-VSYCAQTPTLFGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 460 IMENIRFG---KLEASDEEVYTAareanaheFITSF--PEgynTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 534
Cdd:PRK10247 97 VYDNLIFPwqiRNQQPDPAIFLD--------DLERFalPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170
....*....|....*..
gi 533869216 535 SALDAESERVVQEALDR 551
Cdd:PRK10247 166 SALDESNKHNVNEIIHR 182
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
383-591 |
1.12e-24 |
|
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: 102.60 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGT-TIM 461
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVPQGREIFPRlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 462 ENIRFGkLEAsdeevyTAAREANAHEFITS-FPEgYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD-- 538
Cdd:TIGR03410 94 ENLLTG-LAA------LPRRSRKIPDEIYElFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQps 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 539 --AESERVVQEAldRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEEL 591
Cdd:TIGR03410 166 iiKDIGRVIRRL--RAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
370-615 |
1.24e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.31 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSypcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPsWLRGQVVGFI 449
Cdd:PRK13548 6 RNLSVR---LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 450 SQEPVL-FGTTIMENIRFGKL------EASDEEVYTAAREANAHEFITSFpegYntvvgergTTLSGGQKQRLAIARALI 522
Cdd:PRK13548 82 PQHSSLsFPFTVEEVVAMGRAphglsrAEDDALVAAALAQVDLAHLAGRD---Y--------PQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 523 ------KQPTVLILDEATSALD-AESERVVQEALDRA-SAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEELLK 593
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAhERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
250 260
....*....|....*....|....*...
gi 533869216 594 kgglyAELIRR------QALDAPRTAAP 615
Cdd:PRK13548 231 -----PETLRRvygadvLVQPHPETGAP 253
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
367-613 |
1.33e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.04 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGrDLRTLDPSWLRGQVV 446
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEP--VLFGTTIMENIRFG------KLEASDEEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIA 518
Cdd:PRK13650 84 GMVFQNPdnQFVGATVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 519 RALIKQPTVLILDEATSALDAESE----RVVQEAldRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKK 594
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRleliKTIKGI--RDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
250
....*....|....*....
gi 533869216 595 GGLYAELirrqALDAPRTA 613
Cdd:PRK13650 231 GNDLLQL----GLDIPFTT 245
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
367-586 |
1.81e-24 |
|
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: 101.56 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqvV 446
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRD--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVLF-GTTIMENIRFG-KL-----EASDEEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIAR 519
Cdd:cd03301 75 AMVFQNYALYpHMTVYDNIAFGlKLrkvpkDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 520 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH-RLSTVRGAHCIVVMADGRVWEAG 586
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
380-580 |
1.96e-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: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 380 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQ---VVGFISQEPVLF 456
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrySVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 457 GTTIMENIRFGklEASDEEVYTAAREA-NAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 535
Cdd:cd03290 92 NATVEENITFG--SPFNKQRYKAVTDAcSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 533869216 536 ALDAE-SERVVQEALDR--ASAGRTVLVIAHRLSTVRGAHCIVVMADG 580
Cdd:cd03290 170 ALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
371-613 |
3.49e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.46 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 371 NVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG-QVVGFI 449
Cdd:PRK13639 6 DLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVrKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 450 SQEP--VLFGTTIMENIRFGKLEA--SDEEVYTAAREANAHEFItsfpEGYNTVVGERgttLSGGQKQRLAIARALIKQP 525
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEALKAVGM----EGFENKPPHH---LSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 526 TVLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKKgglyAELIR 603
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSD----IETIR 232
|
250
....*....|
gi 533869216 604 RQALDAPRTA 613
Cdd:PRK13639 233 KANLRLPRVA 242
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
370-602 |
4.68e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.12 E-value: 4.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYpcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVvGFI 449
Cdd:PRK13647 8 EDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV-GLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 450 SQEP--VLFGTTIMENIRFG--KLEASDEEVYTAAREA----NAHEFITSFPegYNtvvgergttLSGGQKQRLAIARAL 521
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAFGpvNMGLDKDEVERRVEEAlkavRMWDFRDKPP--YH---------LSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 522 IKQPTVLILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAG-----THEELLKK 594
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHnQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQ 233
|
....*...
gi 533869216 595 GGLYAELI 602
Cdd:PRK13647 234 AGLRLPLV 241
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
99-309 |
5.01e-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: 102.56 E-value: 5.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 99 VQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGC 178
Cdd:cd18550 51 ASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVAT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 179 LVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEAL--GNVRTVRAFAMEQREEERYGAEL 256
Cdd:cd18550 131 LVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARRS 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 257 EACR---CRAEELGRgiALFQGLSnIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSF 309
Cdd:cd18550 211 RELRdlgVRQALAGR--WFFAALG-LFTAIGPALVYWVGGLLVIGGGLTIGTLVAF 263
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
371-591 |
6.34e-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: 6.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 371 NVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswlrgqvVGFIS 450
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 451 QEPVLFGTTIMENIRFGKleASDEEVYTAAREA-NAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLI 529
Cdd:cd03291 105 QFSWIMPGTIKENIIFGV--SYDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 533869216 530 LDEATSALDAESERVVQEA-LDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEEL 591
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
300-584 |
6.57e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 106.04 E-value: 6.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 300 QLTGGDLMsflvasQTVQrsmanlsvLFGQVVRGLS-------------AGA-RVFEYM-ALNPCIPLSGGCCVPKEQLR 364
Cdd:COG4178 295 EITLGGLM------QAAS--------AFGQVQGALSwfvdnyqslaewrATVdRLAGFEeALEAADALPEAASRIETSED 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 365 GSVTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLlerfYDPTAGVVMLDgRDLRTLdpsw 440
Cdd:COG4178 361 GALALEDLTLRTP--DGRPLLEDLSLSLKPGERLLITGPSGSGKSTllraIAGL----WPYGSGRIARP-AGARVL---- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 441 lrgqvvgFISQEPVLFGTTIMENIRF--GKLEASDEEVYTAAREANAHEFITSFPEGYNtvvgeRGTTLSGGQKQRLAIA 518
Cdd:COG4178 430 -------FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERLDEEAD-----WDQVLSLGEQQRLAFA 497
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 519 RALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWE 584
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQ 563
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
382-623 |
8.95e-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: 105.54 E-value: 8.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 382 FEVLKDFTLTLPPGKIVALVGQSGGGKT----TVASLLERFYDPTAGVVMLDGRDLRTLDPSWL---RGQVVGFISQEPV 454
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELrriRGNRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 -----LF--GTTIMENIRFgKLEASDEEVYTAAREA-------NAHEFITSFP-EgyntvvgergttLSGGQKQRLAIAR 519
Cdd:COG4172 103 tslnpLHtiGKQIAEVLRL-HRGLSGAAARARALELlervgipDPERRLDAYPhQ------------LSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 520 ALIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELL 592
Cdd:COG4172 170 ALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAELF 245
|
250 260 270
....*....|....*....|....*....|..
gi 533869216 593 KK-GGLYAelirRQALDAPRTAAPPPKKPEGP 623
Cdd:COG4172 246 AApQHPYT----RKLLAAEPRGDPRPVPPDAP 273
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
367-582 |
1.01e-23 |
|
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: 99.79 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRg 443
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 444 QVVGFISQEPVLFGT-TIMENIRFGkLEASD-------EEVYTAAREANAHEFITSFPEGyntvvgergttLSGGQKQRL 515
Cdd:cd03292 78 RKIGVVFQDFRLLPDrNVYENVAFA-LEVTGvppreirKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 516 AIARALIKQPTVLILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLSTV-RGAHCIVVMADGRV 582
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkAGTTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
385-582 |
1.35e-23 |
|
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: 99.29 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTLTLP---PGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDL----RTLD-PSWLRGqvVGFISQEPVLF 456
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINlPPQQRK--IGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 457 -GTTIMENIRFGKLEASDEEVYTAAREANAHEFITSfpegyntvVGERGT-TLSGGQKQRLAIARALIKQPTVLILDEAT 534
Cdd:cd03297 88 pHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDH--------LLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 533869216 535 SALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RGAHCIVVMADGRV 582
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRL 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
383-590 |
1.93e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 102.72 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlRGQVVGFISQEPVLF-GTTIM 461
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA---ENRHVNTVFQSYALFpHMTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 462 ENIRFG----KLEASD--EEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPTVLILDEATS 535
Cdd:PRK09452 105 ENVAFGlrmqKTPAAEitPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 533869216 536 ALDAESERVVQ---EALDRaSAGRTVLVIAH----RLS-TVRgahcIVVMADGRVWEAGTHEE 590
Cdd:PRK09452 174 ALDYKLRKQMQnelKALQR-KLGITFVFVTHdqeeALTmSDR----IVVMRDGRIEQDGTPRE 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
370-587 |
1.93e-23 |
|
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: 99.43 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASL---LERfydPTAGVVMLDGRDLRTLDP---SWLR 442
Cdd:COG4181 12 RGLTKTVGTGAGeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDEdarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 443 GQVVGFISQEPVLFGT-TIMENIRFGKLEASDEEVYTAAREANAhefitsfpegynTV-VGERGT----TLSGGQKQRLA 516
Cdd:COG4181 89 ARHVGFVFQSFQLLPTlTALENVMLPLELAGRRDARARARALLE------------RVgLGHRLDhypaQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 533869216 517 IARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGT 587
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
366-589 |
2.07e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 99.32 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLERfydPTAGVVMLDGRDL---RTLDPS 439
Cdd:COG4161 2 SIQLKNINCFYG---SHQALFDINLECPSGETLVLLGPSGAGKSSllrVLNLLET---PDSGQLNIAGHQFdfsQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 440 WLRG--QVVGFISQE----PVLfgtTIMENI--------RFGKLEASDEEVYTAAReANAHEFITSFPegyntvvgergT 505
Cdd:COG4161 76 AIRLlrQKVGMVFQQynlwPHL---TVMENLieapckvlGLSKEQAREKAMKLLAR-LRLTDKADRFP-----------L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 506 TLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVW 583
Cdd:COG4161 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRII 220
|
....*.
gi 533869216 584 EAGTHE 589
Cdd:COG4161 221 EQGDAS 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
367-592 |
2.72e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 99.01 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGrdLRTLDPS----WLR 442
Cdd:PRK09493 2 IEFKNVSKHFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKvderLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 443 gQVVGFISQEPVLF-GTTIMENIRFGKLE---ASDEEVYTAAREANAHefitsfpegyntvVG--ERG----TTLSGGQK 512
Cdd:PRK09493 77 -QEAGMVFQQFYLFpHLTALENVMFGPLRvrgASKEEAEKQARELLAK-------------VGlaERAhhypSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 513 QRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEE 590
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222
|
..
gi 533869216 591 LL 592
Cdd:PRK09493 223 LI 224
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
93-310 |
3.38e-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: 100.26 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 172
Cdd:cd18546 45 YLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 173 TQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERY 252
Cdd:cd18546 125 LTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERF 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 253 GAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL 310
Cdd:cd18546 205 AELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFL 262
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
384-592 |
4.75e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.93 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGTTIMEN 463
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 464 IR---------FGKLEASDEEVYTAAREANahefitsfpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 534
Cdd:PRK11231 97 VAygrspwlslWGRLSAEDNARVNQAMEQT----------RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 533869216 535 SALD----AESERVVQEaldRASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELL 592
Cdd:PRK11231 167 TYLDinhqVELMRLMRE---LNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
365-602 |
4.79e-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: 99.16 E-value: 4.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 365 GSVTFQNVCFSYpCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDpTAGVVMLDGRDLRTLDPSWLRgQ 444
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWR-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 445 VVGFISQEPVLFGTTIMENIR-FGKLeaSDEEVYTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIK 523
Cdd:cd03289 78 AFGVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 524 QPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGLYAELI 602
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
368-563 |
5.13e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 98.78 E-value: 5.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 368 TFQNVCFSYP-CRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTldPSWLRGqVV 446
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADRG-VV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 gFisQEPVLFG-TTIMENIRFG-KLEAsdeeVYTAAREANAHEFITsfpegyntVVGERGT------TLSGGQKQRLAIA 518
Cdd:COG4525 82 -F--QKDALLPwLNVLDNVAFGlRLRG----VPKAERRARAEELLA--------LVGLADFarrriwQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 533869216 519 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH 563
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
367-611 |
5.33e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.39 E-value: 5.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPGFE---VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG 443
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 444 QVVGFISQEP--VLFGTTIMENIRFG--KLEASDEEVYTAAREA----NAHEFITSFPEgyntvvgergtTLSGGQKQRL 515
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGpeNLGIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 516 AIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLK 593
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
250
....*....|....*...
gi 533869216 594 KgglyAELIRRQALDAPR 611
Cdd:PRK13633 234 E----VEMMKKIGLDVPQ 247
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
383-585 |
5.69e-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: 97.29 E-value: 5.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWlrgQVVGFISQEPVLFGT-TIM 461
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL---RRIGALIEAPGFYPNlTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 462 ENIRFGKLeasdeevYTAAREANAHEFITsfpegyntVVGERGT------TLSGGQKQRLAIARALIKQPTVLILDEATS 535
Cdd:cd03268 91 ENLRLLAR-------LLGIRKKRIDEVLD--------VVGLKDSakkkvkGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 533869216 536 ALDAESERVVQEAL-DRASAGRTVLVIAHRLSTVRG-AHCIVVMADGR-VWEA 585
Cdd:cd03268 156 GLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKlIEEG 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
384-626 |
8.27e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.07 E-value: 8.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLrGQVVGFISQEPVL-FGTTIME 462
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA-SRRVASVPQDTSLsFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 463 NIRFGK------LEASDEEVYTAAREANAHEFITSFpegyntvVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 536
Cdd:PRK09536 97 VVEMGRtphrsrFDTWTETDRAAVERAMERTGVAQF-------ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 537 LDAESE-RVVQEALDRASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEELLKKGGLyaelirRQALDA----- 609
Cdd:PRK09536 170 LDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTADTL------RAAFDArtavg 243
|
250 260
....*....|....*....|....*...
gi 533869216 610 --PRTAAP---------PPKKPEGPRSH 626
Cdd:PRK09536 244 tdPATGAPtvtplpdpdRTEAAADTRVH 271
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
382-582 |
1.05e-22 |
|
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: 96.67 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 382 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVVGFISQEPVLFG-TTI 460
Cdd:cd03266 18 VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEAR-RRLGFVSDSTGLYDrLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 461 MENIR-FGKLEASDEEVYTAAREANAHEFitsfpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDA 539
Cdd:cd03266 96 RENLEyFAGLYGLKGDELTARLEELADRL------GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 533869216 540 ESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRV 582
Cdd:cd03266 170 MATRALREFIRQlRALGKCILFSTHIMQEVeRLCDRVVVLHRGRV 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
366-611 |
1.18e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.58 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPCRPGFE--VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDL--RTLDPSWL 441
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 442 RGQVvGFISQEP--VLFGTTIMENIRFG--KLEASDEEVYTAAREANAhefITSFPegYNTVVGERGTTLSGGQKQRLAI 517
Cdd:PRK13637 82 RKKV-GLVFQYPeyQLFEETIEKDIAFGpiNLGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 518 ARALIKQPTVLILDEATSALDAESErvvQEALDRASA-----GRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEEL 591
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGR---DEILNKIKElhkeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREV 232
|
250 260
....*....|....*....|
gi 533869216 592 LKKgglyAELIRRQALDAPR 611
Cdd:PRK13637 233 FKE----VETLESIGLAVPQ 248
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
385-597 |
1.26e-22 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 99.80 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTL----TLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRT------LDPSWLRgqvVGFISQEPV 454
Cdd:TIGR02142 9 LGDFSLdadfTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRR---IGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 LFG-TTIMENIRFGKLEASDEevYTAAREANAHEFItsfpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 533
Cdd:TIGR02142 86 LFPhLSVRGNLRYGMKRARPS--ERRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 534 TSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKKGGL 597
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
370-610 |
1.45e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.86 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrTLDPSWLRGQVVGFI 449
Cdd:PRK13642 8 ENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL-TAENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 450 SQEP--VLFGTTIMENIRFGKLEAS--DEEVYTAAREA----NAHEFITSFPegyntvvgergTTLSGGQKQRLAIARAL 521
Cdd:PRK13642 87 FQNPdnQFVGATVEDDVAFGMENQGipREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 522 IKQPTVLILDEATSALD----AESERVVQEALDRASAgrTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKKGGL 597
Cdd:PRK13642 156 ALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSED 233
|
250
....*....|...
gi 533869216 598 YAELirrqALDAP 610
Cdd:PRK13642 234 MVEI----GLDVP 242
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
384-581 |
2.24e-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: 95.96 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGR----DLRTLDPS---WLRGQVVGFISQ----- 451
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPReilALRRRTIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 452 ----------EPVLfgttimenirfgKLEASDEEVYTAAREANAHefitsfpegYNtvVGER-----GTTLSGGQKQRLA 516
Cdd:COG4778 106 prvsaldvvaEPLL------------ERGVDREEARARARELLAR---------LN--LPERlwdlpPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 517 IARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRG-AHCIVVMADGR 581
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
376-591 |
2.93e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 98.11 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 376 YPCRPGF-------EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRGQV 445
Cdd:PRK11308 15 YPVKRGLfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 ----------------VGFISQEPVLFGTtimenirfgKLEAsdeevytAAREANAHEFITSF---PEGYntvvGERGTT 506
Cdd:PRK11308 95 qivfqnpygslnprkkVGQILEEPLLINT---------SLSA-------AERREKALAMMAKVglrPEHY----DRYPHM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 507 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVV-------QEALdrasaGRTVLVIAHRLSTVRG-AHCIVVMA 578
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVlnlmmdlQQEL-----GLSYVFISHDLSVVEHiADEVMVMY 229
|
250
....*....|...
gi 533869216 579 DGRVWEAGTHEEL 591
Cdd:PRK11308 230 LGRCVEKGTKEQI 242
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
370-582 |
3.18e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.34 E-value: 3.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYPCRPG-FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP---SWLRGQV 445
Cdd:PRK10535 8 KDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalAQLRREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 VGFISQE-PVLFGTTIMENIRFGKLEASDEevyTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQ 524
Cdd:PRK10535 88 FGFIFQRyHLLSHLTAAQNVEVPAVYAGLE---RKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 525 PTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRGAHCIVVMADGRV 582
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
383-630 |
5.35e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 101.39 E-value: 5.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDgrdlrtldpswlrgQVVGFISQEPVLFGTTIME 462
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--------------RSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 463 NIRFgkleaSDEEvyTAAREANA------HEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 536
Cdd:PTZ00243 740 NILF-----FDEE--DAARLADAvrvsqlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 537 LDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEELLKK---GGLYAELIRRQAL---DA 609
Cdd:PTZ00243 813 LDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTslyATLAAELKENKDSkegDA 892
|
250 260
....*....|....*....|.
gi 533869216 610 PRTAAPPPKKPEGPRSHQHKS 630
Cdd:PTZ00243 893 DAEVAEVDAAPGGAVDHEPPV 913
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
367-592 |
1.40e-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: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAG-VVMLDGRDLRTLDPSWLRGQV 445
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 vGFIS---QEPVLFGTTIMENI---RFGKLEASDEevYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIAR 519
Cdd:COG1119 81 -GLVSpalQLRFPRDETVLDVVlsgFFDSIGLYRE--PTDEQRERARELLELL--GLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 520 ALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLV-IAHRLSTVrgAHCI---VVMADGRVWEAGTHEELL 592
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEI--PPGIthvLLLKDGRVVAAGPKEEVL 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
380-616 |
1.46e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 380 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGT- 458
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGMVHQHFMLVPNl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 TIMENIRFGkLEASDEEVYTAAReanAHEFITSFPEGY------NTVVGErgttLSGGQKQRLAIARALIKQPTVLILDE 532
Cdd:COG3845 96 TVAENIVLG-LEPTKGGRLDRKA---ARARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 533 ATSAL-DAESERVVqEALDR-ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVweAGTH-------EELlkkgglyAELI 602
Cdd:COG3845 168 PTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVMAiADRVTVLRRGKV--VGTVdtaetseEEL-------AELM 237
|
250
....*....|....*.
gi 533869216 603 --RRQALDAPRTAAPP 616
Cdd:COG3845 238 vgREVLLRVEKAPAEP 253
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
379-606 |
1.73e-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: 96.32 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 379 RPGFEVlkDFTLTLPPGKIVALVGQSGGGKTTVASL---LERfydPTAGVVMLDGRDLrtLD-------PSWLRGqvVGF 448
Cdd:COG4148 11 RGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVL--QDsargiflPPHRRR--IGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 449 ISQEPVLFGT-TIMENIRFGkleasdeevYTAAREANAHEfitSFPEgyntVVG--------ERG-TTLSGGQKQRLAIA 518
Cdd:COG4148 82 VFQEARLFPHlSVRGNLLYG---------RKRAPRAERRI---SFDE----VVEllgighllDRRpATLSGGERQRVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 519 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKKG 595
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARKAEILPYLERlrDELDIPILYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLSRP 225
|
250
....*....|.
gi 533869216 596 GLYAELIRRQA 606
Cdd:COG4148 226 DLLPLAGGEEA 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
368-563 |
2.10e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.00 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 368 TFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlRTLDPSWLRGQVvg 447
Cdd:PRK11248 3 QISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK--PVEGPGAERGVV-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 448 fISQEPVLFGTTIMENIRFGKLEASdeeVYTAAREANAHEFITSFP-EGYNTvvgERGTTLSGGQKQRLAIARALIKQPT 526
Cdd:PRK11248 76 -FQNEGLLPWRNVQDNVAFGLQLAG---VEKMQRLEIAHQMLKKVGlEGAEK---RYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 533869216 527 VLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH 563
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
367-592 |
2.14e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.99 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP-------S 439
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelakrlA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 440 WLRgQVVGFIS----QEPVLFGttimeniRF----GKLEASDEEVYTAA-----REANAHEFITsfpegyntvvgergtT 506
Cdd:COG4604 79 ILR-QENHINSrltvRELVAFG-------RFpyskGRLTAEDREIIDEAiayldLEDLADRYLD---------------E 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 507 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAS--AGRTVLVIAHRLSTvrgAHC----IVVMADG 580
Cdd:COG4604 136 LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINF---ASCyadhIVAMKDG 212
|
250
....*....|..
gi 533869216 581 RVWEAGTHEELL 592
Cdd:COG4604 213 RVVAQGTPEEII 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
383-582 |
2.20e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 93.34 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSW---LRGQVVGFISQ-EPVLFGT 458
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQKLGFIYQfHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 TIMENIRFGKLEASdeeVYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 538
Cdd:PRK11629 103 TALENVAMPLLIGK---KKPAEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 533869216 539 AESERVVQEALDR--ASAGRTVLVIAHRLSTVRGAHCIVVMADGRV 582
Cdd:PRK11629 178 ARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
381-592 |
2.24e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.66 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVV-----MLDG-----------RDLRtldpswlrgQ 444
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTarslsqqkgliRQLR---------Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 445 VVGFISQEPVLF-GTTIMENIRFG----KLEASDEEVyTAAREANAHEFITSFPEGYNTvvgergtTLSGGQKQRLAIAR 519
Cdd:PRK11264 86 HVGFVFQNFNLFpHRTVLENIIEGpvivKGEPKEEAT-ARARELLAKVGLAGKETSYPR-------RLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 520 ALIKQPTVLILDEATSALDAEserVVQEALDR----ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELL 592
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
388-592 |
2.65e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.11 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 388 FTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlrGQVVGFISQEPVLFG-TTIMENIRF 466
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS---RRPVSMLFQENNLFShLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 467 G-----KLEASD-EEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALD-- 538
Cdd:PRK10771 95 GlnpglKLNAAQrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 539 --AESERVVQEALDRASAgrTVLVIAHRLSTvrgAHCI----VVMADGRVWEAGTHEELL 592
Cdd:PRK10771 164 lrQEMLTLVSQVCQERQL--TLLMVSHSLED---AARIaprsLVVADGRIAWDGPTDELL 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
385-592 |
2.72e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.64 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG---QVVGFISQEPVLF-GTTI 460
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrKKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 461 MENIRFG------KLEASDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIARALIKQPTVLILDEAT 534
Cdd:PRK10070 124 LDNTAFGmelagiNAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 533869216 535 SALDAESERVVQEALDRASAG--RTVLVIAHRL-STVRGAHCIVVMADGRVWEAGTHEELL 592
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
382-565 |
2.73e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.08 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 382 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD--PTA---GVVMLDGRDL--RTLDPSWLRGQVvGFISQEPV 454
Cdd:PRK14243 23 FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLyaPDVDPVEVRRRI-GMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 LFGTTIMENIRFG-KLEAS----DEEVYTAAREANAHEFITSfpegyntVVGERGTTLSGGQKQRLAIARALIKQPTVLI 529
Cdd:PRK14243 102 PFPKSIYDNIAYGaRINGYkgdmDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 533869216 530 LDEATSALDAESERVVQEALDRASAGRTVLVIAHRL 565
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
367-582 |
3.36e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLdGRDLRtldpswlrgqvV 446
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVLF--GTTIMENIRfgkleasdeEVYTAAREANAHEFITSF---PEGYNTVVGergtTLSGGQKQRLAIARAL 521
Cdd:COG0488 381 GYFDQHQEELdpDKTVLDELR---------DGAPGGTEQEVRGYLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 533869216 522 IKQPTVLILDEATSALDAESERVVQEALDrASAGrTVLVIAH-R--LSTVrgAHCIVVMADGRV 582
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGV 507
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
370-611 |
3.93e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.76 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrTLDPSW-----LRgQ 444
Cdd:PRK13636 9 EELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK---PIDYSRkglmkLR-E 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 445 VVGFISQEP--VLFGTTIMENIRFG--KLEASDEEVYTAAREANAHEFITSFPEgyntvvgERGTTLSGGQKQRLAIARA 520
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 521 LIKQPTVLILDEATSALD----AESERVVQEALDraSAGRTVLVIAHRLSTVrGAHC--IVVMADGRVWEAGTHEELLKK 594
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQK--ELGLTIIIATHDIDIV-PLYCdnVFVMKEGRVILQGNPKEVFAE 232
|
250
....*....|....*..
gi 533869216 595 gglyAELIRRQALDAPR 611
Cdd:PRK13636 233 ----KEMLRKVNLRLPR 245
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
364-586 |
9.28e-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: 91.44 E-value: 9.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 364 RGSVTFQNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldPSWLRG 443
Cdd:cd03220 17 SSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSLLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 444 QVVGFisqEPVLfgtTIMENIRF-----GKLEASDEEVYtaareanahEFITSFPEgyntvVGERGT----TLSGGQKQR 514
Cdd:cd03220 91 LGGGF---NPEL---TGRENIYLngrllGLSRKEIDEKI---------DEIIEFSE-----LGDFIDlpvkTYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 515 LAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRgAHC--IVVMADGRVWEAG 586
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIK-RLCdrALVLEKGKIRFDG 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
111-602 |
1.12e-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: 97.29 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 111 LSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRL- 189
Cdd:TIGR01271 949 LVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIf 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 190 --TLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVAdeaLGNVRTVRAFAMEQREEERYGAELEACRCRAEELG 267
Cdd:TIGR01271 1029 iaAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITS---LKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYL 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 268 RGIALFQGLSNIAFNCMVLGTLFIG-GSLVAGQQLTGGDLMSFLVASQTVQRSMaNLSVLFGQVVRGLSagaRVFEYMAL 346
Cdd:TIGR01271 1106 STLRWFQMRIDIIFVFFFIAVTFIAiGTNQDGEGEVGIILTLAMNILSTLQWAV-NSSIDVDGLMRSVS---RVFKFIDL 1181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 347 NPCIPL---SGGCCVPKEQL-------------RGSVTFQNVCFSYpCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT 410
Cdd:TIGR01271 1182 PQEEPRpsgGGGKYQLSTVLvienphaqkcwpsGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKST 1260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 411 VASLLERFYDpTAGVVMLDGRDLRTLDPSWLRgQVVGFISQEPVLFGTTIMENIRfGKLEASDEEVYTAAREANAHEFIT 490
Cdd:TIGR01271 1261 LLSALLRLLS-TEGEIQIDGVSWNSVTLQTWR-KAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIE 1337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 491 SFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRG 570
Cdd:TIGR01271 1338 QFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLE 1417
|
490 500 510
....*....|....*....|....*....|..
gi 533869216 571 AHCIVVMADGRVWEAGTHEELLKKGGLYAELI 602
Cdd:TIGR01271 1418 CQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
366-589 |
1.24e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 91.61 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPCRpgfEVLKDFTLTLPPGKIVALVGQSGGGKTT---VASLLE-----------RFYDPTAGVVMLDGR 431
Cdd:PRK11124 2 SIQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLEmprsgtlniagNHFDFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 432 DLRtldpswlrgQVVGFISQE----PVLfgtTIMENIrfgkLEA-------SDEEVYTAAREANAH----EFITSFPegy 496
Cdd:PRK11124 79 ELR---------RNVGMVFQQynlwPHL---TVQQNL----IEApcrvlglSKDQALARAEKLLERlrlkPYADRFP--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 497 ntvvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCI 574
Cdd:PRK11124 140 --------LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRV 211
|
250
....*....|....*
gi 533869216 575 VVMADGRVWEAGTHE 589
Cdd:PRK11124 212 VYMENGHIVEQGDAS 226
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
379-592 |
1.53e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 91.82 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 379 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWlRGQVVGFISQEPvlfGT 458
Cdd:COG4167 23 RQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RCKHIRMIFQDP---NT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 TIMENIRFGK-LEA--------SDEEvytaaREANAHEFITS---FPEGYNTvvgeRGTTLSGGQKQRLAIARALIKQPT 526
Cdd:COG4167 99 SLNPRLNIGQiLEEplrlntdlTAEE-----REERIFATLRLvglLPEHANF----YPHMLSSGQKQRVALARALILQPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 527 VLILDEATSALDAeSERV--------VQEALdrasaGRTVLVIAHRLSTVRgaHC---IVVMADGRVWEAGTHEELL 592
Cdd:COG4167 170 IIIADEALAALDM-SVRSqiinlmleLQEKL-----GISYIYVSQHLGIVK--HIsdkVLVMHQGEVVEYGKTAEVF 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
369-563 |
1.62e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 369 FQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDgrdlrtldpswlRGQVVGF 448
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------------KGLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 449 ISQEPVLF-GTTIMENI-----RFGKLEASDEEVYTA--------AREANAHEFITSFpEGYN------TVVGERG---- 504
Cdd:COG0488 66 LPQEPPLDdDLTVLDTVldgdaELRALEAELEELEAKlaepdedlERLAELQEEFEAL-GGWEaearaeEILSGLGfpee 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 505 ------TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAEServVQ--EALDRASAGrTVLVIAH 563
Cdd:COG0488 145 dldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSH 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
347-593 |
1.66e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.88 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 347 NPCIPLSGGCCVPKEQLrgsVTFQNVCFSyPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLErFYDPT---- 422
Cdd:TIGR00955 7 NSDVFGRVAQDGSWKQL---VSRLRGCFC-RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 423 AGVVMLDGRdlrTLDPSWLRgQVVGFISQEPVLFGT-TIMENIRFGKLEASDEEVYTAAREANAHEFIT--SFPEGYNTV 499
Cdd:TIGR00955 82 SGSVLLNGM---PIDAKEMR-AISAYVQQDDLFIPTlTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 500 VGERGTT--LSGGQKQRLAIARALIKQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLST--VRGAHCI 574
Cdd:TIGR00955 158 IGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKI 237
|
250
....*....|....*....
gi 533869216 575 VVMADGRVWEAGTHEELLK 593
Cdd:TIGR00955 238 ILMAEGRVAYLGSPDQAVP 256
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
381-591 |
2.17e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.36 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGqvVGFISQEPVLF-GTT 459
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-PPYQRP--INMMFQSYALFpHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 460 IMENIRFG-------KLEASD--EEVYTAAreaNAHEFITSFPEgyntvvgergtTLSGGQKQRLAIARALIKQPTVLIL 530
Cdd:PRK11607 108 VEQNIAFGlkqdklpKAEIASrvNEMLGLV---HMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 533869216 531 DEATSALDAE-SERVVQEALD-RASAGRTVLVIAH-RLSTVRGAHCIVVMADGRVWEAGTHEEL 591
Cdd:PRK11607 174 DEPMGALDKKlRDRMQLEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
381-596 |
2.22e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.09 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlrgQVVGFISQEPVLF-GTT 459
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR-----RRIGYLPEERGLYpKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 460 IMENIR-FGKL---EASDeevytaAREaNAHEFITSFPegyntvVGERGT----TLSGGQKQRLAIARALIKQPTVLILD 531
Cdd:COG4152 88 VGEQLVyLARLkglSKAE------AKR-RADEWLERLG------LGDRANkkveELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 532 EATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTVRgAHC--IVVMADGRVWEAGTHEELLKKGG 596
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVE-ELCdrIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
384-586 |
2.53e-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: 89.65 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDpswlrGQVVGFISQEPVLF-GTTIME 462
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRIGYLPEERGLYpKMKVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 463 NIR-FGKLEA-SDEEvytAAREANahEFITSFP-EGYNTVVGErgtTLSGGQKQRLAIARALIKQPTVLILDEATSALDA 539
Cdd:cd03269 90 QLVyLAQLKGlKKEE---ARRRID--EWLERLElSEYANKRVE---ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 533869216 540 ESERVVQEAL-DRASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAG 586
Cdd:cd03269 162 VNVELLKDVIrELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
383-563 |
2.63e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.74 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD--PTA---GVVMLDGRDLRTLDPSWLRGQVvGFISQEPVLFG 457
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRRV-QMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 458 T-TIMENIRFG----KLEASDEEVYTAAREAnaHEFITSFPEGYNTVVGERGTtLSGGQKQRLAIARALIKQPTVLILDE 532
Cdd:PRK14247 96 NlSIFENVALGlklnRLVKSKKELQERVRWA--LEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190
....*....|....*....|....*....|.
gi 533869216 533 ATSALDAESERVVQEALDRASAGRTVLVIAH 563
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
381-595 |
2.79e-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: 89.12 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF--YDPTAGVVMLDGRDLRTLDPS--WLRGQVVGFisQEPVLF 456
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEerARLGIFLAF--QYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 457 -GTTIMENIRFgkleasdeevytaareanahefitsfpegyntvVGErgtTLSGGQKQRLAIARALIKQPTVLILDEATS 535
Cdd:cd03217 90 pGVKNADFLRY---------------------------------VNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 536 ALDAESERVVQEALDR-ASAGRTVLVIAHR---LSTVRG--AHcivVMADGRVWEAGTHE---ELLKKG 595
Cdd:cd03217 134 GLDIDALRLVAEVINKlREEGKSVLIITHYqrlLDYIKPdrVH---VLYDGRIVKSGDKElalEIEKKG 199
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
384-594 |
3.22e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.48 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTldpSWLRGQVVGFISQEPVLF-GTTIME 462
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRDICMVFQSYALFpHMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 463 NIRFG--KLEASDEEVYTAAREANAHEFITSFPEGYntvVGErgttLSGGQKQRLAIARALIKQPTVLILDEATSALDAE 540
Cdd:PRK11432 98 NVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRY---VDQ----ISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 541 SERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLKK 594
Cdd:PRK11432 171 LRRSMREKIRelQQQFNITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
383-591 |
3.57e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.45 E-value: 3.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlRGQVVGFISQEPVLF-GTTIM 461
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDRKVGFVFQHYALFrHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 462 ENIRFG----------KLEASDEEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPTVLILD 531
Cdd:PRK10851 93 DNIAFGltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 532 EATSALDAESE-------RVVQEALDRASagrtVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHEEL 591
Cdd:PRK10851 162 EPFGALDAQVRkelrrwlRQLHEELKFTS----VFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
370-592 |
3.57e-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: 89.91 E-value: 3.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrTLDPSWLRGQV-VGF 448
Cdd:cd03218 4 ENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMHKRARLgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 449 ISQEPVLF-GTTIMENIR--FGKLEASDEEvytaaREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQP 525
Cdd:cd03218 80 LPQEASIFrKLTVEENILavLEIRGLSKKE-----REEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 526 TVLILDEATSALD----AESERVVQEALDRasaGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEELL 592
Cdd:cd03218 153 KFLLLDEPFAGVDpiavQDIQKIIKILKDR---GIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
366-594 |
3.82e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.96 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPCRPGFE--VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTL----DPS 439
Cdd:PRK13649 2 GINLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 440 WLRGQVvGFISQ--EPVLFGTTIMENIRFG--KLEASDEEVYTAAREANAHEFITsfpegyNTVVGERGTTLSGGQKQRL 515
Cdd:PRK13649 82 QIRKKV-GLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 516 AIARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLK 593
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQ 234
|
.
gi 533869216 594 K 594
Cdd:PRK13649 235 D 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
366-613 |
3.84e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.04 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPCRPGFEV--LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrTLDPS---- 439
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI-TPETGnknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 440 -WLRGQVvGFISQ--EPVLFGTTIMENIRFGKLE--ASDEEvytaAREAnAHEFITSFpeGYNTVVGERGT-TLSGGQKQ 513
Cdd:PRK13641 81 kKLRKKV-SLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDE----AKEK-ALKWLKKV--GLSEDLISKSPfELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 514 RLAIARALIKQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEEL 591
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
250 260
....*....|....*....|..
gi 533869216 592 LKKgglyAELIRRQALDAPRTA 613
Cdd:PRK13641 233 FSD----KEWLKKHYLDEPATS 250
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
370-593 |
4.47e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 89.70 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVasllerFY------DPTAGVVMLDGRDLrTLDPSWLRG 443
Cdd:COG1137 7 ENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDI-THLPMHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 444 QV-VGFISQEPVLF-GTTIMENIRfGKLEASdeEVYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARAL 521
Cdd:COG1137 77 RLgIGYLPQEASIFrKLTVEDNIL-AVLELR--KLSKKEREERLEELLEEF--GITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 522 IKQPTVLILDEATSALD----AESERVVQEALDRasaGRTVLVIAHRlstVRGAHCIV----VMADGRVWEAGTHEELLK 593
Cdd:COG1137 152 ATNPKFILLDEPFAGVDpiavADIQKIIRHLKER---GIGVLITDHN---VRETLGICdrayIISEGKVLAEGTPEEILN 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
383-565 |
5.42e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.83 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD-----PTAGVVMLDGRDL--RTLDPSWLRGQVvGFISQEPVL 455
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEI-GMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 456 FGTTIMENIRFG-------KLEASDEEVYTAAREANAHEFITSfpEGYNTVVGergttLSGGQKQRLAIARALIKQPTVL 528
Cdd:PRK14239 98 FPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVLATSPKII 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 533869216 529 ILDEATSALDAESERVVQEALDRASAGRTVLVIAHRL 565
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
366-595 |
5.75e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.61 E-value: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYpcRPG----FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDL--RTLDpS 439
Cdd:PRK13646 2 TIRFDNVSYTY--QKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthKTKD-K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 440 WLRG--QVVGFISQ--EPVLFGTTIMENIRFG--KLEASDEEVytaarEANAHEFITSFpeGYN-TVVGERGTTLSGGQK 512
Cdd:PRK13646 79 YIRPvrKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEV-----KNYAHRLLMDL--GFSrDVMSQSPFQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 513 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHE 589
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPK 231
|
....*.
gi 533869216 590 ELLKKG 595
Cdd:PRK13646 232 ELFKDK 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
382-591 |
6.49e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.07 E-value: 6.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 382 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLdgRDLRTLDPSWLRGQV---------------- 445
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELItnpyskkiknfkelrr 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 -VGFISQEP--VLFGTTIMENIRFG-------KLEASDEEVYTAAREANAHEFITSFPEGyntvvgergttLSGGQKQRL 515
Cdd:PRK13631 117 rVSMVFQFPeyQLFKDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYLERSPFG-----------LSGGQKRRV 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 516 AIARALIKQPTVLILDEATSALDAESER-VVQEALDRASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEEL 591
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
385-563 |
6.59e-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: 89.06 E-value: 6.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlRGQVVGFISQEPVLfgtTIMENI 464
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD--RMVVFQNYSLLPWL---TVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 465 RFGkLEASDEEVYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERV 544
Cdd:TIGR01184 76 ALA-VDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|.
gi 533869216 545 VQEALDR--ASAGRTVLVIAH 563
Cdd:TIGR01184 153 LQEELMQiwEEHRVTVLMVTH 173
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
377-604 |
7.73e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 94.70 E-value: 7.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 377 PC-RPGFEVLkdfTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRT-LDPswLRgQVVGFISQEPV 454
Cdd:TIGR01257 940 PSgRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETnLDA--VR-QSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 LFG-TTIMENIRF-GKLEASDEEVYTAAREANAHEfitsfpEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDE 532
Cdd:TIGR01257 1014 LFHhLTVAEHILFyAQLKGRSWEEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 533 ATSALDAESERVVQEALDRASAGRTVLVIAHRL--STVRGAHcIVVMADGRVWEAGTheELLKKG----GLYAELIRR 604
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdeADLLGDR-IAIISQGRLYCSGT--PLFLKNcfgtGFYLTLVRK 1162
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
385-560 |
1.39e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.54 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDP---TAGVVMLDGRDLRTLdPSWLRGqvVGFISQEPVLFG-TTI 460
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAL-PAEQRR--IGILFQDDLLFPhLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 461 MENIRFG-----KLEASDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIARALIKQPTVLILDEATS 535
Cdd:COG4136 94 GENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190
....*....|....*....|....*....|
gi 533869216 536 ALDAE-----SERVVQEAldRASAGRTVLV 560
Cdd:COG4136 163 KLDAAlraqfREFVFEQI--RQRGIPALLV 190
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
390-591 |
2.44e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.12 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 390 LTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWL---RGQVVGFisQEPVLFGT-TIMENIr 465
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQiarMGVVRTF--QHVRLFREmTVIENL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 466 fgkLEASDEEVYT----------AAR--EANAHEFITSFPE--GYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILD 531
Cdd:PRK11300 102 ---LVAQHQQLKTglfsgllktpAFRraESEALDRAATWLErvGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 533869216 532 EATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEEL 591
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
375-577 |
3.68e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 375 SYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGrdlrtldpswlrGQVVGFISQ--- 451
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------------GARVAYVPQrse 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 452 EPVLFGTTIMENIRFG---------KLEASDEEVYTAAREAnahefitsfpEGYNTVVGERGTTLSGGQKQRLAIARALI 522
Cdd:NF040873 66 VPDSLPLTVRDLVAMGrwarrglwrRLTRDDRAAVDDALER----------VGLADLAGRQLGELSGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 523 KQPTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRGAHCIVVM 577
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
384-582 |
4.18e-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: 85.18 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEP----VLFGTT 459
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 460 IMENIRFGKLeasdeevytaareanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQPTVLILDEATSALDA 539
Cdd:cd03215 95 VAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 533869216 540 ESERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 582
Cdd:cd03215 138 GAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
370-610 |
6.90e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYpcRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRgQVVGFI 449
Cdd:PRK13652 7 RDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR-KFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 450 SQEP--VLFGTTIMENIRFGKL------EASDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQRLAIARAL 521
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFGPInlgldeETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 522 IKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLkkggLY 598
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIF----LQ 228
|
250
....*....|..
gi 533869216 599 AELIRRQALDAP 610
Cdd:PRK13652 229 PDLLARVHLDLP 240
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
384-584 |
7.93e-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: 86.78 E-value: 7.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG-----QVVGFISQEPVLFGT 458
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrdvQLVFQDSPSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 TIMENIR--FGKLEASDEevytAAREANAHEFITSFpEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 536
Cdd:TIGR02769 106 TVRQIIGepLRHLTSLDE----SEQKARIAELLDMV-GLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 533869216 537 LDAESERVVQEALD--RASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWE 584
Cdd:TIGR02769 181 LDMVLQAVILELLRklQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
381-591 |
8.91e-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: 85.50 E-value: 8.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVVGFISQEPVL-FGTT 459
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVR-RRIGIVFQDLSVdDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 460 IMENIR-FGKLEAsdeeVYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 538
Cdd:cd03265 90 GWENLYiHARLYG----VPGAERRERIDELLDFV--GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 539 AESERVVQEALDR--ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEEL 591
Cdd:cd03265 164 PQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
379-584 |
1.29e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 86.28 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 379 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--QVVGFISQEPV-- 454
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrRDIQMVFQDSIsa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 -----LFGTTIMENIRfgKLEASDEevytAAREANAHEFITSFpEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLI 529
Cdd:PRK10419 102 vnprkTVREIIREPLR--HLLSLDK----AERLARASEMLRAV-DLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 530 LDEATSALDaeseRVVQ-EALD-----RASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWE 584
Cdd:PRK10419 175 LDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
366-606 |
2.32e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.75 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPCRPG-------------------FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVV 426
Cdd:COG1134 4 MIEVENVSKSYRLYHEpsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 427 MLDGRdlrtldPSWLRGQVVGFisqEPVLFGttiMENIRF-----GkleASDEEVytAAREanahEFITSFPEgyntvVG 501
Cdd:COG1134 84 EVNGR------VSALLELGAGF---HPELTG---RENIYLngrllG---LSRKEI--DEKF----DEIVEFAE-----LG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 502 E------RgtTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRgAHC- 573
Cdd:COG1134 138 DfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVR-RLCd 214
|
250 260 270
....*....|....*....|....*....|....
gi 533869216 574 -IVVMADGRVWEAGTHEELLKkggLYAELIRRQA 606
Cdd:COG1134 215 rAIWLEKGRLVMDGDPEEVIA---AYEALLAGRE 245
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
384-592 |
5.45e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.94 E-value: 5.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF---YDP---TAGVVMLDGRDLRTLDPSWLRGQvVGFISQEPVLF- 456
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKE-VGMVFQQPNPFp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 457 GTTIMENIRFG-KLEASDEEVYTAAREANAHEFITSFPEGYNTvVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 535
Cdd:PRK14246 104 HLSIYDNIAYPlKSHGIKEKREIKKIVEECLRKVGLWKEVYDR-LNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 536 ALDAESERVVQEALDRASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELL 592
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
367-563 |
5.78e-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: 80.96 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVmldgrdlrtldpSWLRGQVV 446
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------TWGSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQepvlfgttimenirfgkleasdeevytaareanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQPT 526
Cdd:cd03221 66 GYFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190
....*....|....*....|....*....|....*..
gi 533869216 527 VLILDEATSALDAESERVVQEALdRASAGrTVLVIAH 563
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
390-591 |
5.81e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.29 E-value: 5.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 390 LTLPPGKIVALVGQSGGGKTTVASLLERFY--DPTAG--------VVMLDGRDLRTLDPSwlRGQVvGFISQEPVLFGT- 458
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGshiellgrTVQREGRLARDIRKS--RANT-GYIFQQFNLVNRl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 TIMENIRFGKLEASD-----EEVYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 533
Cdd:PRK09984 102 SVLENVLIGALGSTPfwrtcFSWFTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 533869216 534 TSALDAESERVVQEALD--RASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEEL 591
Cdd:PRK09984 180 IASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-592 |
6.63e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.38 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGV-----VMLDGRDLRTLDPSWLRGQVVGFISQEPVL 455
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 456 FGTTIMENI----RFGKLEASDEevYTAAREANAHEfiTSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILD 531
Cdd:PRK14271 113 FPMSIMDNVlagvRAHKLVPRKE--FRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 532 EATSALDAESERVVQEALDRASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEELL 592
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
370-586 |
6.66e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 6.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYPCRPGF--------EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYdPTAGVVMLDGRDLRTLDPSWL 441
Cdd:PRK15134 279 EQLQVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 442 -----RGQVVgfiSQEP--VLFGTTIMENIRFGKLEASDEEVYTAAREAnahEFITSFPE-GYNTVVGER-GTTLSGGQK 512
Cdd:PRK15134 358 lpvrhRIQVV---FQDPnsSLNPRLNVLQIIEEGLRVHQPTLSAAQREQ---QVIAVMEEvGLDPETRHRyPAEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 513 QRLAIARALIKQPTVLILDEATSALDaeseRVVQE---ALDRASAGR---TVLVIAHRLSTVRG-AHCIVVMADGRVWEA 585
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQ 507
|
.
gi 533869216 586 G 586
Cdd:PRK15134 508 G 508
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
389-592 |
1.03e-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: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 389 TLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML----DGRDLRTLDPSwLRGQV---VGFISQEPVLFG-TTI 460
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRAkryIGILHQEYDLYPhRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 461 MENIRFG-KLEASDEevyTAAREANAHEFITSFPEGYNTVVGERGT-TLSGGQKQRLAIARALIKQPTVLILDEATSALD 538
Cdd:TIGR03269 383 LDNLTEAiGLELPDE---LARMKAVITLKMVGFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 539 AESERVVQEAL--DRASAGRTVLVIAHRLSTVRGAhC--IVVMADGRVWEAGTHEELL 592
Cdd:TIGR03269 460 PITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDV-CdrAALMRDGKIVKIGDPEEIV 516
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
366-591 |
1.17e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.08 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGqv 445
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-ERG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 VGFISQEPVLF-GTTIMENIRFG-KLEAS-----DEEVYTAAREAN-AHefitsfpegyntVVGERGTTLSGGQKQRLAI 517
Cdd:PRK11000 77 VGMVFQSYALYpHLSVAENMSFGlKLAGAkkeeiNQRVNQVAEVLQlAH------------LLDRKPKALSGGQRQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 518 ARALIKQPTVLILDEATSALDAeSERV---VQEALDRASAGRTVLVIAH-RLSTVRGAHCIVVMADGRVWEAGTHEEL 591
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDA-ALRVqmrIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
365-611 |
1.43e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 365 GSVTFQNVCFSYPCRPGFE--VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF------------YDPTAGVVML-D 429
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEfkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetgqtivgdYAIPANLKKIkE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 430 GRDLRtldpswlrgQVVGFISQEP--VLFGTTIMENIRFG--KLEASDEEVYTAAREANAhefITSFPEGYntvVGERGT 505
Cdd:PRK13645 85 VKRLR---------KEIGLVFQFPeyQLFQETIEKDIAFGpvNLGENKQEAYKKVPELLK---LVQLPEDY---VKRSPF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 506 TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RGAHCIVVMADGRV 582
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKV 229
|
250 260
....*....|....*....|....*....
gi 533869216 583 WEAGTHEELLKKgglyAELIRRQALDAPR 611
Cdd:PRK13645 230 ISIGSPFEIFSN----QELLTKIEIDPPK 254
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
379-563 |
1.57e-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: 81.39 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 379 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGqvVGFISQEPVLFGT 458
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG--LLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 -TIMENIRFGKLEASDEEVYTAAREANAHEFiTSFPEGYntvvgergttLSGGQKQRLAIARALIKQPTVLILDEATSAL 537
Cdd:cd03231 88 lSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*..
gi 533869216 538 DAESERVVQEAL-DRASAGRTVLVIAH 563
Cdd:cd03231 157 DKAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
368-579 |
1.61e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.91 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 368 TFQNVCFSYPCRpgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVG 447
Cdd:PRK10575 13 ALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 448 FISQEPVLFGTTIMENI------------RFGKL--EASDEEVYTAAREANAHEFITSfpegyntvvgergttLSGGQKQ 513
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVaigrypwhgalgRFGAAdrEKVEEAISLVGLKPLAHRLVDS---------------LSGGERQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 514 RLAIARALIKQPTVLILDEATSALDaeservVQEALDrasagrtVLVIAHRLSTVRGAHCIVVMAD 579
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALD------IAHQVD-------VLALVHRLSQERGLTVIAVLHD 207
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
386-591 |
1.80e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.99 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 386 KDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--QVVGFISQEPV-------LF 456
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrSDIQMIFQDPLaslnprmTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 457 GTTIMENIRFGKLEASDEEVYTAAREANA-------------HEFitsfpegyntvvgergttlSGGQKQRLAIARALIK 523
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSRQEVKDRVKAMMLkvgllpnlinrypHEF-------------------SGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 533869216 524 QPTVLILDEATSALDAESE-RVVQ--EALDRaSAGRTVLVIAHRLSTVRgaHC---IVVMADGRVWEAGTHEEL 591
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQaQVVNllQQLQR-EMGLSLIFIAHDLAVVK--HIsdrVLVMYLGHAVELGTYDEV 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
359-586 |
1.93e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.06 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 359 PKEQLRGSVTfqnvcfSYPCRPGF------EV--LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDG 430
Cdd:PRK10261 312 PILQVRNLVT------RFPLRSGLlnrvtrEVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 431 RDLRTLDPSWLRG--QVVGFISQEPV-------LFGTTIMENIRFGKLEASDEevyTAAREANAHEFITSFPEGYNTVVG 501
Cdd:PRK10261 386 QRIDTLSPGKLQAlrRDIQFIFQDPYasldprqTVGDSIMEPLRVHGLLPGKA---AAARVAWLLERVGLLPEHAWRYPH 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 502 ErgttLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALD-RASAGRTVLVIAHRLSTV-RGAHCIVVMA 578
Cdd:PRK10261 463 E----FSGGQRQRICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDlQRDFGIAYLFISHDMAVVeRISHRVAVMY 538
|
....*...
gi 533869216 579 DGRVWEAG 586
Cdd:PRK10261 539 LGQIVEIG 546
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
367-564 |
2.03e-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: 79.89 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAG-VVMLDGRDLRtldpswlrgqv 445
Cdd:cd03223 1 IELENLSLATP--DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGrIGMPEGEDLL----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 vgFISQEPVLFGTTIMENIrfgkleasdeeVYTAAREanahefitsfpegyntvvgergttLSGGQKQRLAIARALIKQP 525
Cdd:cd03223 68 --FLPQRPYLPLGTLREQL-----------IYPWDDV------------------------LSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 533869216 526 TVLILDEATSALDAESERVVQEALDRASAgrTVLVIAHR 564
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
380-580 |
2.27e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.61 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 380 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQE-PVLFGT 458
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 TIMENIRFGKLEAsdEEV-------YTAARE-ANAHEFITSFPEGYNTVVGErgttLSGGQKQRLAIARALIKQPTVLIL 530
Cdd:PRK09700 96 TVLENLYIGRHLT--KKVcgvniidWREMRVrAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 533869216 531 DEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRgAHC--IVVMADG 580
Cdd:PRK09700 170 DEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIR-RICdrYTVMKDG 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
370-591 |
2.42e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.49 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlRGQVVG-- 447
Cdd:PRK15439 15 RSISKQYS---GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA--KAHQLGiy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 448 FISQEPVLFGT-TIMENIRFG--KLEASDEEVYTAAREANAHeFITSFPEGyntvvgergtTLSGGQKQRLAIARALIKQ 524
Cdd:PRK15439 90 LVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQ-LDLDSSAG----------SLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 525 PTVLILDEATSALD-AESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEEL 591
Cdd:PRK15439 159 SRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
93-340 |
3.03e-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: 83.00 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 172
Cdd:cd18565 60 TVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 173 TQVAGCLVSLSMLSTRLTLLLMVATPaLMGVGTLMGSG-LRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEER 251
Cdd:cd18565 140 VTVLGIGAILFYLNWQLALVALLPVP-LIIAGTYWFQRrIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERER 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 252 YGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLV------AGQQLTGGDLMSFLVASQTVQRSMANLSV 325
Cdd:cd18565 219 VADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVldgpplFTGTLTVGTLVTFLFYTQRLLWPLTRLGD 298
|
250
....*....|....*
gi 533869216 326 LFGQVVRGLSAGARV 340
Cdd:cd18565 299 LIDQYQRAMASAKRV 313
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
77-340 |
5.58e-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: 82.32 E-value: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 77 DHVGSFMTESQNLSTHLLILYGVQ-GLLTFGYL--VLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTD 153
Cdd:cd18558 46 SSAGPFEKLEEEMTLYAYYYLIIGaIVLITAYIqgSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 154 VQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEAL 233
Cdd:cd18558 126 VSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 234 GNVRTVRAFAMEQREEERYGAELEAcrcrAEELGRGIALFQGLSNIAFNCMVLGT----LFIGGSLVAGQQLTGGDlmsf 309
Cdd:cd18558 206 EAFRTVIAFGGQQKEETRYAQNLEI----AKRNGIKKAITFNISMGAAFLLIYASyalaFWYGTYLVTQQEYSIGE---- 277
|
250 260 270
....*....|....*....|....*....|.
gi 533869216 310 lvasqtvqrsmaNLSVLFGQVVRGLSAGARV 340
Cdd:cd18558 278 ------------VLTVFFSVLIGAFSAGQQV 296
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
379-538 |
9.92e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.60 E-value: 9.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 379 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWlRGQVVGFISQEPvlfGT 458
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-RSQRIRMIFQDP---ST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 TIMENIRFGKL-------------EASDEEVYTAAREANA-HEFITSFPEgyntvvgergtTLSGGQKQRLAIARALIKQ 524
Cdd:PRK15112 99 SLNPRQRISQIldfplrlntdlepEQREKQIIETLRQVGLlPDHASYYPH-----------MLAPGQKQRLGLARALILR 167
|
170
....*....|....
gi 533869216 525 PTVLILDEATSALD 538
Cdd:PRK15112 168 PKVIIADEALASLD 181
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
383-592 |
1.05e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.40 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSwlRGQVVGFISQEPVLFGT---- 458
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDK--DGQLKVADKNQLRLLRTrltm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 -----------TIMENIrfgkLEASDEEVYTAAREANAHEFITSFPEGYN-TVVGERGTTLSGGQKQRLAIARALIKQPT 526
Cdd:PRK10619 97 vfqhfnlwshmTVLENV----MEAPIQVLGLSKQEARERAVKYLAKVGIDeRAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 527 VLILDEATSALD----AESERVVQEAldrASAGRTVLVIAHRLSTVR--GAHcIVVMADGRVWEAGTHEELL 592
Cdd:PRK10619 173 VLLFDEPTSALDpelvGEVLRIMQQL---AEEGKTMVVVTHEMGFARhvSSH-VIFLHQGKIEEEGAPEQLF 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
383-627 |
1.11e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.11 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVvMLDGR--------DLRTLdpswlrgqvvgFisQEPV 454
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTaplaeareDTRLM-----------F--QDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 LFG-TTIMENIRFGkLEASDEEvytAAREANAhefitsfPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 533
Cdd:PRK11247 92 LLPwKKVIDNVGLG-LKGQWRD---AALQALA-------AVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 534 TSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVrgahciVVMADgRVweagtheeLLKKGG-----LYAELIRRQA 606
Cdd:PRK11247 161 LGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSEA------VAMAD-RV--------LLIEEGkigldLTVDLPRPRR 225
|
250 260 270
....*....|....*....|....*....|..
gi 533869216 607 LDAPRTAA-----------PPPKKPEGPRSHQ 627
Cdd:PRK11247 226 RGSARLAEleaevlqrvmsRGESEPTRLRWAG 257
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
381-582 |
1.30e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.15 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL--ERfyDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGT 458
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLGVAYIPEDRLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 ----TIMENIrfgKLEASDEEVYT-------AAREANAHEFITSF---PEGYNTVVGergtTLSGGQKQRLAIARALIKQ 524
Cdd:COG3845 348 vpdmSVAENL---ILGRYRRPPFSrggfldrKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRD 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 533869216 525 PTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTVRgAHC--IVVMADGRV 582
Cdd:COG3845 421 PKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEIL-ALSdrIAVMYEGRI 480
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
384-582 |
2.37e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.36 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGQVVGFISQEPVLfGT----T 459
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRAKYIGRVFQDPMM-GTapsmT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 460 IMEN------------IRFGKleasdeevyTAAREANAHEFITSFPEGY----NTVVGergtTLSGGQKQRLAIARALIK 523
Cdd:COG1101 99 IEENlalayrrgkrrgLRRGL---------TKKRRELFRELLATLGLGLenrlDTKVG----LLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 524 QPTVLILDEATSALD---AE-----SERVVQEaldrasAGRTVLVIAHRLS-TVRGAHCIVVMADGRV 582
Cdd:COG1101 166 KPKLLLLDEHTAALDpktAAlvlelTEKIVEE------NNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
382-564 |
3.66e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.08 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 382 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFY--DPTAGVVMLDGRDlrtldpswlrgqvvgfISQEpvlfgTT 459
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ----------------FGRE-----AS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 460 IMENIrfGKLEASDE--EVYTAAREANAHEFITSFPEgyntvvgergttLSGGQKQRLAIARALIKQPTVLILDEATSAL 537
Cdd:COG2401 102 LIDAI--GRKGDFKDavELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180
....*....|....*....|....*....
gi 533869216 538 DAESERVVQEALDRAS--AGRTVLVIAHR 564
Cdd:COG2401 168 DRQTAKRVARNLQKLArrAGITLVVATHH 196
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
93-340 |
4.85e-16 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 79.03 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRL--TTDVQEFKSSfkLVISQGLR 170
Cdd:cd18570 48 LILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFndANKIREAISS--TTISLFLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 171 SCTQVAGcLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAME----Q 246
Cdd:cd18570 126 LLMVIIS-GIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEeqflK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 247 REEERYGAELEACRcraeELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVL 326
Cdd:cd18570 205 KIEKKFSKLLKKSF----KLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINL 280
|
250
....*....|....
gi 533869216 327 FGQVVRGLSAGARV 340
Cdd:cd18570 281 QPKIQEAKVAADRL 294
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
375-586 |
6.13e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.04 E-value: 6.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 375 SYPCRPGFEvlkDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLD--------------PSW 440
Cdd:PRK11701 15 LYGPRKGCR---DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseaerrrllrTEW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 441 lrgqvvGFISQEP-------VLFGTTIMEnirfgKLEASDEEVYTAAREANAH---------EFITSFPegyntvvgerg 504
Cdd:PRK11701 92 ------GFVHQHPrdglrmqVSAGGNIGE-----RLMAVGARHYGDIRATAGDwlerveidaARIDDLP----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 505 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAEservVQ-EALD--R---ASAGRTVLVIAHRLSTVR-GAHCIVVM 577
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQaRLLDllRglvRELGLAVVIVTHDLAVARlLAHRLLVM 225
|
....*....
gi 533869216 578 ADGRVWEAG 586
Cdd:PRK11701 226 KQGRVVESG 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
383-563 |
6.42e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.96 E-value: 6.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYD--PTA---GVVMLDGRDLRT--LDPSWLRGQVvGFISQEPVL 455
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSpdVDPIEVRREV-GMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 456 F-GTTIMENIRFG----KLEAS----DEEVYTAAREANAHEFITSFPEGYntvvgerGTTLSGGQKQRLAIARALIKQPT 526
Cdd:PRK14267 97 FpHLTIYDNVAIGvklnGLVKSkkelDERVEWALKKAALWDEVKDRLNDY-------PSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 533869216 527 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAH 563
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
379-562 |
7.43e-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: 76.24 E-value: 7.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 379 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWlrGQVVGFISQEPVLFGT 458
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 -TIMENIRFGK--LEASDEEVYTAAREANAHEFiTSFPEGYntvvgergttLSGGQKQRLAIARALIKQPTVLILDEATS 535
Cdd:TIGR01189 88 lSALENLHFWAaiHGGAQRTIEDALAAVGLTGF-EDLPAAQ----------LSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*..
gi 533869216 536 ALDAESERVVQEALdRASAGRTVLVIA 562
Cdd:TIGR01189 157 ALDKAGVALLAGLL-RAHLARGGIVLL 182
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
365-568 |
9.34e-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: 75.74 E-value: 9.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 365 GSVTFQNVCFSYPCRPGF-EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL-ERfydPTAGVV----MLDGrdlRTLDP 438
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKrQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR---KTAGVItgeiLING---RPLDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 439 SWLRgqVVGFISQEPVLFGT-TIMENIRFgkleasdeevytaarEANAhefitsfpegyntvvgeRGttLSGGQKQRLAI 517
Cdd:cd03232 76 NFQR--STGYVEQQDVHSPNlTVREALRF---------------SALL-----------------RG--LSVEQRKRLTI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 533869216 518 ARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV 568
Cdd:cd03232 120 GVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSAS 171
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
384-604 |
1.05e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.72 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdPSWLRGQVVGFISQEPVLFG-TTIME 462
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY-ASKEVARRIGLLAQNATTPGdITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 463 NIR---------FGKLEASDEEVYTAAREANahefitsfpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 533
Cdd:PRK10253 101 LVArgryphqplFTRWRKEDEEAVTKAMQAT----------GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 533869216 534 TSALDAESERVVQEALDRAS--AGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEELLKkgglyAELIRR 604
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNreKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT-----AELIER 239
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
83-563 |
1.39e-15 |
|
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: 79.84 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 83 MTESQNLSTHLLILYGVQGLLTF----GYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFk 158
Cdd:COG4615 40 LNATGAALARLLLLFAGLLVLLLlsrlASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 159 SSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVAtpalMGVGTLMGsglRKLSRQCQEQIARAMGVADEALGNVRT 238
Cdd:COG4615 119 SQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVL----LGLGVAGY---RLLVRRARRHLRRAREAEDRLFKHFRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 239 V----RAFAM-EQREEERYGAELEACRCRAEEL-GRGIALFqgLSNIAF-NCMVLGtlFIGGSLVAGQQLTGGDLmsfLV 311
Cdd:COG4615 192 LlegfKELKLnRRRRRAFFDEDLQPTAERYRDLrIRADTIF--ALANNWgNLLFFA--LIGLILFLLPALGWADP---AV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 312 ASQTVqrsmanLSVLF-----GQVVRGLSA--GARVfeymALN---------PCIPLSGGCCVPKEQLRG--SVTFQNVC 373
Cdd:COG4615 265 LSGFV------LVLLFlrgplSQLVGALPTlsRANV----ALRkieelelalAAAEPAAADAAAPPAPADfqTLELRGVT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 374 FSYPC---RPGFEVlKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGqvvgfis 450
Cdd:COG4615 335 YRYPGedgDEGFTL-GPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ------- 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 451 qepvLFgTTImenirFgkleaSD----EEVY---TAAREANAHEFITSFP-EGYNTVVGERGTT--LSGGQKQRLAIARA 520
Cdd:COG4615 407 ----LF-SAV-----F-----SDfhlfDRLLgldGEADPARARELLERLElDHKVSVEDGRFSTtdLSQGQRKRLALLVA 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 533869216 521 LIKQPTVLILDEATSALDAESERVVQEAL--DRASAGRTVLVIAH 563
Cdd:COG4615 472 LLEDRPILVFDEWAADQDPEFRRVFYTELlpELKARGKTVIAISH 516
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
384-563 |
1.71e-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: 76.16 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLERFYDpTAGVVMLDGRDLRtldpswlRGQV---VGFISQEPVLF 456
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPRK-------PDQFqkcVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 457 -GTTIMENIRFGKLEASDEEVYTAAREANAHefITSFPEGYNTVVG-ERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 534
Cdd:cd03234 94 pGLTVRETLTYTAILRLPRKSSDAIRKKRVE--DVLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|
gi 533869216 535 SALDAESERVVQEALDR-ASAGRTVLVIAH 563
Cdd:cd03234 172 SGLDSFTALNLVSTLSQlARRNRIVILTIH 201
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
388-594 |
1.96e-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: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 388 FTLTLPPGKIVALVGQSGGGKTTVASLLERFYDP----TAGVVMLDGRDLRTLDPSWLR---GQVVGFISQEP------- 453
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRkiiGREIAMIFQEPsscldps 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 454 VLFGTTIMENIRFGKLEASDEEVYTAAREANA----------HEFI-TSFPEgyntvvgergtTLSGGQKQRLAIARALI 522
Cdd:COG4170 106 AKIGDQLIEAIPSWTFKGKWWQRFKWRKKRAIellhrvgikdHKDImNSYPH-----------ELTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 523 KQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKK 594
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARlnQLQGTSILLISHDLESIsQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
384-584 |
2.20e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.97 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP---SWLRGQVVGFISQEPVLFGT-T 459
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAKHVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 460 IMENIRFGKLEASDEEvytAAREANAHEFITSFPegyntvVGER----GTTLSGGQKQRLAIARALIKQPTVLILDEATS 535
Cdd:PRK10584 105 ALENVELPALLRGESS---RQSRNGAKALLEQLG------LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 533869216 536 ALDAES-ERVVQE--ALDRASAGRTVLVIAHRLSTVRGAHCIVVMaDGRVWE 584
Cdd:PRK10584 176 NLDRQTgDKIADLlfSLNREHGTTLILVTHDLQLAARCDRRLRLV-NGQLQE 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
379-589 |
2.48e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 379 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLdpswLRGQVVGFISQE------ 452
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNLVAYVPQSeevdws 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 453 -PVLFGTTIMENiRFGKL------EASDEEVYTAAREAnahefiTSFPEGYNTVVGErgttLSGGQKQRLAIARALIKQP 525
Cdd:PRK15056 93 fPVLVEDVVMMG-RYGHMgwlrraKKRDRQIVTAALAR------VDMVEFRHRQIGE----LSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 526 TVLILDEATSALDAESE-RVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMADGRVWEAGTHE 589
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
367-611 |
5.77e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.93 E-value: 5.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSY-PCRP-GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAG------VVMLDGRDLRTLDP 438
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 439 swLRGQV-VGFISQEPVLFGTTIMENIRFG--KLEASDEEVYTAAreANAHEFITSFPEGYNTVVGErgttLSGGQKQRL 515
Cdd:PRK13643 82 --VRKKVgVVFQFPESQLFEETVLKDVAFGpqNFGIPKEKAEKIA--AEKLEMVGLADEFWEKSPFE----LSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 516 AIARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLK 593
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
250
....*....|....*...
gi 533869216 594 KgglyAELIRRQALDAPR 611
Cdd:PRK13643 234 E----VDFLKAHELGVPK 247
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
381-582 |
6.75e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.14 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS---WLRGQVvGFISQEP-VLF 456
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQI-GMIFQDHhLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 457 GTTIMENIRFGKL--EASDEE----VYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPTVLIL 530
Cdd:PRK10908 93 DRTVYDNVAIPLIiaGASGDDirrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 531 DEATSALD-AESERVVQ--EALDRasAGRTVLVIAHRLSTV-RGAHCIVVMADGRV 582
Cdd:PRK10908 162 DEPTGNLDdALSEGILRlfEEFNR--VGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
366-568 |
9.99e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.69 E-value: 9.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPCRpgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDpTAGVVMLDGR--------DLRTLD 437
Cdd:PRK14258 7 AIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqniYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 438 PSWLRGQVvGFISQEPVLFGTTIMENIRFG--------KLEAsDEEVYTAAREANAHEFITSfpegyntVVGERGTTLSG 509
Cdd:PRK14258 83 LNRLRRQV-SMVHPKPNLFPMSVYDNVAYGvkivgwrpKLEI-DDIVESALKDADLWDEIKH-------KIHKSALDLSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 533869216 510 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV 568
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 ... |
381-594 |
1.09e-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: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF--YDPTAGVVMLDgrdlRTLDPSWLRGQVVGFISQE-PVLFG 457
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYH----VALCEKCGYVERPSKVGEPcPVCGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 458 TTIMENIRFGKLeasDEEVYTAAREANAHEF----------------ITSFPE-GYN--------------TVVGERGT- 505
Cdd:TIGR03269 88 TLEPEEVDFWNL---SDKLRRRIRKRIAIMLqrtfalygddtvldnvLEALEEiGYEgkeavgravdliemVQLSHRITh 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 506 ---TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAsagrtvlVIAHRLSTVRGAHCIVVMAD--- 579
Cdd:TIGR03269 165 iarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEA-------VKASGISMVLTSHWPEVIEDlsd 237
|
250 260
....*....|....*....|..
gi 533869216 580 -------GRVWEAGTHEELLKK 594
Cdd:TIGR03269 238 kaiwlenGEIKEEGTPDEVVAV 259
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
380-591 |
1.45e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 380 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQE----PVL 455
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQElhlvPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 456 fgtTIMENIRFGKLEAS-----DEEVYTAAREANAHEFITSFPegyNTVVGErgttLSGGQKQRLAIARALIKQPTVLIL 530
Cdd:PRK11288 95 ---TVAENLYLGQLPHKggivnRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 531 DEATSALDA-ESE---RVVQEALDRasaGRTVLVIAHRLSTV-RGAHCIVVMADGRvwEAGTHEEL 591
Cdd:PRK11288 165 DEPTSSLSArEIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGR--YVATFDDM 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
383-582 |
2.62e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.83 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS--WLRGqvVGFIS----QEPVLF 456
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdaIRAG--IAYVPedrkGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 457 GTTIMENI---------RFGKLEASDEEvytaareANAHEFITSF---PEGYNTVVGergtTLSGGQKQRLAIARALIKQ 524
Cdd:COG1129 344 DLSIRENItlasldrlsRGGLLDRRRER-------ALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 533869216 525 PTVLILDEATSALD--AESE--RVVQEAldrASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 582
Cdd:COG1129 413 PKVLILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVISSELPELLGlSDRILVMREGRI 472
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
382-591 |
3.96e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.58 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 382 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSW--------------------- 440
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKekekvleklviqktrfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 441 ---LRGQV-VGFISQEPVLFGTTIMENIRFGKLE--ASDEEVYTAAREanaHEFITSFPEGYNtvvgERGT-TLSGGQKQ 513
Cdd:PRK13651 100 ikeIRRRVgVVFQFAEYQLFEQTIEKDIIFGPVSmgVSKEEAKKRAAK---YIELVGLDESYL----QRSPfELSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 514 RLAIARALIKQPTVLILDEATSALDAEServVQEALD----RASAGRTVLVIAHRLSTV--RGAHCIVVmADGR-VWEAG 586
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQG---VKEILEifdnLNKQGKTIILVTHDLDNVleWTKRTIFF-KDGKiIKDGD 248
|
....*
gi 533869216 587 THEEL 591
Cdd:PRK13651 249 TYDIL 253
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
383-617 |
5.68e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.74 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVA-SLLERFYDP----TAGVVMLDGRDLRTLDPSWLR---GQVVGFISQEPV 454
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRgvrGNKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 lfgttimenIRFGKLEASDEEVYTA-------AREANAHEFITSFPEgyntvVGERGTT---------LSGGQKQRLAIA 518
Cdd:PRK15134 103 ---------VSLNPLHTLEKQLYEVlslhrgmRREAARGEILNCLDR-----VGIRQAAkrltdyphqLSGGERQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 519 RALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLKKG 595
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAP 248
|
250 260
....*....|....*....|..
gi 533869216 596 glyAELIRRQALDAPRTAAPPP 617
Cdd:PRK15134 249 ---THPYTQKLLNSEPSGDPVP 267
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
381-592 |
5.96e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.85 E-value: 5.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRD--LRTLDPSWLRGqvVGFISQEPVLFGT 458
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisLLPLHARARRG--IGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 TIMENIRFGKLEASDEeVYTAAREANAHEFITSFPEGYntVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 538
Cdd:PRK10895 93 LSVYDNLMAVLQIRDD-LSAEQREDRANELMEEFHIEH--LRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 539 AES----ERVVQEALDRasaGRTVLVIAHRL-STVRGAHCIVVMADGRVWEAGTHEELL 592
Cdd:PRK10895 170 PISvidiKRIIEHLRDS---GLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
380-565 |
7.48e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 7.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 380 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFGT- 458
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 TIMENI--------RFGKLEASdeEVYtaaREANAHEFITSFPEGYNTVVGErgttLSGGQKQRLAIARALIKQPTVLIL 530
Cdd:PRK10762 95 TIAENIflgrefvnRFGRIDWK--KMY---AEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 533869216 531 DEATSAL-DAESE---RVVQEALDRasaGRTVLVIAHRL 565
Cdd:PRK10762 166 DEPTDALtDTETEslfRVIRELKSQ---GRGIVYISHRL 201
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
379-593 |
1.73e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 379 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVV----MLDGR------DLRTLDPSWL---RGQV 445
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkMLLRRrsrqviELSEQSAAQMrhvRGAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 VGFISQEPVL-------FGTTIMENIRFGKlEASDEEvytAAREANAHEFITSFPEGyNTVVGERGTTLSGGQKQRLAIA 518
Cdd:PRK10261 106 MAMIFQEPMTslnpvftVGEQIAESIRLHQ-GASREE---AMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 519 RALIKQPTVLILDEATSALDAESE-------RVVQEALDRAsagrtVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEE 590
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQ 255
|
...
gi 533869216 591 LLK 593
Cdd:PRK10261 256 IFH 258
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
383-610 |
2.16e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.81 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrTLDPSwLRG-----QVVGFISQEP--VL 455
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYS-KRGllalrQQVATVFQDPeqQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 456 FGTTIMENIRFG--KLEASDEEVYTAAREANahefitsfpegynTVVGERG------TTLSGGQKQRLAIARALIKQPTV 527
Cdd:PRK13638 91 FYTDIDSDIAFSlrNLGVPEAEITRRVDEAL-------------TLVDAQHfrhqpiQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 528 LILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLKKGglyaELIRRQ 605
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACT----EAMEQA 233
|
....*
gi 533869216 606 ALDAP 610
Cdd:PRK13638 234 GLTQP 238
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
387-591 |
2.35e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 71.68 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 387 DFTLTLPPGKIVALVGQSGGGKTTVA----SLLERfYDPTAGVVMLDGRDLRTLDPSWL---RGQVVGFISQEPVL---- 455
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAfalmGLLAA-NGRIGGSATFNGREILNLPEKELnklRAEQISMIFQDPMTslnp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 456 ---FGTTIMENI----RFGKLEASDEEV--YTAAREANAHEFITSFPEGYntvvgergttlSGGQKQRLAIARALIKQPT 526
Cdd:PRK09473 113 ymrVGEQLMEVLmlhkGMSKAEAFEESVrmLDAVKMPEARKRMKMYPHEF-----------SGGMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 527 VLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRGAhC--IVVMADGRVWEAGTHEEL 591
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLNelKREFNTAIIMITHDLGVVAGI-CdkVLVMYAGRTMEYGNARDV 249
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
384-592 |
2.39e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 71.37 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrtldPSWLR------GQVVGFISQEPVLfg 457
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARharqrvGVVPQFDNLDPDF-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 458 tTIMENIR-FGKleasdeevYTAAREANAHEFITSFPE------GYNTVVGErgttLSGGQKQRLAIARALIKQPTVLIL 530
Cdd:PRK13537 96 -TVRENLLvFGR--------YFGLSAAAARALVPPLLEfaklenKADAKVGE----LSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 533869216 531 DEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELL 592
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
386-591 |
2.43e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.50 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 386 KDFTLTLPPGKIVALVGQSGGGKT-TVASLLERF---YDPTAGVVMLDGRdlrTLDPSWLRGQVVGFISQEP-------V 454
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGK---PVAPCALRGRKIATIMQNPrsafnplH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 LFGTTIMENIR-FGKLeaSDEEVYTAAREA----NAHEFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPTVLI 529
Cdd:PRK10418 97 TMHTHARETCLaLGKP--ADDATLTAALEAvgleNAARVLKLYP-----------FEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 530 LDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEEL 591
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
368-563 |
2.61e-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: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 368 TFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLerfydptAGVvmldgrDLRTLDPSWLR-GQVV 446
Cdd:TIGR03719 6 TMNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGV------DKDFNGEARPQpGIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVLFGT-TIMENIRFGKLEASD-----EEVYTAARE---------------------ANAHEFITSF------- 492
Cdd:TIGR03719 71 GYLPQEPQLDPTkTVRENVEEGVAEIKDaldrfNEISAKYAEpdadfdklaaeqaelqeiidaADAWDLDSQLeiamdal 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 493 --PEGYNTVvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES----ERVVQEaldraSAGrTVLVIAH 563
Cdd:TIGR03719 151 rcPPWDADV-----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE-----YPG-TVVAVTH 216
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
379-582 |
3.18e-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: 68.83 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 379 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLERFYDPTaGVVMLDGRDLRTlDPSWLRGQVVgFISQEPV 454
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKE-FAEKYPGEII-YVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 LFGT-TIMENIRFgkleasdeevytaAREANAHEFItsfpegyntvvgeRGttLSGGQKQRLAIARALIKQPTVLILDEA 533
Cdd:cd03233 94 HFPTlTVRETLDF-------------ALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 534 TSALDAEServvqeALDRASAGRTvlvIAHRLSTVRGAHC-------------IVVMADGRV 582
Cdd:cd03233 146 TRGLDSST------ALEILKCIRT---MADVLKTTTFVSLyqasdeiydlfdkVLVLYEGRQ 198
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
367-568 |
4.81e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRpgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswLRgqvV 446
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR---I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVLFGTTIMENIRFGKLE--ASDEEVYTAAREANAHEFItSFPEgyntvvgergTTLSGGQKQRLAIARALIKQ 524
Cdd:PRK09544 70 GYVPQKLYLDTTLPLTVNRFLRLRpgTKKEDILPALKRVQAGHLI-DAPM----------QKLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 533869216 525 PTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV 568
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDLHLV 184
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
380-581 |
5.26e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.50 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 380 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYdPTA---GVVMLDGRDLR--TLDPSWLRGQVVgfISQEPV 454
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQasNIRDTERAGIAI--IHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 LF-GTTIMENI-------RFGKLEasDEEVYTAAREANAHEFITSFPegyNTVVGErgttLSGGQKQRLAIARALIKQPT 526
Cdd:PRK13549 93 LVkELSVLENIflgneitPGGIMD--YDAMYLRAQKLLAQLKLDINP---ATPVGN----LGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 527 VLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTVRG-AHCIVVMADGR 581
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIrDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
360-568 |
6.72e-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: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 360 KEQLRGSVTF--QNVCFSYPCRPGFEV-LKDFTLTLPPGKIVALVGQSGGGKTTVASLL-ERFydpTAGVVMLDGR--DL 433
Cdd:TIGR00956 751 MEKESGEDIFhwRNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERV---TTGVITGGDRlvNG 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 434 RTLDPSWLRgqVVGFISQEPVLFGT-TIMENIRFGKL-----EASDEEVYTAAREANAHEFITSFPEGyntVVGERGTTL 507
Cdd:TIGR00956 828 RPLDSSFQR--SIGYVQQQDLHLPTsTVRESLRFSAYlrqpkSVSKSEKMEYVEEVIKLLEMESYADA---VVGVPGEGL 902
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 533869216 508 SGGQKQRLAIARALIKQPTVLI-LDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV 568
Cdd:TIGR00956 903 NVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSAI 965
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
51-306 |
7.09e-13 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 69.45 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 51 LGAALVNVQIPLLLGQLVevvakytrDHVGSFMTESQNLSTHLLILYGVQGLLT--FGYL--VLLSHVGERMAVDMRRAL 126
Cdd:cd18582 6 VLAKLLNVAVPFLLKYAV--------DALSAPASALLAVPLLLLLAYGLARILSslFNELrdALFARVSQRAVRRLALRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 127 FSSLLRQDITFFDANKTGQLVSrlttdvqefkssfklVISQGLRSCTQVAG------------CLVSLSMLSTRLTL--- 191
Cdd:cd18582 78 FRHLHSLSLRFHLSRKTGALSR---------------AIERGTRGIEFLLRfllfnilptileLLLVCGILWYLYGWsya 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 192 LLMVATPALMGVGTLMGSGLR-KLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGI 270
Cdd:cd18582 143 LITLVTVALYVAFTIKVTEWRtKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSL 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 533869216 271 ALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDL 306
Cdd:cd18582 223 ALLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDF 258
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
382-581 |
8.47e-13 |
|
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: 8.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 382 FEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLERFYDPTAGVVMLDGRDLRTLDPSwLRGQVVgFISQEPVLFG 457
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKH-YRGDVV-YNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 458 T-TIMENIRFG--------KLEASDEEVYtAAREANAHEFITSFPEGYNTVVGE---RGttLSGGQKQRLAIARALIKQP 525
Cdd:TIGR00956 152 HlTVGETLDFAarcktpqnRPDGVSREEY-AKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 526 TVLILDEATSALDAEServvqeALDRASAGRTVLVIAHRLSTVRGAHC----------IVVMADGR 581
Cdd:TIGR00956 229 KIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVAIYQCsqdayelfdkVIVLYEGY 288
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
87-326 |
8.91e-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: 69.13 E-value: 8.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 87 QNLSTHLLILYGVQGLLTFGYLV------LLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRL--TTDVQEF- 157
Cdd:cd18568 36 KNISLLNLILIGLLIVGIFQILLsavrqyLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFqeNQKIRRFl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 158 -KSSFKLVisqgLRSCTQVAgCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNV 236
Cdd:cd18568 116 tRSALTTI----LDLLMVFI-YLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 237 RTVRAFAMEQ----REEERYGAELEAcRCRAEELGRGIALFQGLSNIAFNCMVlgtLFIGGSLVAGQQLTGGDLMSFLVA 312
Cdd:cd18568 191 ATIKALAAERpirwRWENKFAKALNT-RFRGQKLSIVLQLISSLINHLGTIAV---LWYGAYLVISGQLTIGQLVAFNML 266
|
250
....*....|....
gi 533869216 313 SQTVQRSMANLSVL 326
Cdd:cd18568 267 FGSVINPLLALVGL 280
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
383-582 |
1.17e-12 |
|
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: 68.13 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLR--GQVVGFISQE----PVLF 456
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRriGVVFGQKTQLwwdlPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 457 GTTIMENI------RFGKL--EASD-----EEVYTAAREanahefitsfpegyntvvgergttLSGGQKQRLAIARALIK 523
Cdd:cd03267 115 SFYLLAAIydlppaRFKKRldELSElldleELLDTPVRQ------------------------LSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 524 QPTVLILDEATSALDAESERVVQEALDRASAGR--TVLVIAHRLSTV-RGAHCIVVMADGRV 582
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRL 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
379-615 |
1.28e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 379 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT-VASLLERFYDPTA-------GVVMLDGRDLRTLDPSWL-RGQVV--- 446
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTlLKALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLaRLRAVlpq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 ------GFISQEPVLFGtTIMENIRFGKLEASDEEVYTAAREAnahefitsfpEGYNTVVGERGTTLSGGQKQRLAIARA 520
Cdd:PRK13547 91 aaqpafAFSAREIVLLG-RYPHARRAGALTHRDGEIAWQALAL----------AGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 521 L---------IKQPTVLILDEATSALD-AESERVVQEALDRASAGRT-VLVIAHRLS-TVRGAHCIVVMADGRVWEAGTH 588
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGAP 239
|
250 260 270
....*....|....*....|....*....|...
gi 533869216 589 EELLKkgglyAELIRR------QALDAPRTAAP 615
Cdd:PRK13547 240 ADVLT-----PAHIARcygfavRLVDAGDGVPP 267
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
383-537 |
1.47e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFG-TTIM 461
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSrMTVE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 462 ENIRFGKLEASDEEVYTaaREANAHEFitsFPEGYNTVVgERGTTLSGGQKQRLAIARALIKQPTVLILDEATSAL 537
Cdd:PRK11614 99 ENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
379-563 |
2.04e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 379 RPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLErfydPTAGVVMLDGRDLRTLDPswlrGQVVGFISQ--- 451
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTllrlIAGLLP----PAAGTIKLDGGDIDDPDV----AEACHYLGHrna 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 452 -EPVLfgtTIMENIRF-GKLEASDEEVYTAAREANAHEFITSFPEGYntvvgergttLSGGQKQRLAIARALIKQPTVLI 529
Cdd:PRK13539 84 mKPAL---TVAENLEFwAAFLGGEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*
gi 533869216 530 LDEATSALDAESERVVQEAL-DRASAGRTVLVIAH 563
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIrAHLAQGGIVIAATH 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
359-590 |
3.72e-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: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 359 PKEQLRGSVT-FQNVCFSYPCRPGFEvlkDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML--------- 428
Cdd:TIGR03719 314 PGPRLGDKVIeAENLTKAFGDKLLID---DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayv 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 429 -DGRDlrTLDPS---WlrgqvvgfisqEPVLFGTTImenIRFGKleasdeevytaaREANAHEFITSFpegyN------- 497
Cdd:TIGR03719 391 dQSRD--ALDPNktvW-----------EEISGGLDI---IKLGK------------REIPSRAYVGRF----Nfkgsdqq 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 498 TVVGErgttLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDrASAGrTVLVIAH------RLSTvrga 571
Cdd:TIGR03719 439 KKVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL-NFAG-CAVVISHdrwfldRIAT---- 508
|
250 260
....*....|....*....|
gi 533869216 572 HCIVVMADGRV-WEAGTHEE 590
Cdd:TIGR03719 509 HILAFEGDSHVeWFEGNFSE 528
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
384-581 |
3.82e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.14 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLE-RFYDPT-AGVVMLDGRDLRTldPSWLRgqvVGFISQEPVLF-GTTI 460
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTK--QILKR---TGFVTQDDILYpHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 461 MENIRFGKL----EASDEEVYTAAREANAHEFITSFPEgyNTVVGE---RGttLSGGQKQRLAIARALIKQPTVLILDEA 533
Cdd:PLN03211 158 RETLVFCSLlrlpKSLTKQEKILVAESVISELGLTKCE--NTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 533869216 534 TSALDAESE-RVVQEALDRASAGRTVLVIAHRLST--VRGAHCIVVMADGR 581
Cdd:PLN03211 234 TSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
369-584 |
7.81e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 7.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 369 FQNVCFSYPcRPGFEVlKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRGqvvgf 448
Cdd:PRK10522 325 LRNVTFAYQ-DNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK----- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 449 isqepvLFGTTIMENIRFGKL-----EASDEEVYTA--AREANAHEFitsfpegynTVVGERGTT--LSGGQKQRLAIAR 519
Cdd:PRK10522 398 ------LFSAVFTDFHLFDQLlgpegKPANPALVEKwlERLKMAHKL---------ELEDGRISNlkLSKGQKKRLALLL 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 520 ALIKQPTVLILDEATSALDAESERVV-QEALDRASA-GRTVLVIAHRLSTVRGAHCIVVMADGRVWE 584
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
383-605 |
8.01e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.58 E-value: 8.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLL--ERFYDPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPV------ 454
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVeipgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 --LFGTTIMENIR-FGKLEASDEEVYTAAREANAHefITSFPEGYNTVVGERGttLSGGQKQRLAIARALIKQPTVLILD 531
Cdd:PRK09580 95 nqFFLQTALNAVRsYRGQEPLDRFDFQDLMEEKIA--LLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 532 EATSALDAESERVVQEALDRASAG-RTVLVIAHR---LSTVRGAHcIVVMADGRVWEAGTH---EELLKKGglYAELIRR 604
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHYqriLDYIKPDY-VHVLYQGRIVKSGDFtlvKQLEEQG--YGWLTEQ 247
|
.
gi 533869216 605 Q 605
Cdd:PRK09580 248 Q 248
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
387-590 |
1.26e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.44 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 387 DFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDL-----RTLDPSWLRGqvVGFISQEPVLF-GTTI 460
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekGICLPPEKRR--IGYVFQDARLFpHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 461 MENIRFGKLEASDEE----VYTAAREAnaheFITSFPegyntvvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSA 536
Cdd:PRK11144 94 RGNLRYGMAKSMVAQfdkiVALLGIEP----LLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 537 LDAESERVVQEALDRASagRTV----LVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEE 590
Cdd:PRK11144 159 LDLPRKRELLPYLERLA--REInipiLYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
382-595 |
1.69e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.66 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 382 FEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERF--YDPTAGVVMLDGRDLRTLDPSwLRGQVVGFIS-QEPV-LFG 457
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIFLAfQYPIeIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 458 TTimeNIRFGKLEASDEEVYTAAREANAHEFITSFPEGYNtVVGERGTTL--------SGGQKQRLAIARALIKQPTVLI 529
Cdd:CHL00131 99 VS---NADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 530 LDEATSALDAESERVVQEALDR-ASAGRTVLVIAH--RLSTVRGAHCIVVMADGRVWEAGTHE---ELLKKG 595
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElakELEKKG 246
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
366-581 |
1.99e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.62 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLrtldPSWLR--- 442
Cdd:PRK13536 41 AIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARlar 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 443 ---GQVVGFISQEPVLfgtTIMENI----RFGKLEASDEEvytaareanahEFITSFPE--GYNTVVGERGTTLSGGQKQ 513
Cdd:PRK13536 114 ariGVVPQFDNLDLEF---TVRENLlvfgRYFGMSTREIE-----------AVIPSLLEfaRLESKADARVSDLSGGMKR 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 514 RLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAH----------RLSTVRGAHCIvvmADGR 581
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHfmeeaerlcdRLCVLEAGRKI---AEGR 255
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
381-581 |
2.19e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.39 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 381 GFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFY--DPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLF-G 457
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTERAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 458 TTIMENIRFG-KLEASDEEVYTAAREANAHEFI--TSFPEGYNT-VVGERGttlsGGQKQRLAIARALIKQPTVLILDEA 533
Cdd:TIGR02633 93 LSVAENIFLGnEITLPGGRMAYNAMYLRAKNLLreLQLDADNVTrPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 533869216 534 TSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRgAHC--IVVMADGR 581
Cdd:TIGR02633 169 SSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVK-AVCdtICVIRDGQ 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
395-593 |
2.45e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 65.15 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 395 GKIVALVGQSGGGKTtVASLLERFYDPTAGVVM-----LDGRDLRTLDPSWLR---GQVVGFISQEPVL-------FGTT 459
Cdd:PRK11022 33 GEVVGIVGESGSGKS-VSSLAIMGLIDYPGRVMaekleFNGQDLQRISEKERRnlvGAEVAMIFQDPMTslnpcytVGFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 460 IMENIRFGKLEASdeevytAAREANAHEFITSF----PEGYNTVVGERgttLSGGQKQRLAIARALIKQPTVLILDEATS 535
Cdd:PRK11022 112 IMEAIKVHQGGNK------KTRRQRAIDLLNQVgipdPASRLDVYPHQ---LSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 533869216 536 ALDAESE-RVVQEALDRASAGRTVLV-IAHRLSTV-RGAHCIVVMADGRVWEAGTHEELLK 593
Cdd:PRK11022 183 ALDVTIQaQIIELLLELQQKENMALVlITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
93-309 |
2.83e-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: 64.91 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLttdvQEFKSSFKLVISQGLRSC 172
Cdd:cd18566 48 VVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL----NSLEQIREFLTGQALLAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 173 TQVAGCLVSLSM---LSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREE 249
Cdd:cd18566 124 LDLPFVLIFLGLiwyLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQML 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 250 ERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSF 309
Cdd:cd18566 204 RRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIAC 263
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
394-571 |
3.48e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 61.62 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 394 PGKIVALVGQSGGGKTTVASLLERFYDPT-AGVVMLDGRDLRTLDPSWLRgqvvgfisqepvlfgttimenirfgkleas 472
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 473 deevytaareanahefitsfpegyNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD-- 550
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180
....*....|....*....|....*.
gi 533869216 551 -----RASAGRTVLVIAHRLSTVRGA 571
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPA 132
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
63-309 |
3.64e-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: 64.45 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 63 LLGQLVEVVAKYTRDHVgsFMTESQNLSTHLLI----LYGVQGLLTF--GYLVLlsHVGERMAVDMRRALFSSLLRQDIT 136
Cdd:cd18555 16 LLTLLIPILTQYVIDNV--IVPGNLNLLNVLGIgiliLFLLYGLFSFlrGYIII--KLQTKLDKSLMSDFFEHLLKLPYS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 137 FFDANKTGQLVSRLT--TDVQEFKSSfkLVISqGLRSCTQVAGCLVSLSMLSTRLTLLLMVATpALMGVGTLMGSG-LRK 213
Cdd:cd18555 92 FFENRSSGDLLFRANsnVYIRQILSN--QVIS-LIIDLLLLVIYLIYMLYYSPLLTLIVLLLG-LLIVLLLLLTRKkIKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 214 LSRQCQEQIARAMGVADEALGNVRTVRAFAMEQRE----EERYGAELEAcrcrAEELGRGIALFQGLSNIAFNCMVLGTL 289
Cdd:cd18555 168 LNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIykkwENLFKKQLKA----FKKKERLSNILNSISSSIQFIAPLLIL 243
|
250 260
....*....|....*....|
gi 533869216 290 FIGGSLVAGQQLTGGDLMSF 309
Cdd:cd18555 244 WIGAYLVINGELTLGELIAF 263
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
385-575 |
6.15e-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: 63.40 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTLTLPPGKIVALVGQSGGGKTT---------VASLLERFYDPTAGVVMLDGrdLRTLDpswlrgQVVgFISQEPVl 455
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSlindtlypaLARRLHLKKEQPGNHDRIEG--LEHID------KVI-VIDQSPI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 456 fGTT----------IMENIR--F-------------------GK-----LEASDEEvytaareanAHEFITSFPE----- 494
Cdd:cd03271 81 -GRTprsnpatytgVFDEIRelFcevckgkrynretlevrykGKsiadvLDMTVEE---------ALEFFENIPKiarkl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 495 --------GYNTVvGERGTTLSGGQKQRLAIARALIKQ---PTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIA 562
Cdd:cd03271 151 qtlcdvglGYIKL-GQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIE 229
|
250
....*....|...
gi 533869216 563 HRLSTVRGAHCIV 575
Cdd:cd03271 230 HNLDVIKCADWII 242
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
49-310 |
6.69e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 63.65 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 49 LALGAALVNVQIPLLlgqlvevvAKYTRDHvgsFMTES--QNLsTHLLILYG----VQGLLTFGYLVLLSHVGERMAVDM 122
Cdd:cd18540 10 LMLLVALLDAVFPLL--------TKYAIDH---FITPGtlDGL-TGFILLYLglilIQALSVFLFIRLAGKIEMGVSYDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 123 RRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMG 202
Cdd:cd18540 78 RKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 203 VGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALF----QGLSN 278
Cdd:cd18540 158 VSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFlpivLFLGS 237
|
250 260 270
....*....|....*....|....*....|..
gi 533869216 279 IAfncmVLGTLFIGGSLVAGQQLTGGDLMSFL 310
Cdd:cd18540 238 IA----TALVLWYGGILVLAGAITIGTLVAFI 265
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
380-584 |
7.46e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 7.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 380 PGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYdPTA---GVVMLDG--RDLRTLDPSWLRGQVVgfISQE-- 452
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGevCRFKDIRDSEALGIVI--IHQEla 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 453 --PVLfgtTIMENIRFGKLEASD-----EEVYTAAREANAHEFITSFPEgynTVVGERGTtlsgGQKQRLAIARALIKQP 525
Cdd:NF040905 89 liPYL---SIAENIFLGNERAKRgvidwNETNRRARELLAKVGLDESPD---TLVTDIGV----GKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 533869216 526 TVLILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWE 584
Cdd:NF040905 159 KLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
367-591 |
8.98e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.86 E-value: 8.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPGFEvlkDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLRG--Q 444
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFD---NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 445 VVGFISQEPVLF-GTTIMENIRFGKLEasdeevYTAAREANAHEFITSFPEGyntvVGERG------TTLSGGQKQRLAI 517
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAYPLRE------HTQLPAPLLHSTVMMKLEA----VGLRGaaklmpSELSGGMARRAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 518 ARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEEL 591
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISElnSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
385-563 |
1.56e-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: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTLTLPPGKI-----VALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRdlrtldpswlrgqvvgfISQEPvlfgtt 459
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-----------------ISYKP------ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 460 imenirfGKLEA-SDEEVYTAAREANAHEFITSFpegYNTVVGER----------GTTLSGGQKQRLAIARALIKQPTVL 528
Cdd:COG1245 408 -------QYISPdYDGTVEEFLRSANTDDFGSSY---YKTEIIKPlgleklldknVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190
....*....|....*....|....*....|....*...
gi 533869216 529 ILDEATSALDAEsERV-VQEALDR--ASAGRTVLVIAH 563
Cdd:COG1245 478 LLDEPSAHLDVE-QRLaVAKAIRRfaENRGKTAMVVDH 514
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
365-563 |
1.72e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 365 GSVTF--QNVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLdGRDLR-------- 434
Cdd:PRK11147 316 GKIVFemENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEvayfdqhr 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 435 -TLDPSwlrgqvvgfisqepvlfgTTIMENIRFGKleasdEEVYTAAREANAHEFITSF---PEGYNTVVgergTTLSGG 510
Cdd:PRK11147 392 aELDPE------------------KTVMDNLAEGK-----QEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGG 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 533869216 511 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAgrTVLVIAH 563
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; ... |
93-317 |
1.96e-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: 62.13 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRlttdVQEFKSSFKLVISQGLRSC 172
Cdd:cd18588 48 LLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVAR----VRELESIRQFLTGSALTLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 173 TQVAGCLVSLSML---STRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREE 249
Cdd:cd18588 124 LDLVFSVVFLAVMfyySPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQ 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 250 ERYGAELeacrcrAEELGRGIALfQGLSNIAFN-------CMVLGTLFIGGSLVAGQQLTGGDLMSF-LVASQTVQ 317
Cdd:cd18588 204 RRWEELL------ARYVKASFKT-ANLSNLASQivqliqkLTTLAILWFGAYLVMDGELTIGQLIAFnMLAGQVSQ 272
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
379-563 |
2.62e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 379 RPGFEVLkDFTLTlpPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLR-----GQVVGFisqEP 453
Cdd:PRK13538 14 RILFSGL-SFTLN--AGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdllylGHQPGI---KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 454 VLfgtTIMENIRF-GKL--EASDEevytAAREANAHefitsfpegyntvVGERGT------TLSGGQKQRLAIARALIKQ 524
Cdd:PRK13538 88 EL---TALENLRFyQRLhgPGDDE----ALWEALAQ-------------VGLAGFedvpvrQLSAGQQRRVALARLWLTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 533869216 525 PTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAH 563
Cdd:PRK13538 148 APLWILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
366-539 |
3.30e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.17 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 366 SVTFQNVCFSYPcrPGFEVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLlERFydpTAGVVMLDGRDLRTLDPSwL 441
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTllrmVAGL-ERI---TSGEIWIGGRVVNELEPA-D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 442 RGQVVGFisQEPVLF-GTTIMENI-------RFGKLEAsDEEVYTAAREANAHEFITSFPEgyntvvgergtTLSGGQKQ 513
Cdd:PRK11650 76 RDIAMVF--QNYALYpHMSVRENMayglkirGMPKAEI-EERVAEAARILELEPLLDRKPR-----------ELSGGQRQ 141
|
170 180
....*....|....*....|....*.
gi 533869216 514 RLAIARALIKQPTVLILDEATSALDA 539
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
388-608 |
4.73e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 388 FTLTLPPGKIVALVGQSGGGKTT----VASLLerfydPTAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPVLFgttIMEN 463
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTllarMAGLL-----PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPF---AMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 464 IRFGKLEASDEeVYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQR-------LAIARALIKQPTVLILDEATSA 536
Cdd:PRK03695 87 FQYLTLHQPDK-TRTEAVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 537 LDaeserVVQE-ALDR-----ASAGRTVLVIAHRLS-TVRGAHCIVVMADGRVWEAGTHEELLKKGGL---YAELIRRQA 606
Cdd:PRK03695 164 LD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENLaqvFGVNFRRLD 238
|
..
gi 533869216 607 LD 608
Cdd:PRK03695 239 VE 240
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
389-592 |
7.02e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.97 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 389 TLTLPPGKIVALVGQSGGGKTTVASLL----ERFYDPTAGVVMLDGRDLRTLDPSWLR---GQVVGFISQEP-------V 454
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRklvGHNVSMIFQEPqscldpsE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 LFGTTIMENI-----------RFGKLEASDEEVYTAAREANAHEFITSFPegyntvvgergTTLSGGQKQRLAIARALIK 523
Cdd:PRK15093 107 RVGRQLMQNIpgwtykgrwwqRFGWRKRRAIELLHRVGIKDHKDAMRSFP-----------YELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 524 QPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RGAHCIVVMADGRVWEAGTHEELL 592
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRlnQNNNTTILLISHDLQMLsQWADKINVLYCGQTVETAPSKELV 247
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
93-324 |
7.14e-10 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 60.68 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRL--TTDVQEFkssfklVISQGLR 170
Cdd:cd18782 48 MLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIseLDTIRGF------LTGTALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 171 SCTQVA---GCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAME-- 245
Cdd:cd18782 122 TLLDVLfsvIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAElk 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 246 --QREEERYGAELEAcrcrAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANL 323
Cdd:cd18782 202 arWRWQNRYARSLGE----GFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRL 277
|
.
gi 533869216 324 S 324
Cdd:cd18782 278 S 278
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
385-592 |
1.53e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPS-WLRGQVVgFISQEP----VLFGTT 459
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIV-YISEDRkrdgLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 460 IMENI----------RFGKLEASDEevytaaREAnAHEFITSF----PeGYNTVVGErgttLSGGQKQRLAIARALIKQP 525
Cdd:PRK10762 347 VKENMsltalryfsrAGGSLKHADE------QQA-VSDFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 533869216 526 TVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRG-AHCIVVMADGRV-----WEAGTHEELL 592
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
380-563 |
2.32e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 380 PGFEVLKDFTLTLPPG-KIvALVGQSGGGKTTVASLLerfydptAGVvmldgrdlrtlDPS-----WLR-GQVVGFISQE 452
Cdd:PRK11819 18 PKKQILKDISLSFFPGaKI-GVLGLNGAGKSTLLRIM-------AGV-----------DKEfegeaRPApGIKVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 453 PVLFGT-TIMENIRFGKLEASD-----EEVY------------TAAREA---------NAHEfITS----------FPEG 495
Cdd:PRK11819 79 PQLDPEkTVRENVEEGVAEVKAaldrfNEIYaayaepdadfdaLAAEQGelqeiidaaDAWD-LDSqleiamdalrCPPW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 496 YNTVvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES----ERVVQEaldraSAGrTVLVIAH 563
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 ... |
485-591 |
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 533869216 485 AHEFITSFPE-------------GYNTVvGERGTTLSGGQKQRLAIARALIKQ---PTVLILDEATSALDAESERVVQEA 548
Cdd:TIGR00630 796 AYEFFEAVPSisrklqtlcdvglGYIRL-GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEV 874
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 533869216 549 LDR-ASAGRTVLVIAHRLSTVRGAHCIVVM------ADGRVWEAGTHEEL 591
Cdd:TIGR00630 875 LQRlVDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
55-340 |
5.63e-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: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 55 LVNVQIPLLLGQLVevvaKYTRDHV--GSFMTESQNLStHLLILYGVQGLLtfgYLVL----------LSH-VGERMAVD 121
Cdd:cd18554 9 LVRFGIPLLLPLIL----KYIVDDViqGSSLTLDEKVY-KLFTIIGIMFFI---FLILrppveyyrqyFAQwIANKILYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 122 MRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALM 201
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 202 GVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAF 281
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTIT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 533869216 282 NCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSAGARV 340
Cdd:cd18554 241 DLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
385-596 |
7.05e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.98 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTLTLPPGKIVALVGQSGGGKTTVASLLerfydptAGV-------VMLDGRDLRtlDPSWlRGQVVGFISQEPV--- 454
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGArkiqqgrVEVLGGDMA--DARH-RRAVCPRIAYMPQglg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 --LFGT-TIMENIRF-GKLEASDEevytAAREANAHEFITS-----FPE---GyntvvgergtTLSGGQKQRLAIARALI 522
Cdd:NF033858 87 knLYPTlSVFENLDFfGRLFGQDA----AERRRRIDELLRAtglapFADrpaG----------KLSGGMKQKLGLCCALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 523 KQPTVLILDEATSALDAESERVVQEALDRASAGR---TVLViahrlSTV------RGAHCiVVMADGRVWEAGTHEELLK 593
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLV-----ATAymeeaeRFDWL-VAMDAGRVLATGTPAELLA 226
|
...
gi 533869216 594 KGG 596
Cdd:NF033858 227 RTG 229
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
385-563 |
8.04e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 56.65 E-value: 8.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTLTLPPG-----KIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDlrtldpswlrgqvVGFISQEPVLFGTT 459
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-------------VSYKPQYIKADYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 460 IMENIRFGKLEASDEEVYTAAREANahefitsfPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDA 539
Cdd:cd03237 77 TVRDLLSSITKDFYTHPYFKTEIAK--------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180
....*....|....*....|....*.
gi 533869216 540 ESERVVQEALDR--ASAGRTVLVIAH 563
Cdd:cd03237 149 EQRLMASKVIRRfaENNEKTAFVVEH 174
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
383-596 |
1.48e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.32 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERfyDPTAGVVMLDGRdlrtldpswlrgqVVGFISQEPV---LFGTT 459
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-------------ISGFPKKQETfarISGYC 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 460 IMENIRFGKLEASDEEVYTA----AREANAHE---FITSFPEGY------NTVVGERGTT-LSGGQKQRLAIARALIKQP 525
Cdd:PLN03140 959 EQNDIHSPQVTVRESLIYSAflrlPKEVSKEEkmmFVDEVMELVeldnlkDAIVGLPGVTgLSTEQRKRLTIAVELVANP 1038
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 526 TVLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTvrgahcivvmadgRVWEAGTHEELLKKGG 596
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI-------------DIFEAFDELLLMKRGG 1097
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
364-597 |
1.52e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.59 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 364 RGSVTFQNVCFSYPCRPGFevlKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVmldgrdlrtldpSWLRG 443
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLF---KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSEN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 444 QVVGFISQEPVL-F--GTTIMENIRFGKLEASDEEVYtaareanahefitsfpegyntvvgeRGT--------------- 505
Cdd:PRK15064 382 ANIGYYAQDHAYdFenDLTLFDWMSQWRQEGDDEQAV-------------------------RGTlgrllfsqddikksv 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 506 -TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAgrTVLVIAH------RLSTvrgaHCIVVMA 578
Cdd:PRK15064 437 kVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSHdrefvsSLAT----RIIEITP 510
|
250
....*....|....*....
gi 533869216 579 DGRVWEAGTHEELLKKGGL 597
Cdd:PRK15064 511 DGVVDFSGTYEEYLRSQGI 529
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
385-563 |
1.67e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTLTLPPGKI-----VALVGQSGGGKTTVASLLERFYDPTAGVVMLDgrdlrtLD----PSWLR----GQVVGFISQ 451
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKisykPQYIKpdydGTVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 452 EPVLFGTTIMEnirfgkleasdeevytaareanaHEFItsFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILD 531
Cdd:PRK13409 424 ITDDLGSSYYK-----------------------SEII--KPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLD 478
|
170 180 190
....*....|....*....|....*....|....
gi 533869216 532 EATSALDAESERVVQEALDRASAGR--TVLVIAH 563
Cdd:PRK13409 479 EPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
367-563 |
5.16e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYpcrpGFEVL-KDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML----------DGRDlrT 435
Cdd:PRK11819 325 IEAENLSKSF----GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvklayvdQSRD--A 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 436 LDPSwlrgqvvgfisqepvlfgTTIMENIrfgkleaSD--EEVYTAAREANAHEFITSFpegyntvvGERGT-------T 506
Cdd:PRK11819 399 LDPN------------------KTVWEEI-------SGglDIIKVGNREIPSRAYVGRF--------NFKGGdqqkkvgV 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 533869216 507 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDrASAGrTVLVIAH 563
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL-EFPG-CAVVISH 500
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
383-582 |
6.23e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP-----------------------S 439
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlarglvylpedrqssglyldA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 440 WLRGQVVGFISQEPVLFGTTIMENIRFgkleasdeevytaareanahefitsfpEGYNTVVGERGT-------TLSGGQK 512
Cdd:PRK15439 357 PLAWNVCALTHNRRGFWIKPARENAVL---------------------------ERYRRALNIKFNhaeqaarTLSGGNQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 533869216 513 QRLAIARALIKQPTVLILDEATSALDAeSER--VVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 582
Cdd:PRK15439 410 QKVLIAKCLEASPQLLIVDEPTRGVDV-SARndIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
385-580 |
6.48e-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: 52.71 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTLTLPPGKIVALVGQSGGGKTTVasLLERFYdpTAGVVMLDGrDLRTLDPSWLrgqvvgfisqepvlfgttimenI 464
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLIS-FLPKFSRNKL----------------------I 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 465 RFGKLEasdeevytaareanaheFITSFPEGYNTVvGERGTTLSGGQKQRLAIARALIKQP--TVLILDEATSALDAESE 542
Cdd:cd03238 64 FIDQLQ-----------------FLIDVGLGYLTL-GQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 533869216 543 RVVQEALDR-ASAGRTVLVIAHRLSTVRGAHCIVVMADG 580
Cdd:cd03238 126 NQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
383-602 |
6.86e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 54.71 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 383 EVLKDFTLTLPPGKIVALVGQSGGGKTT----VASLLErfydPTAGVVMLDGRDlrtldPSWLRGQVVGFISqepVLFGT 458
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILV----PTSGEVRVLGYV-----PFKRRKEFARRIG---VVFGQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 459 --------TIMENIRFGKleasdeEVY---TAAREANAHEF-----ITSFpegYNTVVgeRgtTLSGGQKQRLAIARALI 522
Cdd:COG4586 104 rsqlwwdlPAIDSFRLLK------AIYripDAEYKKRLDELvelldLGEL---LDTPV--R--QLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 523 KQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRgAHC--IVVMADGRVWEAGTHEELLKKGGLY 598
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIE-ALCdrVIVIDHGRIIYDGSLEELKERFGPY 249
|
....
gi 533869216 599 AELI 602
Cdd:COG4586 250 KTIV 253
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
371-564 |
9.93e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 371 NVCFSYPCRPgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRGQV--VGF 448
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLcfVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 449 ISQ-EPVLfgtTIMENIRFgkleasdeEVYTAAREANAHEFITSFPEGYntVVGERGTTLSGGQKQRLAIARALIKQPTV 527
Cdd:PRK13540 82 RSGiNPYL---TLRENCLY--------DIHFSPGAVGITELCRLFSLEH--LIDYPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 533869216 528 LILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHR 564
Cdd:PRK13540 149 WLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
93-323 |
1.19e-07 |
|
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: 53.62 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTF--GYLVLlsHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRL--TTDVQEFkssfklvISQG 168
Cdd:cd18567 48 FGLLLLLQALLSAlrSWLVL--YLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFgsLDEIQQT-------LTTG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 169 LrsctqVAG------CLVSLSML---STRLTLLLMVATPALMGVGTLMgsgLRKLSRQCQEQI---ARAMGVADEALGNV 236
Cdd:cd18567 119 F-----VEAlldglmAILTLVMMflySPKLALIVLAAVALYALLRLAL---YPPLRRATEEQIvasAKEQSHFLETIRGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 237 RTVRAFameQREEERYGAELEAcrcRAEELGRGI------ALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL 310
Cdd:cd18567 191 QTIKLF---GREAEREARWLNL---LVDAINADIrlqrlqILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFL 264
|
250
....*....|...
gi 533869216 311 VASQTVQRSMANL 323
Cdd:cd18567 265 AYKDQFSSRASSL 277
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
392-567 |
2.01e-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: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 392 LP---PGKIVALVGQSGGGKTTVASLLerfydptAGVVM-----LDGrdlrtlDPSWlrgqvvgfisqEPVL--FGTTIM 461
Cdd:COG1245 93 LPvpkKGKVTGILGPNGIGKSTALKIL-------SGELKpnlgdYDE------EPSW-----------DEVLkrFRGTEL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 462 ENiRFGKLeaSDEEVyTAAREANAHEFITSFPEGynTV------VGERG-------------------TTLSGGQKQRLA 516
Cdd:COG1245 149 QD-YFKKL--ANGEI-KVAHKPQYVDLIPKVFKG--TVrellekVDERGkldelaeklglenildrdiSELSGGELQRVA 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 517 IARALIKQPTVLILDEATSALD----AESERVVQEAldrASAGRTVLVIAHRLST 567
Cdd:COG1245 223 IAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAI 274
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
506-565 |
2.62e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 2.62e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 533869216 506 TLSGGQKQRLAIARALIKQPTVLILDEATSALDAEsERV-VQEALDRASAGRTVLVIAHRL 565
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
367-571 |
2.99e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.41 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRpgfeVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPSWLrgqvv 446
Cdd:PRK13541 2 LSLHQLQFNIEQK----NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GFISQEPVL-FGTTIMENIRF-GKLEASDEEVYTAAREANAHEFITsfpegyntvvgERGTTLSGGQKQRLAIARALIKQ 524
Cdd:PRK13541 73 TYIGHNLGLkLEMTVFENLKFwSEIYNSAETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQ 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 533869216 525 PTVLILDEATSALDAESERVVQEALD-RASAGRTVLVIAHRLSTVRGA 571
Cdd:PRK13541 142 SDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSA 189
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
464-596 |
4.79e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.43 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 464 IRFGKLEA--SDEEVYTAAR---------EANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDE 532
Cdd:NF000106 93 VR*GRRESfsGRENLYMIGR*ldlsrkdaRARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 533 ATSALDAESERVV-QEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLKKGG 596
Cdd:NF000106 171 PTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
87-307 |
5.31e-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: 51.84 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 87 QNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTdVQEFKSSFKLVis 166
Cdd:cd18586 42 LGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELPLESRPSGYWQQLLRDLDT-LRNFLTGPSLF-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 167 qGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQ 246
Cdd:cd18586 119 -AFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLG 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 533869216 247 REEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLM 307
Cdd:cd18586 198 NLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGELTIGALI 258
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
388-615 |
6.03e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 388 FTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDPswlRGQVVGFI-------SQEPVLFGTTI 460
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSP---RDAIRAGImlcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 461 MENI---------RFGKLEASDEEvytaarEANAHEFITSF----PEGYNTVVgergtTLSGGQKQRLAIARALIKQPTV 527
Cdd:PRK11288 349 ADNInisarrhhlRAGCLINNRWE------AENADRFIRSLniktPSREQLIM-----NLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 528 LILDEATSALD--AESErVVQEALDRASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVweAGtheELLKkgglyAELIRR 604
Cdd:PRK11288 418 ILLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRI--AG---ELAR-----EQATER 486
|
250
....*....|...
gi 533869216 605 QALDA--PRTAAP 615
Cdd:PRK11288 487 QALSLalPRTSAA 499
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
49-302 |
6.56e-07 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 51.33 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 49 LALGAALVNVQIPLLLGQLVEVVAKYTRDHVgsfmtesqnlsTHLLILYGVQGLLTFGYLVLLSHV---GERMAVDMRRA 125
Cdd:cd18579 5 LKLLEDLLSLAQPLLLGLLISYLSSYPDEPL-----------SEGYLLALALFLVSLLQSLLLHQYfflSFRLGMRVRSA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 126 LFSSL----LRQDITFFDANKTGQLVSRLTTDVQEFKSSFkLVISQGLRSCTQVAGCLVSLSML---STRLTLLLMVatp 198
Cdd:cd18579 74 LSSLIyrkaLRLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALYLLYRLlgwAALAGLGVLL--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 199 ALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMeqreEERYGAELEAcrCRAEELG--RGIALFQGL 276
Cdd:cd18579 150 LLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAW----EKPFLKRIEE--LRKKELKalRKFGYLRAL 223
|
250 260
....*....|....*....|....*...
gi 533869216 277 SNIAFNCM-VLGTLFIGGSLVA-GQQLT 302
Cdd:cd18579 224 NSFLFFSTpVLVSLATFATYVLlGNPLT 251
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
495-598 |
9.16e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 495 GYNTVVGergtTLSGGQKQRLAIARALIKQPTVLILDEATSALD--AESErVVQEALDRASAGRTVLVIAHRLSTVRG-A 571
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKFE-IYQLIAELAKKDKGIIIISSEMPELLGiT 458
|
90 100 110
....*....|....*....|....*....|....
gi 533869216 572 HCIVVMADGRVweAG-------THEELLKKGGLY 598
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 ... |
62-252 |
9.84e-07 |
|
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: 50.97 E-value: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 62 LLLGQLVEVVAKYTRDHVGSFMTESQNLSTHLLILY------GVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDI 135
Cdd:cd18580 8 LLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVyaallvLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 136 TFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTrltlLLMVATPALMGVGTLMGSGLRKLS 215
Cdd:cd18580 88 SFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP----YFLIVLPPLLVVYYLLQRYYLRTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 533869216 216 RQCQ--EQIARA--MGVADEALGNVRTVRAFAMEQREEERY 252
Cdd:cd18580 164 RQLRrlESESRSplYSHFSETLSGLSTIRAFGWQERFIEEN 204
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
507-566 |
1.08e-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: 1.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 507 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRasAGRTVLVIAHRLS 566
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKS 640
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
507-568 |
1.58e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.58e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 507 LSGGQkQRLA-IARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLV------------IAHRLSTV 568
Cdd:PRK10938 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacITHRLEFV 476
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
371-581 |
1.60e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 371 NVCFSYPcrpGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGR--DLRTLDPSWLRGqvVGF 448
Cdd:PRK10982 3 NISKSFP---GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSKEALENG--ISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 449 ISQE-PVLFGTTIMENIRFGK-----LEASDEEVYTAAREANAHEFITSFPEgyntvvgERGTTLSGGQKQRLAIARALI 522
Cdd:PRK10982 78 VHQElNLVLQRSVMDNMWLGRyptkgMFVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 523 KQPTVLILDEATSALdAESE-----RVVQEALDRasaGRTVLVIAHRLSTVRgAHC--IVVMADGR 581
Cdd:PRK10982 151 YNAKIVIMDEPTSSL-TEKEvnhlfTIIRKLKER---GCGIVYISHKMEEIF-QLCdeITILRDGQ 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
367-582 |
1.81e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 367 VTFQNVCFSYPCRPgfEVLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMldgRDLRTLDPSWLRGQVV 446
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---RSAKVRMAVFSQHHVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 GF-ISQEPVLFgttiMENIRFGKLEasdeevytaaREANAHefITSFPEGYNTVVgERGTTLSGGQKQRLAIARALIKQP 525
Cdd:PLN03073 584 GLdLSSNPLLY----MMRCFPGVPE----------QKLRAH--LGSFGVTGNLAL-QPMYTLSGGQKSRVAFAKITFKKP 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 526 TVLILDEATSALDAESERVVQEALDRASAGrtVLVIAHRLSTVRGA-HCIVVMADGRV 582
Cdd:PLN03073 647 HILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKV 702
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
394-596 |
1.86e-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: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 394 PGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTlDPSWLRgQVVGFISQEPVLfgttimenirfGKLEASD 473
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVH-QNMGYCPQFDAI-----------DDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 474 EEVYTAAR---------EANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERV 544
Cdd:TIGR01257 2031 EHLYLYARlrgvpaeeiEKVANWSIQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 545 VQEAL-DRASAGRTVLVIAHRLSTVRgAHC--IVVMADGRVWEAGTHEELLKKGG 596
Cdd:TIGR01257 2109 LWNTIvSIIREGRAVVLTSHSMEECE-ALCtrLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
505-620 |
2.01e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 505 TTLSGGQKQRLAIARALI---KQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMA-- 578
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGpe 887
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 533869216 579 ----DGRVWEAGTHEELLKKGGLYAELIR---RQALDAPRTAAPPPKKP 620
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) ... |
379-566 |
2.18e-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: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 379 RPGFEVLKDFTLTLP-PGKIVALVGQSGGGKTTVASLLE--------RFYDPTAGVVMLD---GRDLRTLDPSWLRGQV- 445
Cdd:cd03236 9 RYGPNSFKLHRLPVPrEGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 446 ----VGFISQEPVLFGTTIMENirfgkLEASDEEvytaareaNAHEFITSFPEgYNTVVGERGTTLSGGQKQRLAIARAL 521
Cdd:cd03236 89 vivkPQYVDLIPKAVKGKVGEL-----LKKKDER--------GKLDELVDQLE-LRHVLDRNIDQLSGGELQRVAIAAAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 533869216 522 IKQPTVLILDEATSALDAESE----RVVQEaldRASAGRTVLVIAHRLS 566
Cdd:cd03236 155 ARDADFYFFDEPSSYLDIKQRlnaaRLIRE---LAEDDNYVLVVEHDLA 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
387-538 |
2.33e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 387 DFT------LTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVML-----DGRDLRTldpswlRgQVVGFISQEPVL 455
Cdd:NF033858 278 DFTavdhvsFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDIAT------R-RRVGYMSQAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 456 FGT-TIMENIrfgKLEASDEEVYTAAREANAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 534
Cdd:NF033858 351 YGElTVRQNL---ELHARLFHLPAAEIAARVAEMLERF--DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
....
gi 533869216 535 SALD 538
Cdd:NF033858 426 SGVD 429
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
505-565 |
3.37e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.41 E-value: 3.37e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 505 TTLSGGQKQRLAIARALIK---QPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRL 565
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRlVDKGNTVVVIEHNL 889
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
442-565 |
4.52e-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: 47.57 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 442 RGQVVGFISqePVLFGTTIMENIRFGKLEASDEEvytaareanahefiTSFPeGYNTVVGERGTTLSGGQKQRLAIARAL 521
Cdd:cd03222 24 EGEVIGIVG--PNGTGKTTAVKILAGQLIPNGDN--------------DEWD-GITPVYKPQYIDLSGGELQRVAIAAAL 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 533869216 522 IKQPTVLILDEATSALDAESERVVQEALDRAS--AGRTVLVIAHRL 565
Cdd:cd03222 87 LRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDL 132
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
390-616 |
6.54e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 390 LTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAG--------VVMLDGRDLRTL-DPSWLRGQVvGFISQEPVLFGTTI 460
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshITRLSFEQLQKLvSDEWQRNNT-DMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 461 MENIRfgkleasdEEVYTAAReanAHEFITSFpeGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE 540
Cdd:PRK10938 103 AEIIQ--------DEVKDPAR---CEQLAQQF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 541 SERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRVWEAGTHEELLKKgGLYAELIRRQALDA---PRTAAP 615
Cdd:PRK10938 170 SRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ-ALVAQLAHSEQLEGvqlPEPDEP 248
|
.
gi 533869216 616 P 616
Cdd:PRK10938 249 S 249
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
377-582 |
9.12e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 377 PCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKTTVA-SLLERFYDP-TAGVVMLDGRDLRTLDPSWLRGQVVGFISQEPV 454
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 455 LFGTTIMENIRF-------GKLeaSDEEVYTAAREAN-AHEFITSF----PEGYNTVVgergtTLSGGQKQRLAIARALI 522
Cdd:NF040905 348 GYGLNLIDDIKRnitlanlGKV--SRRGVIDENEEIKvAEEYRKKMniktPSVFQKVG-----NLSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 523 KQPTVLILDEATSALD--AESE--RVVQEAldrASAGRTVLVIAHRLSTVRGAhC--IVVMADGRV 582
Cdd:NF040905 421 TDPDVLILDEPTRGIDvgAKYEiyTIINEL---AAEGKGVIVISSELPELLGM-CdrIYVMNEGRI 482
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
370-582 |
9.15e-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: 48.67 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 370 QNVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKT-TVASLLERFYDPTAGVVMLDGRDLRTLDPS-WLRGQVV- 446
Cdd:TIGR02633 261 RNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVDIRNPAqAIRAGIAm 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 447 --------GFISQEPVLFGTTIMENIRFGKLEASDE--EVYTAAREANAHEFITSFPEgyntvvgERGTTLSGGQKQRLA 516
Cdd:TIGR02633 341 vpedrkrhGIVPILGVGKNITLSVLKSFCFKMRIDAaaELQIIGSAIQRLKVKTASPF-------LPIGRLSGGNQQKAV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 533869216 517 IARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRG-AHCIVVMADGRV 582
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
389-563 |
9.93e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.93 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 389 TLTLPPGkIVALVGQSGGGKTTVASLLER-FYDPTAGVVMLDgRDLRTLDPS------------------WLRGQVVGFI 449
Cdd:COG0419 18 TIDFDDG-LNLIVGPNGAGKSTILEAIRYaLYGKARSRSKLR-SDLINVGSEeasvelefehggkryrieRRQGEFAEFL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 450 SQEP--------VLFGTTIMENI--RFGKLEASDEEVYTAAREANA-HEFITSFPEGYNTVvgergTTLSGGQKQRLAIA 518
Cdd:COG0419 96 EAKPserkealkRLLGLEIYEELkeRLKELEEALESALEELAELQKlKQEILAQLSGLDPI-----ETLSGGERLRLALA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 533869216 519 RALikqptVLILDeaTSALDAESERVVQEALDRASagrtvlVIAH 563
Cdd:COG0419 171 DLL-----SLILD--FGSLDEERLERLLDALEELA------IITH 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
365-582 |
1.04e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 365 GSVTFQ--NVCFSYPCRPGFEVLKDFTLTLPPGKIVALVGQSGGGKT-TVASLLERFYDPTAGVVMLDGRDLRTLDPSWL 441
Cdd:PRK13549 256 GEVILEvrNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 442 RGQVVGFISQEPVLFG-TTIM---ENI------RFGKLEASDEevytAAREANAHEFI------TSFPEgyntvvgERGT 505
Cdd:PRK13549 336 IAQGIAMVPEDRKRDGiVPVMgvgKNItlaaldRFTGGSRIDD----AAELKTILESIqrlkvkTASPE-------LAIA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 506 TLSGGQKQRLAIARALIKQPTVLILDEATSALD----AESERVVQEAldrASAGRTVLVIAHRLSTVRG-AHCIVVMADG 580
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakYEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEG 481
|
..
gi 533869216 581 RV 582
Cdd:PRK13549 482 KL 483
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
93-330 |
1.35e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 47.51 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRL--TTDVQEFkssfklvISQGLR 170
Cdd:cd18783 48 VVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMqqIERIRQF-------LTGQLF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 171 SCTQVAGCLV----SLSMLSTRLTLLLMVATPALMG-VGTLMGSGLRKLSRQCQEQIAR-AMGVadEALGNVRTVRAFAM 244
Cdd:cd18783 121 GTLLDATSLLvflpVLFFYSPTLALVVLAFSALIALiILAFLPPFRRRLQALYRAEGERqAFLV--ETVHGIRTVKSLAL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 245 EQREEERYGAEL-EACRcRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANL 323
Cdd:cd18783 199 EPRQRREWDERVaRAIR-ARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQL 277
|
....*..
gi 533869216 324 SVLFGQV 330
Cdd:cd18783 278 AGLVQEY 284
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
384-549 |
2.11e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 384 VLKDFTLTLPPGKIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDgrdlrtldpswlRGQVVGFISQEPVLFgttimen 463
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------------KGIKLGYFAQHQLEF------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 464 irfgkLEASDEEVYTAAR------EANAHEFITSFpeGYN-TVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 536
Cdd:PRK10636 388 -----LRADESPLQHLARlapqelEQKLRDYLGGF--GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170
....*....|...
gi 533869216 537 LDAESERVVQEAL 549
Cdd:PRK10636 461 LDLDMRQALTEAL 473
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
100-268 |
2.92e-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: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 100 QGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFkSSFKLVISQGLRSCTQVAGCL 179
Cdd:cd18559 51 QGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRV-DSMAPQVIKMWMGPLQNVIGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 180 VSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAmeqrEEERYGAELEAc 259
Cdd:cd18559 130 YLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFE----WEEAFIRQVDA- 204
|
....*....
gi 533869216 260 rCRAEELGR 268
Cdd:cd18559 205 -KRDNELAY 212
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
51-311 |
3.08e-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: 46.06 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 51 LGAALVNVQIPLLLGQLVEVVAKYTRDHVGSFMTesqnlsthLLILYGVQGLL--TFGYL--VLLSHVGERMAVDMRRAL 126
Cdd:cd18560 6 ILGKACNVLAPLFLGRAVNALTLAKVKDLESAVT--------LILLYALLRFSskLLKELrsLLYRRVQQNAYRELSLKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 127 FSSLLRQDITFFDANKTGQLVS---RLTTDVQEFKSSFKLVISQGLRSCtqVAGCLVSLSMLSTRLTLLLMVATpALMGV 203
Cdd:cd18560 78 FAHLHSLSLDWHLSKKTGEVVRimdRGTESANTLLSYLVFYLVPTLLEL--IVVSVVFAFHFGAWLALIVFLSV-LLYGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 204 GTLMGSGLR-KLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEAcrcrAEELGRGIALFQGLSNIA-- 280
Cdd:cd18560 155 FTIKVTEWRtKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKE----YQKSSVKVQASLSLLNVGqq 230
|
250 260 270
....*....|....*....|....*....|...
gi 533869216 281 --FNCMVLGTLFIGGSLVAGQQLTGGDLMSFLV 311
Cdd:cd18560 231 liIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNT 263
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
495-598 |
3.55e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 495 GYNTVvGERGTTLSGGQKQRLAIARALIKQPT---VLILDEATSALDAESER----VVQEALDRasaGRTVLVIAHRLST 567
Cdd:PRK00349 820 GYIKL-GQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRklleVLHRLVDK---GNTVVVIEHNLDV 895
|
90 100 110
....*....|....*....|....*....|....*..
gi 533869216 568 VRGAHCIVVM------ADGRVWEAGTHEELLKKGGLY 598
Cdd:PRK00349 896 IKTADWIIDLgpeggdGGGEIVATGTPEEVAKVEASY 932
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
93-310 |
9.55e-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: 44.85 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRL--TTDVQEfkssfkLVISQGLR 170
Cdd:cd18779 48 LAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLssNATIRE------LLTSQTLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 171 SC---TQVAGCLVSLSMLSTRLTLLLMVAtpALMGVGTLMGSG--LRKLSRQCQEQIARAMGVADEALGNVRTVRAFAME 245
Cdd:cd18779 122 ALldgTLVLGYLALLFAQSPLLGLVVLGL--AALQVALLLATRrrVRELMARELAAQAEAQSYLVEALSGIETLKASGAE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 246 QREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFL 310
Cdd:cd18779 200 DRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALN 264
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
396-438 |
9.68e-05 |
|
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: 9.68e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 533869216 396 KIVALVGQSGGGKTTVASLLERFYDPTAGVVMLDGRDLRTLDP 438
Cdd:pfam06414 12 KAILLGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELHP 54
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
62-336 |
1.02e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 44.58 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 62 LLLGQLVEVVakYTRDHVGSFMTesqnLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDAN 141
Cdd:cd18561 17 WLLARALARI--FAGGPWEDIMP----PLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 142 KTGQLVSRLTTDVQEFKSSFKLVISQGLRSCTQVAGCLVSLSMLSTRLTLLLMVATPALMGVGTLMGSGLRKLSRQCQEQ 221
Cdd:cd18561 91 RTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 222 IARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRCRAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQL 301
Cdd:cd18561 171 YGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQL 250
|
250 260 270
....*....|....*....|....*....|....*
gi 533869216 302 TGGDLMSFLVASQTVQRSMANLSVLFGQVVRGLSA 336
Cdd:cd18561 251 TLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISA 285
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
505-593 |
1.21e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 505 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRgAHC--IVVMADGR 581
Cdd:PRK09700 408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEII-TVCdrIAVFCEGR 486
|
90
....*....|....*...
gi 533869216 582 V------WEAGTHEELLK 593
Cdd:PRK09700 487 LtqiltnRDDMSEEEIMA 504
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
93-292 |
2.37e-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: 43.67 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 93 LLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKSSFKLVISQGLRSC 172
Cdd:cd18605 48 YGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 173 TQVAGCLVSLSMLSTRLTLLLMVatpaLMGVGTLMGSGLRKLSRqcqeQIARAMGVA--------DEALGNVRTVRAFAM 244
Cdd:cd18605 128 FGLLGYLVVICYQLPWLLLLLLP----LAFIYYRIQRYYRATSR----ELKRLNSVNlsplythfSETLKGLVTIRAFRK 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 533869216 245 EQREEERYGAELEACRcRAEELGRGIAL-----FQGLSniafNCMVLGTLFIG 292
Cdd:cd18605 200 QERFLKEYLEKLENNQ-RAQLASQAASQwlsirLQLLG----VLIVTFVALTA 247
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
505-541 |
2.54e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 2.54e-04
10 20 30
....*....|....*....|....*....|....*..
gi 533869216 505 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES 541
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
506-538 |
3.33e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 3.33e-04
10 20 30
....*....|....*....|....*....|...
gi 533869216 506 TLSGGQKQRLAIARALIKQPTVLILDEATSALD 538
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
392-563 |
3.89e-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: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 392 LPPGKIVALVGQSGGGKTTVASLLerfydptaGVVMLDGRdlrtldpSWLRGQVVGfiSQEPVLFGTTIMENIRFGK-LE 470
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDL--------AAAVATGK-------PWLGGPRVP--EQGKVLYVSAEGPADELRRrLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 471 ASdeevyTAAREANAHEFITSFPEGYNTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSAL-----DAESERVV 545
Cdd:pfam13481 93 AA-----GADLDLPARLLFLSLVESLPLFFLDRGGPLLDADVDALEAALEEVEDPDLVVIDPLARALggdenSNSDVGRL 167
|
170 180
....*....|....*....|
gi 533869216 546 QEALDRASA--GRTVLVIAH 563
Cdd:pfam13481 168 VKALDRLARrtGATVLLVHH 187
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
385-588 |
5.36e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.86 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 385 LKDFTLTLPPGKIVALVGQSGGGKTTVAsllerfYDptagVVMLDG--RDLRTLdPSWLRgQVVGFISQEPV-----LFG 457
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLA------FD----TIYAEGqrRYVESL-SAYAR-QFLGQMDKPDVdsiegLSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 458 TTIMENIRFGKLEASD----EEVYTA-----AREA--NAHEFITSFPEGYNTVvGERGTTLSGGQKQRLAIARALIKQPT 526
Cdd:cd03270 79 AIAIDQKTTSRNPRSTvgtvTEIYDYlrllfARVGirERLGFLVDVGLGYLTL-SRSAPTLSGGEAQRIRLATQIGSGLT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 533869216 527 --VLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRGAHCIVVMADGrvweAGTH 588
Cdd:cd03270 158 gvLYVLDEPSIGLHPRDNDRLIETLKRlRDLGNTVLVVEHDEDTIRAADHVIDIGPG----AGVH 218
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
56-334 |
6.05e-04 |
|
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: 42.13 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 56 VNVQIPLLLGQLVEvvakytrdhvgSFMTESQNLSTHLLILYGV------QGLLTFGYLVLLSHVGERMAVDMRRALFSS 129
Cdd:cd18583 11 LNVLVPRQLGIIVD-----------SLSGGSGKSPWKEIGLYVLlrflqsGGGLGLLRSWLWIPVEQYSYRALSTAAFNH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 130 LLRQDITFFDANKTGQLVSrlttdvqefkssfklVISQGlRSCTQ------------VAGCLVSLSMLSTR----LTLLL 193
Cdd:cd18583 80 VMNLSMDFHDSKKSGEVLK---------------AIEQG-SSINDlleqilfqivpmIIDLVIAIVYLYYLfdpyMGLIV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 194 MVATPALMGVGTLMGSGLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMEQREEERYGAELEACRcRAE-ELGRGIAL 272
Cdd:cd18583 144 AVVMVLYVWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQ-KAErKYLFSLNL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 533869216 273 FQGLSNIAFNCMVLGTLFIGGSLVAGQQLTGGDLMSFLVASQTVQRSMANLSVLFGQVVRGL 334
Cdd:cd18583 223 LNAVQSLILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDL 284
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
502-563 |
7.85e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.05 E-value: 7.85e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 533869216 502 ERGTtLSGGQKQ------RLAIARALIKQPTVLILDEATSALDAES-ERVVQEALD--RASAGRTVLVIAH 563
Cdd:cd03240 112 MRGR-CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEerKSQKNFQLIVITH 181
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
390-565 |
8.02e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.42 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 390 LTLPPGKIVALVGQSGGGKTTVasllerfydptagvvmldgrdLRTldpswlrgqvVGFIsqepvLFGTtiMENIRFGKL 469
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTI---------------------LDA----------IGLA-----LGGA--QSATRRRSG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 470 EASDEEVytAAREAnahEFITSFPegyntvvgergtTLSGGQKQRLAIARAL----IKQPTVLILDEATSALDAESERVV 545
Cdd:cd03227 58 VKAGCIV--AAVSA---ELIFTRL------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQAL 120
|
170 180
....*....|....*....|.
gi 533869216 546 QEAL-DRASAGRTVLVIAHRL 565
Cdd:cd03227 121 AEAIlEHLVKGAQVIVITHLP 141
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
84-184 |
2.14e-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: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 84 TESQNLSTHLLILYG----VQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDVQEFKS 159
Cdd:cd18603 34 TQDTEQRDYRLGVYGalglGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDN 113
|
90 100
....*....|....*....|....*
gi 533869216 160 SFKLVISQGLRSCTQVAGCLVSLSM 184
Cdd:cd18603 114 TLPQNIRSFLNCLFQVISTLVVISI 138
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
505-619 |
2.62e-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: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 505 TTLSGGQKQRLAIARALIKQPT-VL-ILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRGAHCIVVMA--- 578
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIGSGLTgVLyVLDEPSIGLhQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIGpga 566
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 533869216 579 ---DGRVWEAGTHEELLKKG----GLYaeLIRRQALDAPRTAAPPPKK 619
Cdd:TIGR00630 567 gehGGEVVASGTPEEILANPdsltGQY--LSGRKKIEVPAERRPGNGK 612
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
99-154 |
3.32e-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: 3.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 533869216 99 VQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDANKTGQLVSRLTTDV 154
Cdd:cd18606 47 LQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDT 102
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
61-306 |
4.49e-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: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 61 PLLLGQLVevvAKYTRDHVGSfMTESQNLSTHLLILYGVQGLLTFGYLVLLSHVGERMAVDMRRALFSSLLRQDITFFDA 140
Cdd:cd18594 17 PLLLGRLV---AYFVPDSTVT-KTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALSK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 141 NKTGQLVSRLTTDVQEFKSSFK----LVISQGLRSCTQV-------AGCLVSLSMLstrLTLLLMVAtpalmgvgtLMGS 209
Cdd:cd18594 93 ITTGHIVNLLSNDVQKFDEVLVylhfLWIAPLQVIVLTGllwreigPSSLAGLGVL---LLLLPLQA---------YLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 210 GLRKLSRQCQEQIARAMGVADEALGNVRTVRAFAMeqreEERYGAELEACRCRAEELGRGIALFQGLsNIAFncMVLGTL 289
Cdd:cd18594 161 LFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTW----EESFAKLIENIRKKELKLIRKAAYIRAF-NMAF--FFFSPT 233
|
250
....*....|....*..
gi 533869216 290 FIGGSLVAGQQLTGGDL 306
Cdd:cd18594 234 LVSFATFVPYVLTGNTL 250
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
494-563 |
5.14e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 494 EGYNTVVGERGT-----TLSGGQKQ------RLAIARALIKQPTVLILDEATSALDAESER----VVQEALDRASAGRTV 558
Cdd:PRK01156 784 QDFNITVSRGGMvegidSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTnlkdIIEYSLKDSSDIPQV 863
|
....*
gi 533869216 559 LVIAH 563
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; ... |
139-302 |
7.16e-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: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 139 DANKTGQLVSRLTTDVQEFkSSFKLVISQGLRSCTQVAGCLVSLSMLstrltlllmVATPALMGVGTLMGSG-----LRK 213
Cdd:cd18596 110 SSASVGKINNLMSVDANRI-SEFAAFLHLLVSAPLQIVIAIVFLYRL---------LGWSALVGLAVMVLLLplngyLAK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 533869216 214 LSRQCQEQIARA----MGVADEALGNVRTVRAFAMEQREEERYgaeLEAcrcRAEELG--RGIALFQGLSNIAFNCM-VL 286
Cdd:cd18596 180 RYSRAQKELMKArdarVQLVTEVLQGIRMIKFFAWERKWEERI---LEA---REEELKwlRKRFLLDLLLSLLWFLIpIL 253
|
170
....*....|....*...
gi 533869216 287 GTLFIGGS--LVAGQQLT 302
Cdd:cd18596 254 VTVVTFATytLVMGQELT 271
|
|
| |
