|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
103-687 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 612.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 103 KMGRSQYGRLLSLTKSEKWVLTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSgmdsaAMAKLGEYSVLLFGIFVLGGFA 182
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG-----DLSALLLLLLLLLGLALLRALL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 183 NFARVHLFGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMI 262
Cdd:COG1132 78 SYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 263 YTSPQLAAVSALVVPAMAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIG 342
Cdd:COG1132 158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 343 YKETRARAIFFGLTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERIWEI 422
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 423 LDRECSIPIDKGVVPLEKPVGEVGFQNVFFTFPtrPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGG 502
Cdd:COG1132 318 LDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 503 TVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILYGaNPGETpsPERLQQVIEDANVSQFTDQLPDGLDTLVGQ 582
Cdd:COG1132 396 RILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYG-RPDAT--DEEVEEAAKAAQAHEFIEALPDGYDTVVGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 583 RGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKI 662
Cdd:COG1132 473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
570 580
....*....|....*....|....*
gi 23397593 663 VEQGSYNELMGiQEGVFRELVASQA 687
Cdd:COG1132 553 VEQGTHEELLA-RGGLYARLYRLQF 576
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
111-683 |
9.68e-164 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 487.69 E-value: 9.68e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 111 RLLSLTKSEKWVLTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSAAMAklgeysVLLFGIFVLGG-FANFARVHL 189
Cdd:TIGR00958 151 RLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASA------IFFMCLLSIASsVSAGLRGGS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 190 FGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLA 269
Cdd:TIGR00958 225 FNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLT 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 270 AVSALVVPAMAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRAR 349
Cdd:TIGR00958 305 MVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAY 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 350 AIFFGLTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERIWEILDRECSI 429
Cdd:TIGR00958 385 AGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 430 PIDKGVVPlEKPVGEVGFQNVFFTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGI 509
Cdd:TIGR00958 465 PLTGTLAP-LNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 510 DLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILYGANPGETpspERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSG 589
Cdd:TIGR00958 544 PLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPD---EEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSG 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 590 GQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNalDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYN 669
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
570
....*....|....
gi 23397593 670 ELMGiQEGVFRELV 683
Cdd:TIGR00958 699 QLME-DQGCYKHLV 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
106-687 |
2.66e-160 |
|
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: 478.94 E-value: 2.66e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 106 RSQYGRLLSLTKSEKWVLTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSaamakLGEYSVLLFGIFVLGGFANFA 185
Cdd:COG2274 141 PFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLST-----LWVLAIGLLLALLFEGLLRLL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 186 RVHLFGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLsNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTS 265
Cdd:COG2274 216 RSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYS 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 266 PQLAAVSALVVPAMAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKE 345
Cdd:COG2274 295 PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 346 TRARAIFFGLTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERIWEILDR 425
Cdd:COG2274 375 RRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 426 ECSIPIDKGVVPLEKPVGEVGFQNVFFTFPTRpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVH 505
Cdd:COG2274 455 PPEREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 506 LDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILYGAnpgETPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGM 585
Cdd:COG2274 534 IDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD---PDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGS 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 586 MLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQ 665
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
570 580
....*....|....*....|..
gi 23397593 666 GSYNELMGiQEGVFRELVASQA 687
Cdd:COG2274 691 GTHEELLA-RKGLYAELVQQQL 711
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
126-419 |
9.14e-143 |
|
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: 418.46 E-value: 9.14e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 126 GIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSAAMAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLRSRL 205
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 206 YRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAIV 285
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 286 YGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIII 365
Cdd:cd18573 161 YGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 23397593 366 SVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18573 241 SVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
109-686 |
3.68e-134 |
|
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: 406.80 E-value: 3.68e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 109 YGRLLSLTKSEKWVLT-AGIGCLVVSSAITMsVPLFLGKVIDVVFNKsgmdsAAMAKLGEYSVLLFGIFVLGGFANFARV 187
Cdd:TIGR02203 2 FRRLWSYVRPYKAGLVlAGVAMILVAATEST-LAALLKPLLDDGFGG-----RDRSVLWWVPLVVIGLAVLRGICSFVST 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 188 HLFGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVgtslSQNVSDGLRSV---AMIGVG-TGMMIY 263
Cdd:TIGR02203 76 YLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQV----ASAATDAFIVLvreTLTVIGlFIVLLY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 264 TSPQLAAVSALVVPAMAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGY 343
Cdd:TIGR02203 152 YSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 344 KETRARAIFFGLTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERIWEIL 423
Cdd:TIGR02203 232 KMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 424 DREcsIPIDKGVVPLEKPVGEVGFQNVFFTFPTRpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGT 503
Cdd:TIGR02203 312 DSP--PEKDTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 504 VHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILYGAnpGETPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQR 583
Cdd:TIGR02203 389 ILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR--TEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGEN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 584 GMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIV 663
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
570 580
....*....|....*....|...
gi 23397593 664 EQGSYNELMGiQEGVFRELVASQ 686
Cdd:TIGR02203 547 ERGTHNELLA-RNGLYAQLHNMQ 568
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
447-686 |
1.30e-124 |
|
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: 369.95 E-value: 1.30e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAV 526
Cdd:cd03249 3 FKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEPVLFSCSIRENILYGANPGETpspERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPA 606
Cdd:cd03249 83 SQEPVLFDGTIAENIRYGKPDATD---EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 607 ILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGiQEGVFRELVASQ 686
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLVKAQ 238
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
111-689 |
9.08e-110 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 343.92 E-value: 9.08e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 111 RLLSLTKSEKWVLTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSgmDSAAMAKLgeySVLLFGIFVLGGFANFARVHLF 190
Cdd:PRK11176 15 RLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKA--DRSVLKWM---PLVVIGLMILRGITSFISSYCI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 191 GNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAA 270
Cdd:PRK11176 90 SWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 271 VSALVVPAMA-GMAIVYGRYvRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRAR 349
Cdd:PRK11176 170 ILIVIAPIVSiAIRVVSKRF-RNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSAS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 350 AIFFGLTGFCGNFIIISVLYYGGTLVLQDSLTIGALTafMLYAGYVAI--SMNGLSNFYSQLNKGIGASERIWEILDREC 427
Cdd:PRK11176 249 SISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTIT--VVFSSMIALmrPLKSLTNVNAQFQRGMAACQTLFAILDLEQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 428 SIpiDKGVVPLEKPVGEVGFQNVFFTFPTRPESAvLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLD 507
Cdd:PRK11176 327 EK--DEGKRVIERAKGDIEFRNVTFTYPGKEVPA-LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 508 GIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILYGANpgETPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMML 587
Cdd:PRK11176 404 GHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYART--EQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 588 SGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGS 667
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGT 561
|
570 580
....*....|....*....|..
gi 23397593 668 YNELMGiQEGVFRELVASQaFG 689
Cdd:PRK11176 562 HAELLA-QNGVYAQLHKMQ-FG 581
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
314-687 |
6.59e-104 |
|
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: 329.47 E-value: 6.59e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 314 NVKTVKTFCREQQEVAAFDGKLDEalqigYKETRARAIF-FGLTGFCGNFII----ISVLYYGGTLVLQDSLTIGALT-- 386
Cdd:COG5265 227 NYETVKYFGNEAREARRYDEALAR-----YERAAVKSQTsLALLNFGQALIIalglTAMMLMAAQGVVAGTMTVGDFVlv 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 387 -AFM--LYagyvaISMNGLSNFYSQLNKGIGASERIWEILDRECSIPIDKGVVPLEKPVGEVGFQNVFFTFptRPESAVL 463
Cdd:COG5265 302 nAYLiqLY-----IPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGY--DPERPIL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 464 TDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILY 543
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAY 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 544 GaNPGETPspERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSEN 623
Cdd:COG5265 455 G-RPDASE--EEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTER 531
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 624 LVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGiQEGVFRELVASQA 687
Cdd:COG5265 532 AIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLA-QGGLYAQMWARQQ 594
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
111-672 |
3.24e-102 |
|
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: 323.63 E-value: 3.24e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 111 RLLSLTKSEKWVLTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSAAMAKLGeysvLLFGIFVLGGFANFARVHLF 190
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLG----LLLAVLLLRALLAWLRERAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 191 GNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELInrlsndTLMV----------GTSLSQNVSDGLRSVAMIGVgtgm 260
Cdd:COG4988 83 FRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELA------TLLTegvealdgyfARYLPQLFLAALVPLLILVA---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 261 MIYTSPQLAAVSALVVPAM-AGMAIVygryvRRITKVELDKYAEIMkfaeERFGN--------VKTVKTFCREQQEVAAF 331
Cdd:COG4988 153 VFPLDWLSGLILLVTAPLIpLFMILV-----GKGAAKASRRQWRAL----ARLSGhfldrlrgLTTLKLFGRAKAEAERI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 332 DgKLDEALqigyketRAR-----AIFFgLTGFCGNFI----IISVLYYGGTLVLQDSLTI-GALTAFMLyAGYVAISMNG 401
Cdd:COG4988 224 A-EASEDF-------RKRtmkvlRVAF-LSSAVLEFFaslsIALVAVYIGFRLLGGSLTLfAALFVLLL-APEFFLPLRD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 402 LSNFYSQLNKGIGASERIWEILDRECSIPIDKGVVPLEKPVGEVGFQNVFFTFPTRPEsaVLTDFSLNLMPGTTTAVVGR 481
Cdd:COG4988 294 LGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRP--ALDGLSLTIPPGERVALVGP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 482 SGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILYGAnpgETPSPERLQQVIE 561
Cdd:COG4988 372 SGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR---PDASDEELEAALE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 562 DANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTI 641
Cdd:COG4988 449 AAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILI 528
|
570 580 590
....*....|....*....|....*....|.
gi 23397593 642 AHRLSTIRNADQIAVLSDGKIVEQGSYNELM 672
Cdd:COG4988 529 THRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
445-682 |
6.29e-101 |
|
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: 308.78 E-value: 6.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 445 VGFQNVFFTFPTRPEsAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIG 524
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 525 AVSQEPVLFSCSIRENILYGaNPGETPspERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKN 604
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG-RPGATR--EEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 605 PAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGiQEGVFREL 682
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA-QGGVYAKL 233
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
126-419 |
2.72e-98 |
|
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: 303.71 E-value: 2.72e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 126 GIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDsaamaKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLRSRL 205
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLD-----VLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 206 YRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAIV 285
Cdd:cd18557 76 FSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 286 YGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIII 365
Cdd:cd18557 156 YGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 23397593 366 SVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18557 236 LVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
135-686 |
1.63e-97 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 315.14 E-value: 1.63e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 135 AITMSVPLFLGKVIDVVFNKSGMDSAAMAKLGEYSVLLFGIFvLGGFanfaRVHLFGNAALRIVRSLRSRLYRSMLMQEV 214
Cdd:TIGR01846 153 LFALVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPA-LGGL----RTYLFAHLTSRIDVELGARLYRHLLGLPL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 215 GWFDTKGTGELINR----------LSNDTLMVgtslsqnVSDGLRSVAMIGVgtgmMIYTSPQLAAVSALVVPAMAGMAI 284
Cdd:TIGR01846 228 GYFESRRVGDTVARvreleqirnfLTGSALTV-------VLDLLFVVVFLAV----MFFYSPTLTGVVIGSLVCYALLSV 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 285 VYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQevaaFDGKLDEALQiGYKETRARAIFFGLTGFCGNFII 364
Cdd:TIGR01846 297 FVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQ----FQNRWDRQLA-AYVAASFRVTNLGNIAGQAIELI 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 365 -----ISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERIWEILDrECSIPIDKGVVPLE 439
Cdd:TIGR01846 372 qkltfAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPRSAGLAALP 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 440 KPVGEVGFQNVFFTFptRPESA-VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQW 518
Cdd:TIGR01846 451 ELRGAITFENIRFRY--APDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAW 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 519 LRNNIGAVSQEPVLFSCSIRENILYGaNPGEtpSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIA 598
Cdd:TIGR01846 529 LRRQMGVVLQENVLFSRSIRDNIALC-NPGA--PFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIA 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 599 RALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGiQEGV 678
Cdd:TIGR01846 606 RALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLA-LQGL 684
|
....*...
gi 23397593 679 FRELVASQ 686
Cdd:TIGR01846 685 YARLWQQQ 692
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
109-686 |
6.92e-95 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 305.35 E-value: 6.92e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 109 YGRLLSLTKSEKWVLTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSAAMAKLGeysvllFGIFVLGGFANFARvh 188
Cdd:PRK13657 7 YARVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAISGKGDIFPLLAAWAG------FGLFNIIAGVLVAR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 189 lfgnAALRIvrSLRSRL-----YRSMLMQ-EVGWFDTKGTGELINrlsndTLMVGTSlsqnvsdglrsvAMIGVGTGMMi 262
Cdd:PRK13657 79 ----HADRL--AHRRRLavlteYFERIIQlPLAWHSQRGSGRALH-----TLLRGTD------------ALFGLWLEFM- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 263 ytSPQLAAVSALVV--P-AMA----------GMAIVY---GRYVRRITK-----VElDKYAEIMKFAEERFGNVKTVKTF 321
Cdd:PRK13657 135 --REHLATLVALVVllPlALFmnwrlslvlvVLGIVYtliTTLVMRKTKdgqaaVE-EHYHDLFAHVSDAIGNVSVVQSY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 322 CREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNG 401
Cdd:PRK13657 212 NRIEAETQALRDIADNLLAAQMPVLSWWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 402 LSNFYSQLnkgIGASERIWEILDRECSIPIDK---GVVPLEKPVGEVGFQNVFFTFPTRPESavLTDFSLNLMPGTTTAV 478
Cdd:PRK13657 292 VVAFINQV---FMAAPKLEEFFEVEDAVPDVRdppGAIDLGRVKGAVEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 479 VGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILYGAnpgETPSPERLQQ 558
Cdd:PRK13657 367 VGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGR---PDATDEEMRA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 559 VIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTV 638
Cdd:PRK13657 444 AAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTT 523
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 23397593 639 LTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGiQEGVFRELVASQ 686
Cdd:PRK13657 524 FIIAHRLSTVRNADRILVFDNGRVVESGSFDELVA-RGGRFAALLRAQ 570
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
192-684 |
1.59e-93 |
|
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: 300.91 E-value: 1.59e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 192 NAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSND--TLmvgtslsQNVSdgLR-------SVAMIGVGTGMMI 262
Cdd:COG4987 81 DATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADvdAL-------DNLY--LRvllpllvALLVILAAVAFLA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 263 YTSPQLA-------AVSALVVPAMAgmAIVYGRYVRRITKVELDKYAEIMkfaeERFGNVKTVKTFCREQQEVAAFDGKL 335
Cdd:COG4987 152 FFSPALAlvlalglLLAGLLLPLLA--ARLGRRAGRRLAAARAALRARLT----DLLQGAAELAAYGALDRALARLDAAE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 336 DEALQIGYKETRARAIFFGLTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGA 415
Cdd:COG4987 226 ARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 416 SERIWEILDRECSIPIDKGVVPLEKPVGeVGFQNVFFTFPTRPEsAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLR 495
Cdd:COG4987 306 ARRLNELLDAPPAVTEPAEPAPAPGGPS-LELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 496 LYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILYgANPGetPSPERLQQVIEDANVSQFTDQLPDG 575
Cdd:COG4987 384 FLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRL-ARPD--ATDEELWAALERVGLGDWLAALPDG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 576 LDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIA 655
Cdd:COG4987 461 LDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL 540
|
490 500
....*....|....*....|....*....
gi 23397593 656 VLSDGKIVEQGSYNELMGiQEGVFRELVA 684
Cdd:COG4987 541 VLEDGRIVEQGTHEELLA-QNGRYRQLYQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
445-686 |
2.60e-93 |
|
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: 289.13 E-value: 2.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 445 VGFQNVFFTFPtrPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIG 524
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 525 AVSQEPVLFSCSIRENILYGaNPGETPsperlQQVIEDANVSQFTD---QLPDGLDTLVGQRGMMLSGGQKQRVAIARAL 601
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYG-RPDATD-----EEVIEAAKAAQIHDkimRFPDGYDTIVGERGLKLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGiQEGVFRE 681
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAE 231
|
....*
gi 23397593 682 LVASQ 686
Cdd:cd03253 232 MWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
443-672 |
2.91e-91 |
|
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: 283.35 E-value: 2.91e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 443 GEVGFQNVFFTF-PTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRN 521
Cdd:cd03254 1 GEIEFENVNFSYdEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 522 NIGAVSQEPVLFSCSIRENILYGANpgeTPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARAL 601
Cdd:cd03254 78 MIGVVLQDTFLFSGTIMENIRLGRP---NATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELM 672
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
126-419 |
1.39e-86 |
|
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: 273.74 E-value: 1.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 126 GIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSA-AMAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLRSR 204
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEeALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 205 LYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAI 284
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 285 VYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFII 364
Cdd:cd18780 161 IYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 365 ISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18780 241 VLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
126-419 |
8.03e-82 |
|
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: 260.88 E-value: 8.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 126 GIGCLVVSSAITMSVPLFLGKVIDVVFnksgmDSAAMAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLRSRL 205
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAAL-----GGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 206 YRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAIV 285
Cdd:cd18576 76 YRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 286 YGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIII 365
Cdd:cd18576 156 FGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 23397593 366 SVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18576 236 AVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
447-661 |
3.35e-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: 252.30 E-value: 3.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPEsAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAV 526
Cdd:cd03228 3 FKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEPVLFSCSIRENILyganpgetpsperlqqviedanvsqftdqlpdgldtlvgqrgmmlSGGQKQRVAIARALIKNPA 606
Cdd:cd03228 82 PQDPFLFSGTIRENIL---------------------------------------------SGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 607 ILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGK 661
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
445-686 |
7.50e-79 |
|
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: 251.25 E-value: 7.50e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 445 VGFQNVFFTFptRPESA-VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNI 523
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 524 GAVSQEPVLFSCSIRENILYgANPGetPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIK 603
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIAL-ADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 604 NPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGiQEGVFRELV 683
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA-ENGLYAYLY 234
|
...
gi 23397593 684 ASQ 686
Cdd:cd03252 235 QLQ 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
443-662 |
1.15e-78 |
|
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: 250.47 E-value: 1.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 443 GEVGFQNVFFTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNN 522
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 523 IGAVSQEPVLFSCSIRENILYGAnpgETPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALI 602
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGL---QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 603 KNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKI 662
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
111-672 |
2.60e-77 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 258.88 E-value: 2.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 111 RLLSLTKSEKWVLTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSAAMAKLGEYSVLLFgifVLGGFANFARVHLF 190
Cdd:PRK10790 13 RLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLGLVAGLAAAYVGLQ---LLAAGLHYAQSLLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 191 GNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAA 270
Cdd:PRK10790 90 NRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 271 VSALVVPAMAGMAIVYGRY----VRRITKVeldkYAEIMKFAEERFGNVKTVKTFcREQqevAAFDGKLDEALQIGYKet 346
Cdd:PRK10790 170 VAIMIFPAVLVVMVIYQRYstpiVRRVRAY----LADINDGFNEVINGMSVIQQF-RQQ---ARFGERMGEASRSHYM-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 347 rARAIFFGLTGFCGN--FIIISVLYYGGTLVL-----QDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:PRK10790 240 -ARMQTLRLDGFLLRplLSLFSALILCGLLMLfgfsaSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 420 WEILDRECSiPIDKGVVPLEKpvGEVGFQNVffTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDP 499
Cdd:PRK10790 319 FELMDGPRQ-QYGNDDRPLQS--GRIDIDNV--SFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 500 QGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILYGANPGEtpspERLQQVIEDANVSQFTDQLPDGLDTL 579
Cdd:PRK10790 394 TEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISE----EQVWQALETVQLAELARSLPDGLYTP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 580 VGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSD 659
Cdd:PRK10790 470 LGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHR 549
|
570
....*....|...
gi 23397593 660 GKIVEQGSYNELM 672
Cdd:PRK10790 550 GQAVEQGTHQQLL 562
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
126-419 |
3.02e-75 |
|
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: 243.60 E-value: 3.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 126 GIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDsaamaKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLRSRL 205
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSRE-----AFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 206 YRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAIV 285
Cdd:cd18572 76 FRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 286 YGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIII 365
Cdd:cd18572 156 YGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 23397593 366 SVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18572 236 LVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
170-684 |
6.57e-73 |
|
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: 249.86 E-value: 6.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 170 VLLFGIFVLGGF-ANFARVHLFGNAALRIVRSLRS--RLYRSMLMQEVGWFDTKGTGELINRL-SNDTlmVGTSLS-QNV 244
Cdd:TIGR03796 195 PLLLGMGLTALLqGVLTWLQLYYLRRLEIKLAVGMsaRFLWHILRLPVRFFAQRHAGDIASRVqLNDQ--VAEFLSgQLA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 245 SDGLRSVAMIGVGTGMMIYtSPQLAavsaLVVPAMAGMAIVYGRYVRRiTKVELDkyaeiMKFAEER-------FGNVKT 317
Cdd:TIGR03796 273 TTALDAVMLVFYALLMLLY-DPVLT----LIGIAFAAINVLALQLVSR-RRVDAN-----RRLQQDAgkltgvaISGLQS 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 318 VKT----------FCReqqeVAAFDGKLDEALQ-IGYKETRARAIFFGLTGFCGnfiiISVLYYGGTLVLQDSLTIGALT 386
Cdd:TIGR03796 342 IETlkasglesdfFSR----WAGYQAKLLNAQQeLGVLTQILGVLPTLLTSLNS----ALILVVGGLRVMEGQLTIGMLV 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 387 AFMLYAGYVAISMNGLSNFYSQLNKGIGASERIWEILDRECSI------PIDKGVVPLEKPVGEVGFQNVFFTFpTRPES 460
Cdd:TIGR03796 414 AFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRNPVDPlleepeGSAATSEPPRRLSGYVELRNITFGY-SPLEP 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 461 AVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIREN 540
Cdd:TIGR03796 493 PLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDN 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 I-LYGAnpgeTPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDA 619
Cdd:TIGR03796 573 LtLWDP----TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDP 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 620 VSENLVqnaLDNLIQ-GRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGiQEGVFRELVA 684
Cdd:TIGR03796 649 ETEKII---DDNLRRrGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWA-VGGAYARLIR 710
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
443-667 |
1.66e-71 |
|
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: 231.23 E-value: 1.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 443 GEVGFQNVFFTFptRPESA-VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRN 521
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 522 NIGAVSQEPVLFSCSIRENIlygaNPGETPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARAL 601
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL----DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGS 667
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
443-666 |
3.11e-71 |
|
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: 230.55 E-value: 3.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 443 GEVGFQNVFFTFPTRpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNN 522
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 523 IGAVSQEPVLFSCSIRENILYGANPGETpspERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALI 602
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADD---ERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 603 KNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQG 666
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
130-682 |
5.74e-67 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 230.37 E-value: 5.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 130 LVVSSAITMSVPLFLGKVIDVVFNKSGMDSAAMAKLGeysVLLFGIFVLGGFANFARVHLFGnAALRIVRSLRSRLYRSM 209
Cdd:PRK10789 4 LIIIAMLQLIPPKVVGIIVDGVTEQHMTTGQILMWIG---TMVLIAVVVYLLRYVWRVLLFG-ASYQLAVELREDFYRQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 210 LMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAM-IGVGTGMMIYTSPQLAAVSALVVPAMAGMAIVYGR 288
Cdd:PRK10789 80 SRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMgCAVLIVMSTQISWQLTLLALLPMPVMAIMIKRYGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 289 YVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDgklDEALQIGYKETR-----AR---AIFFGLtGFcG 360
Cdd:PRK10789 160 QLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFA---ADAEDTGKKNMRvaridARfdpTIYIAI-GM-A 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 361 NFIIISvlyyGGT-LVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERIWEILDRECSIPIDKGVVPLE 439
Cdd:PRK10789 235 NLLAIG----GGSwMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 440 KPVGEVGFQNvfFTFPTRpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWL 519
Cdd:PRK10789 311 RGELDVNIRQ--FTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 520 RNNIGAVSQEPVLFSCSIRENILYGaNPGETPspERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIAR 599
Cdd:PRK10789 388 RSRLAVVSQTPFLFSDTVANNIALG-RPDATQ--QEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIAR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 600 ALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGiQEGVF 679
Cdd:PRK10789 465 ALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ-QSGWY 543
|
...
gi 23397593 680 REL 682
Cdd:PRK10789 544 RDM 546
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
121-686 |
6.28e-67 |
|
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: 232.92 E-value: 6.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 121 WVLTAGigclVVSSAITMSVPLFLGKVIDVVFNKSgmDSAAMAKLGeysvllfgiFVLGGFAnfarvhlFGNAALRIVRS 200
Cdd:TIGR03797 140 AILAMG----LLGTLLGMLVPIATGILIGTAIPDA--DRSLLVQIA---------LALLAAA-------VGAAAFQLAQS 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 201 L-------------RSRLYRSMLMQEVGWFDTKGTGELINRLSNDT----LMVGTSLSQNVSdGLRSVAMIGVgtgmMIY 263
Cdd:TIGR03797 198 LavlrletrmdaslQAAVWDRLLRLPVSFFRQYSTGDLASRAMGISqirrILSGSTLTTLLS-GIFALLNLGL----MFY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 264 TSPQLAAVS-ALVVPAMAGMAIVYGRYVRRITK-VELDkyAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQI 341
Cdd:TIGR03797 273 YSWKLALVAvALALVAIAVTLVLGLLQVRKERRlLELS--GKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 342 gykETRARAIFFGLTGFCGNFIIIS---VLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASER 418
Cdd:TIGR03797 351 ---ELSAQRIENLLTVFNAVLPVLTsaaLFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWER 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 419 IWEILDRECSIPIDKgvVPLEKPVGEVGFQNVFFTFptRPES-AVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLY 497
Cdd:TIGR03797 428 AKPILEALPEVDEAK--TDPGKLSGAIEVDRVTFRY--RPDGpLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 498 DPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILyGANPgetPSPERLQQVIEDANVSQFTDQLPDGLD 577
Cdd:TIGR03797 504 TPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAP---LTLDEAWEAARMAGLAEDIRAMPMGMH 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 578 TLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVltIAHRLSTIRNADQIAVL 657
Cdd:TIGR03797 580 TVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTRIV--IAHRLSTIRNADRIYVL 657
|
570 580
....*....|....*....|....*....
gi 23397593 658 SDGKIVEQGSYNELMGiQEGVFRELVASQ 686
Cdd:TIGR03797 658 DAGRVVQQGTYDELMA-REGLFAQLARRQ 685
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
101-683 |
1.04e-66 |
|
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: 233.09 E-value: 1.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 101 PVKMGRSQYGRLLSLTKSEK----WVLTAGIGCLVVSSAITmsvpLFLGKVIDVVFNKSGMDSaamakLGEYSVLLFGIF 176
Cdd:TIGR01193 136 PIKEKENSLLKFIPLITRQKklivNIVIAAIIVTLISIAGS----YYLQKIIDTYIPHKMMGT-----LGIISIGLIIAY 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 177 VLGGFANFARVHLFGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGV 256
Cdd:TIGR01193 207 IIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 257 GTgMMIYTSPQLAAVSALVVPAMAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLD 336
Cdd:TIGR01193 287 GL-FLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFG 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 337 EALQIGYKETRARAIFFGLTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGAS 416
Cdd:TIGR01193 366 DYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVAN 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 417 ERIWEILDRECSIPIDKGVVPLEKPVGEVGFQNVFFTFPTrpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRL 496
Cdd:TIGR01193 446 NRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 497 YDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILYGANPGETPspERLQQVIEDANVSQFTDQLPDGL 576
Cdd:TIGR01193 524 FQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQ--DEIWAACEIAEIKDDIENMPLGY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 577 DTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLiQGRTVLTIAHRLSTIRNADQIAV 656
Cdd:TIGR01193 602 QTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIV 680
|
570 580
....*....|....*....|....*..
gi 23397593 657 LSDGKIVEQGSYNELMgIQEGVFRELV 683
Cdd:TIGR01193 681 LDHGKIIEQGSHDELL-DRNGFYASLI 706
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
123-419 |
8.39e-66 |
|
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: 218.96 E-value: 8.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKsgmdsAAMAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLR 202
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPA-----GDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 203 SRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGM 282
Cdd:cd07346 76 RDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 283 AIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNF 362
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 363 IIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd07346 236 GTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
129-419 |
1.64e-64 |
|
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: 215.43 E-value: 1.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 129 CLVVSSAITMSVPLFLGKVIDvvfnkSGMDSAAMAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLRSRLYRS 208
Cdd:cd18575 4 ALLIAAAATLALGQGLRLLID-----QGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 209 MLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAIVYGR 288
Cdd:cd18575 79 LLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 289 YVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIIISVL 368
Cdd:cd18575 159 RVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 23397593 369 YYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18575 239 WLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
123-395 |
3.42e-64 |
|
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: 214.04 E-value: 3.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSAAMAKlgeYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLR 202
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNV---YSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 203 SRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGM 282
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 283 AIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNF 362
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|...
gi 23397593 363 IIISVLYYGGTLVLQDSLTIGALTAFMLYAGYV 395
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGDLVAFLSLFAQL 270
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
143-657 |
1.19e-63 |
|
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: 220.24 E-value: 1.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 143 FLGKVIDVVFnksgMDSAAMAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGT 222
Cdd:TIGR02857 25 LLARVVDGLI----SAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 223 GELInrlsndTLMVgtslsQNVSD----------GLRSVAMIGVGTGMMIYT-SPQLAAVSALVVPAMAGMAIVYGRYVR 291
Cdd:TIGR02857 101 GELA------TLAL-----EGVEAldgyfarylpQLVLAVIVPLAILAAVFPqDWISGLILLLTAPLIPIFMILIGWAAQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 292 RITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDgKLDEALQigyKETRA--RAIFfgLTGFCGNFI-IISVL 368
Cdd:TIGR02857 170 AAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIR-RSSEEYR---ERTMRvlRIAF--LSSAVLELFaTLSVA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 369 ---------YYGGTLVLQDSLTIgaltafMLYAGYVAISMNGLSNFYSQLNKGIGASERIWEILDRECSIPIDKGVVPlE 439
Cdd:TIGR02857 244 lvavyigfrLLAGDLDLATGLFV------LLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVT-A 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 440 KPVGEVGFQNVFFTFPTRPesAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWL 519
Cdd:TIGR02857 317 APASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 520 RNNIGAVSQEPVLFSCSIRENILYGANPGetpSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIAR 599
Cdd:TIGR02857 395 RDQIAWVPQHPFLFAGTIAENIRLARPDA---SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALAR 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 600 ALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVL 657
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
402-684 |
6.36e-63 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 219.72 E-value: 6.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 402 LSNFYSQLNKGIGASERIWEILDRECSIPIDKGV-VPLEKPVgEVGFQNVFFTfptRPESAVLTD-FSLNLMPGTTTAVV 479
Cdd:PRK11174 307 LGTFYHAKAQAVGAAESLVTFLETPLAHPQQGEKeLASNDPV-TIEAEDLEIL---SPDGKTLAGpLNFTLPAGQRIALV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 480 GRSGSGKTTIaLLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILYGAnpgETPSPERLQQV 559
Cdd:PRK11174 383 GPSGAGKTSL-LNALLGFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN---PDASDEQLQQA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 560 IEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVL 639
Cdd:PRK11174 459 LENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTL 538
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 23397593 640 TIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGiQEGVFRELVA 684
Cdd:PRK11174 539 MVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQ-AGGLFATLLA 582
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
123-419 |
3.71e-58 |
|
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: 198.42 E-value: 3.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSAAMAklgeySVLLFGIFVLGGFANFARVHLFGNAALRIVRSLR 202
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLV-----PLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 203 SRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGM 282
Cdd:cd18552 76 NDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 283 AIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNF 362
Cdd:cd18552 156 IRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAI 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 363 IIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18552 236 AIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
349-687 |
1.01e-57 |
|
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: 204.98 E-value: 1.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 349 RAIFFG-LTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYV------AISMnglsnfYSQLNKGIGASERIWE 421
Cdd:COG4618 237 RAGGFSaLSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIAASILMGRAlapieqAIGG------WKQFVSARQAYRRLNE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 422 ILDrecSIPIDKGVVPLEKPVGEVGFQNVFFTFPTRpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQG 501
Cdd:COG4618 311 LLA---AVPAEPERMPLPRPKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTA 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 502 GTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENIlygANPGEtPSPERlqqVIEDA---NVSQFTDQLPDGLDT 578
Cdd:COG4618 387 GSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI---ARFGD-ADPEK---VVAAAklaGVHEMILRLPDGYDT 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 579 LVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNL-IQGRTVLTIAHRLSTIRNADQIAVL 657
Cdd:COG4618 460 RIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVL 539
|
330 340 350
....*....|....*....|....*....|
gi 23397593 658 SDGKIVEQGSYNElmgiqegVFRELVASQA 687
Cdd:COG4618 540 RDGRVQAFGPRDE-------VLARLARPAA 562
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
193-645 |
7.42e-57 |
|
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: 201.82 E-value: 7.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 193 AALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLA--- 269
Cdd:TIGR02868 80 AALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAAlil 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 270 ----AVSALVVPA-------MAGMAIVYGR--YVRRITKVeLDKYAEIMKFAeerfgnvktvktfcREQQEVAAFDGKLD 336
Cdd:TIGR02868 160 aaglLLAGFVAPLvslraarAAEQALARLRgeLAAQLTDA-LDGAAELVASG--------------ALPAALAQVEEADR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 337 EALQIGYKETRARAIFFGLTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGAS 416
Cdd:TIGR02868 225 ELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 417 ERIWEILDREcsIPIDKGVVPLEKPVGEVG----FQNVFFTFPTRPEsaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALL 492
Cdd:TIGR02868 305 ERIVEVLDAA--GPVAEGSAPAAGAVGLGKptleLRDLSAGYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLAT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 493 MLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILYGAnpgETPSPERLQQVIEDANVSQFTDQL 572
Cdd:TIGR02868 381 LAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLAR---PDATDEELWAALERVGLADWLRAL 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 573 PDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDA-VSENLVQNALDNLiQGRTVLTIAHRL 645
Cdd:TIGR02868 458 PDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAeTADELLEDLLAAL-SGRTVVLITHHL 530
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
115-659 |
6.32e-56 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 207.19 E-value: 6.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 115 LTKSEKWVLTAGIGCLVVSSAitmSVPLFLgKVIDVVFNKsgmdsaamAKLGE------YSVLLFGI--FVLGGFANFAr 186
Cdd:PTZ00265 54 LPASHRKLLGVSFVCATISGG---TLPFFV-SVFGVIMKN--------MNLGEnvndiiFSLVLIGIfqFILSFISSFC- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 187 vhlFGNAALRIVRSLRSRLYRSMLMQEvGWFDTKGTGeliNRLSNDtlmVGTSLSQ-NVSDGLRSVAMIGVGTGMM---- 261
Cdd:PTZ00265 121 ---MDVVTTKILKTLKLEFLKSVFYQD-GQFHDNNPG---SKLTSD---LDFYLEQvNAGIGTKFITIFTYASAFLglyi 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 262 --IYTSPQLAAVSALVVPAMAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDgkLDEAL 339
Cdd:PTZ00265 191 wsLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFN--LSEKL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 340 QIGY--KETRARAIFFGL-TGFC----------GNFIIISVL--------YYGGTLVlqdSLTIGAL-TAFMLyagyvAI 397
Cdd:PTZ00265 269 YSKYilKANFMESLHIGMiNGFIlasyafgfwyGTRIIISDLsnqqpnndFHGGSVI---SILLGVLiSMFML-----TI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 398 SMNGLSNFYsqlnKGIGASERIWEILDRECSIPIDKGVVPLeKPVGEVGFQNVFFTFPTRPESAVLTDFSLNLMPGTTTA 477
Cdd:PTZ00265 341 ILPNITEYM----KSLEATNSLYEIINRKPLVENNDDGKKL-KDIKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYA 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 478 VVGRSGSGKTTIALLMLRLYDPQGGTVHL-DGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILY------------- 543
Cdd:PTZ00265 416 FVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsn 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 544 -----------GANPGE----------------TPSPERLQ-----QVIEDA---NVSQ------FTDQLPDGLDTLVGQ 582
Cdd:PTZ00265 496 yynedgndsqeNKNKRNscrakcagdlndmsntTDSNELIEmrknyQTIKDSevvDVSKkvlihdFVSALPDKYETLVGS 575
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23397593 583 RGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLI--QGRTVLTIAHRLSTIRNADQIAVLSD 659
Cdd:PTZ00265 576 NASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
358-682 |
2.96e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 198.51 E-value: 2.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 358 FCGNFIIISVLYYGGTLVLQDSLTiGALTAFMLYAGYVAISMNG-LSNFYSQLNKGIGASERIWEILDRECSIPIDkGVV 436
Cdd:PRK11160 253 LANGLTVVLMLWLAAGGVGGNAQP-GALIALFVFAALAAFEALMpVAGAFQHLGQVIASARRINEITEQKPEVTFP-TTS 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 437 PLEKPVGEVGFQNVFFTFPTRPESaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNP 516
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYPDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 517 QWLRNNIGAVSQEPVLFSCSIRENILYGAnpgETPSPERLQQVIEDANVSQFTDQlPDGLDTLVGQRGMMLSGGQKQRVA 596
Cdd:PRK11160 410 AALRQAISVVSQRVHLFSATLRDNLLLAA---PNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLG 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 597 IARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGiQE 676
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLA-QQ 564
|
....*.
gi 23397593 677 GVFREL 682
Cdd:PRK11160 565 GRYYQL 570
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
123-419 |
1.40e-54 |
|
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: 188.80 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGmdsaamakLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLR 202
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGS--------SGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 203 SRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGM 282
Cdd:cd18551 73 RRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 283 AIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNF 362
Cdd:cd18551 153 ILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 363 IIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18551 233 ALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
196-683 |
1.45e-54 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 202.95 E-value: 1.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 196 RIVRSLRSRLYRSMLMQEVGWFD--TKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVsa 273
Cdd:PTZ00265 896 KVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAV-- 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 274 lvvpaMAGMAIVYGRY--VR-RITK-VELDKYA--------------EIMK----FAEERFGNVKTVKTFCREQQEVAAF 331
Cdd:PTZ00265 974 -----LTGTYFIFMRVfaIRaRLTAnKDVEKKEinqpgtvfaynsddEIFKdpsfLIQEAFYNMNTVIIYGLEDYFCNLI 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 332 DGKLDEALQIGYKETRARAIFFGLTGFCGNFIIISVLYYGGTLVLQDSLTIG----ALTAFMLYAGYVA--ISMNGLSNf 405
Cdd:PTZ00265 1049 EKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDdfmkSLFTFLFTGSYAGklMSLKGDSE- 1127
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 406 ysqlNKGIgASERIWEILDRECSIPI-DKGVVPLEKP---VGEVGFQNVFFTFPTRPESAVLTDFSLNLMPGTTTAVVGR 481
Cdd:PTZ00265 1128 ----NAKL-SFEKYYPLIIRKSNIDVrDNGGIRIKNKndiKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGE 1202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 482 SGSGKTTIALLMLRLYD----------------------PQG--------------------------------GTVHLD 507
Cdd:PTZ00265 1203 TGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdYQGdeeqnvgmknvnefsltkeggsgedstvfknsGKILLD 1282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 508 GIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENILYGAnpgETPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMML 587
Cdd:PTZ00265 1283 GVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGK---EDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSL 1359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 588 SGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRNADQIAVLSD----GK 661
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGS 1439
|
570 580
....*....|....*....|...
gi 23397593 662 IVE-QGSYNELMGIQEGVFRELV 683
Cdd:PTZ00265 1440 FVQaHGTHEELLSVQDGVYKKYV 1462
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
164-679 |
2.46e-53 |
|
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: 199.40 E-value: 2.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 164 KLGEYSVLlfGIfvLGGFANFARVHLFGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQN 243
Cdd:TIGR00957 1007 RLSVYGAL--GI--LQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPV 1082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 244 VSDGLRSVAMIgVGTGMMIYTSPQLAAVsalVVPAMAGMAIVYGRYV----RRITKVELDKYAEIMKFAEERFGNVKTVK 319
Cdd:TIGR00957 1083 IKMFMGSLFNV-IGALIVILLATPIAAV---IIPPLGLLYFFVQRFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIR 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 320 TFCREQQEVAAFDGKLDEALQIGYKETRA-RAIFFGLTgFCGNFIIISVLYYGgtLVLQDSLTIGALTAFMLYAGYVAIS 398
Cdd:TIGR00957 1159 AFEEQERFIHQSDLKVDENQKAYYPSIVAnRWLAVRLE-CVGNCIVLFAALFA--VISRHSLSAGLVGLSVSYSLQVTFY 1235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 399 MNGLSNFYSQLNKGIGASERIWEILDRECSIP-IDKGVVPLEK--PVGEVGFQNvfFTFPTRPE-SAVLTDFSLNLMPGT 474
Cdd:TIGR00957 1236 LNWLVRMSSEMETNIVAVERLKEYSETEKEAPwQIQETAPPSGwpPRGRVEFRN--YCLRYREDlDLVLRHINVTIHGGE 1313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 475 TTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENIlygaNPGETPSPE 554
Cdd:TIGR00957 1314 KVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL----DPFSQYSDE 1389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 555 RLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ 634
Cdd:TIGR00957 1390 EVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE 1469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 23397593 635 GRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGiQEGVF 679
Cdd:TIGR00957 1470 DCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ-QRGIF 1513
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
123-419 |
3.43e-53 |
|
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: 185.37 E-value: 3.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVvFNKSGMDSAA----MAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIV 198
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDA-FTDFGSGESSpdefLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 199 RSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPA 278
Cdd:cd18577 80 RRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 279 MAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGF 358
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFF 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 359 CGNFIIISVLYYGGTLVLQDSLTIGA-LTAFM--LYAgyvAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18577 240 IIFAMYALAFWYGSRLVRDGEISPGDvLTVFFavLIG---AFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
113-429 |
1.04e-50 |
|
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: 179.18 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 113 LSLTKSEKWVLTAGIGCLVVSSAITmsvPLF---LGKVIDVvFNKSGmDSAAMAKLGEYSVLLFGIFVLGGFANFARVHL 189
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVF---PVFailFSKLISV-FSLPD-DDELRSEANFWALMFLVLAIVAGIAYFLQGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 190 FGNAALRIVRSLRSRLYRSMLMQEVGWFDTKG--TGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQ 267
Cdd:cd18578 76 FGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 268 LAAVSALVVPAMAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETR 347
Cdd:cd18578 156 LALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 348 ARAIFFGLTGFCGNFIIISVLYYGGTLVLQDSLTIGA-LTAFM--LYAgyvAISMNGLSNFYSQLNKGIGASERIWEILD 424
Cdd:cd18578 236 ISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQfFIVFMalIFG---AQSAGQAFSFAPDIAKAKAAAARIFRLLD 312
|
....*
gi 23397593 425 RECSI 429
Cdd:cd18578 313 RKPEI 317
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
349-662 |
1.21e-50 |
|
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: 184.86 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 349 RAIFFG-LTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERIWEILDREc 427
Cdd:TIGR01842 223 RAGMLSnLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANY- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 428 siPIDKGVVPLEKPVGEVGFQNVFFTfPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLD 507
Cdd:TIGR01842 302 --PSRDPAMPLPEPEGHLSVENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 508 GIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENIlygANPGETPSPErlqQVIEDANVSQFTD---QLPDGLDTLVGQRG 584
Cdd:TIGR01842 379 GADLKQWDRETFGKHIGYLPQDVELFPGTVAENI---ARFGENADPE---KIIEAAKLAGVHElilRLPDGYDTVIGPGG 452
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23397593 585 MMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNL-IQGRTVLTIAHRLSTIRNADQIAVLSDGKI 662
Cdd:TIGR01842 453 ATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
123-419 |
1.65e-50 |
|
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: 177.62 E-value: 1.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDsaamaKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLR 202
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRE-----LLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 203 SRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGM 282
Cdd:cd18542 76 NDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 283 AIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNF 362
Cdd:cd18542 156 SYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 363 IIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18542 236 QIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
123-419 |
1.32e-49 |
|
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: 175.28 E-value: 1.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVVFN-KSGMDSAAMAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSL 201
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEgLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 202 RSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAG 281
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 282 MAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKetrarAIFFG-----LT 356
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFK-----AQFYSgllmpIM 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397593 357 GFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18547 236 NFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
123-419 |
3.95e-49 |
|
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: 173.75 E-value: 3.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSgmdsAAMAKLGEYSVLLFGIFVLGGFANFA-RVHLFGnAALRIVRSL 201
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGT----LTASQLLRYALLILLLALLIGIFRFLwRYLIFG-ASRRIEYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 202 RSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAG 281
Cdd:cd18541 76 RNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 282 MAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGN 361
Cdd:cd18541 156 LVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 362 FIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18541 236 LSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
123-419 |
4.17e-49 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 173.73 E-value: 4.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSAAMAKLGeysVLLFGIFVLGGFANFARVHLFGNAALRIVRSLR 202
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLLA---LLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 203 SRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGM 282
Cdd:cd18544 78 RDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 283 AIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNF 362
Cdd:cd18544 158 TYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 363 IIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18544 238 ALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
447-667 |
4.36e-48 |
|
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: 177.02 E-value: 4.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPESAV--LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQ---WLRN 521
Cdd:COG1123 263 VRNLSKRYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 522 NIGAVSQEPvlFSC-----SIRENILYGA-NPGETPSPERLQQVIE--DAnVsqftdqlpdGLDTLVGQR-GMMLSGGQK 592
Cdd:COG1123 343 RVQMVFQDP--YSSlnprmTVGDIIAEPLrLHGLLSRAERRERVAEllER-V---------GLPPDLADRyPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 593 QRVAIARALIKNPAILILDEATSALDaVSenlVQNALDNLIQ------GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQ 665
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALD-VS---VQAQILNLLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVED 486
|
..
gi 23397593 666 GS 667
Cdd:COG1123 487 GP 488
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
448-662 |
4.82e-48 |
|
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: 166.62 E-value: 4.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVS 527
Cdd:cd03246 4 ENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 528 QEPVLFSCSIRENILyganpgetpsperlqqviedanvsqftdqlpdgldtlvgqrgmmlSGGQKQRVAIARALIKNPAI 607
Cdd:cd03246 83 QDDELFSGSIAENIL---------------------------------------------SGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 608 LILDEATSALDAVSENLVQNALDNL-IQGRTVLTIAHRLSTIRNADQIAVLSDGKI 662
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
445-661 |
5.29e-48 |
|
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: 167.65 E-value: 5.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 445 VGFQNVFFTFPTRPESA--VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGidlrtvnpqwlrnN 522
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 523 IGAVSQEPVLFSCSIRENILYGAnpgetP-SPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARAL 601
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGK-----PfDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 602 IKNPAILILDEATSALDA-VSENLVQNAL-DNLIQGRTVLTIAHRLSTIRNADQIAVLSDGK 661
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAhVGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
127-419 |
2.27e-47 |
|
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: 169.26 E-value: 2.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 127 IGCLVVSSAITMSVPLFLGKVIDVVFN-KSGMDSAAMAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLRSRL 205
Cdd:cd18574 2 VLSALAAALVNIQIPLLLGDLVNVISRsLKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 206 YRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAIV 285
Cdd:cd18574 82 FSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 286 YGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIII 365
Cdd:cd18574 162 YGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGLSNLALNGIVL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 23397593 366 SVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18574 242 GVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
447-672 |
4.02e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 166.35 E-value: 4.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPtrPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAV 526
Cdd:COG1122 3 LENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEPV--LFSCSIRENILYG-ANPGETPS--PERLQQVIEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIARAL 601
Cdd:COG1122 81 FQNPDdqLFAPTVEEDVAFGpENLGLPREeiRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNELM 672
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
453-666 |
8.51e-47 |
|
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: 165.37 E-value: 8.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 453 TFPTRPES-AVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWL---RNNIGAVSQ 528
Cdd:cd03257 10 SFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 529 EPvlFSC-----SIRENILYGANPGETPSPERLQQVIEDANVSQFTDqLPDGLDTLVGQrgmmLSGGQKQRVAIARALIK 603
Cdd:cd03257 90 DP--MSSlnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGL-PEEVLNRYPHE----LSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 604 NPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQG 666
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
448-688 |
6.17e-45 |
|
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: 160.74 E-value: 6.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRPES-AVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAV 526
Cdd:COG1124 5 RNLSVSYGQGGRRvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEPvlfscsirenilYGA-NPGETpsperLQQVIEDANVSQFTDQLPDGLDTLVGQRGM----------MLSGGQKQRV 595
Cdd:COG1124 85 FQDP------------YASlHPRHT-----VDRILAEPLRIHGLPDREERIAELLEQVGLppsfldryphQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 596 AIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNELM 672
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*...
gi 23397593 673 -GIQEGVFRELV-ASQAF 688
Cdd:COG1124 228 aGPKHPYTRELLaASLAF 245
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
130-419 |
2.15e-44 |
|
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: 160.94 E-value: 2.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 130 LVVSSAITMSVPLFLGKVID-VVFNKSgMDSAAMAklgeysVLLFGIFVLG-GFANFARVHLFGNAALRIVRSLRSRLYR 207
Cdd:cd18784 5 LLAAAVGEIFIPYYTGQVIDgIVIEKS-QDKFSRA------IIIMGLLAIAsSVAAGIRGGLFTLAMARLNIRIRNLLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 208 SMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRS-VAMIGVgTGMMIYTSPQLAAVSALVVPAMAGMAIVY 286
Cdd:cd18784 78 SIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSlVKAIGV-IVFMFKLSWQLSLVTLIGLPLIAIVSKVY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 287 GRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDgkldEALQIGYKETRARAIFFG----LTGFCGNF 362
Cdd:cd18784 157 GDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYS----EKLKDTYKLKIKEALAYGgyvwSNELTELA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 363 IIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18784 233 LTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
443-667 |
3.71e-44 |
|
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: 157.57 E-value: 3.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 443 GEVGFQNVFFTF-PTRPEsaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRN 521
Cdd:cd03369 5 GEIEVENLSVRYaPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 522 NIGAVSQEPVLFSCSIRENIlygaNPGETPSPERLQQVIEdanvsqftdqlpdgldtlVGQRGMMLSGGQKQRVAIARAL 601
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL----DPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGS 667
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
447-673 |
3.84e-44 |
|
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: 165.85 E-value: 3.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPESAVlTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQG---GTVHLDGIDLRTVNPQWLRNNI 523
Cdd:COG1123 7 VRDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 524 GAVSQEP--VLFSCSIRENILYGANPGETPSPERLQQVIEDANVSqftdqlpdGLDTLVGQRGMMLSGGQKQRVAIARAL 601
Cdd:COG1123 86 GMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAV--------GLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNELMG 673
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
462-683 |
3.88e-44 |
|
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: 158.92 E-value: 3.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENI 541
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 542 lygaNPGETPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVS 621
Cdd:cd03288 116 ----DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 622 ENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGIQEGVFRELV 683
Cdd:cd03288 192 ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
447-662 |
4.01e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 157.29 E-value: 4.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAV 526
Cdd:COG4619 3 LEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEPVLFSCSIRENILYGAN-PGETPSPERLQQVIEDANVSqftdqlPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNP 605
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQlRERKFDRERALELLERLGLP------PDILDKPVER----LSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 606 AILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTI-RNADQIAVLSDGKI 662
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHDPEQIeRVADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
462-687 |
5.53e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.92 E-value: 5.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTvNPQWLRNNIGAVSQEPVLF-SCSIREN 540
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYpDLTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 I-----LYGANPGEtpSPERLQQVIEDANvsqftdqLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:COG1131 94 LrffarLYGLPRKE--ARERIDELLELFG-------LTDAADRKVGT----LSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 616 ALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNELMGIQ-EGVFRELVASQA 687
Cdd:COG1131 161 GLDPEARRELWELLRELAaEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARLlEDVFLELTGEEA 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
447-661 |
4.06e-43 |
|
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: 154.55 E-value: 4.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAV 526
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEP--VLFSCSIRENILYGA-NPGETPS--PERLQQVIEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIARAL 601
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLeNLGLPEEeiEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIRN-ADQIAVLSDGK 661
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
448-671 |
4.22e-42 |
|
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: 153.09 E-value: 4.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTvNPQWLRNNIGAVS 527
Cdd:COG4555 5 ENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 528 QEPVLFS-CSIRENI-----LYGANPGETPspERLQQVIEDAnvsqftdQLPDGLDTLVGQrgmmLSGGQKQRVAIARAL 601
Cdd:COG4555 81 DERGLYDrLTVRENIryfaeLYGLFDEELK--KRIEELIELL-------GLEEFLDRRVGE----LSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNEL 671
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
463-615 |
6.41e-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: 148.95 E-value: 6.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFS-CSIRENI 541
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 542 LYGANPGETPSPERLQQVIEDANvsqfTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALE----KLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
123-419 |
2.70e-41 |
|
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: 152.31 E-value: 2.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVVFNksgmDSAAMAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLR 202
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTI----GSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 203 SRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGM 282
Cdd:cd18778 77 SDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 283 AIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNF 362
Cdd:cd18778 157 AWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 363 IIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18778 237 GTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
459-671 |
3.58e-41 |
|
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: 149.64 E-value: 3.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYD-----PQGGTVHLDGIDLRT--VNPQWLRNNIGAVSQEPV 531
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVLELRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 532 LFSCSIRENILYGANPGETPSPERLQQVIEDAnvsqftdqLPD-GLDTLVGQR--GMMLSGGQKQRVAIARALIKNPAIL 608
Cdd:cd03260 92 PFPGSIYDNVAYGLRLHGIKLKEELDERVEEA--------LRKaALWDEVKDRlhALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 609 ILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNEL 671
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
447-666 |
5.17e-41 |
|
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: 147.46 E-value: 5.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwLRNNIGAV 526
Cdd:cd03247 3 INNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEPVLFSCSIRENIlyganpgetpsperlqqviedanvsqftdqlpdgldtlvgqrGMMLSGGQKQRVAIARALIKNPA 606
Cdd:cd03247 81 NQRPYLFDTTLRNNL------------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 607 ILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQG 666
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
447-672 |
7.70e-41 |
|
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: 149.36 E-value: 7.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNP---QWLRNNI 523
Cdd:COG1127 8 VRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 524 GAVSQEPVLF-SCSIRENILYganP----GETPSPERLQQV---IEDANVSQFTDQLPDGldtlvgqrgmmLSGGQKQRV 595
Cdd:COG1127 85 GMLFQGGALFdSLTVFENVAF---PlrehTDLSEAEIRELVlekLELVGLPGAADKMPSE-----------LSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 596 AIARALIKNPAILILDEATSALDAVSenlvQNALDNLIQ------GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSY 668
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPIT----SAVIDELIRelrdelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTP 226
|
....
gi 23397593 669 NELM 672
Cdd:COG1127 227 EELL 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
447-676 |
1.16e-40 |
|
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: 148.80 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNP---QWLRNNI 523
Cdd:cd03261 3 LRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 524 GAVSQEPVLF-SCSIRENILY-----GANPgETPSPERLQQVIEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAI 597
Cdd:cd03261 80 GMLFQSGALFdSLTVFENVAFplrehTRLS-EEEIREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 598 ARALIKNPAILILDEATSALDAVSenlvQNALDNLIQ------GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNE 670
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIA----SGVIDDLIRslkkelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEE 223
|
....*.
gi 23397593 671 LMGIQE 676
Cdd:cd03261 224 LRASDD 229
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
123-419 |
1.58e-40 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 150.35 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDsAAMAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLR 202
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPG-GNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 203 SRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIgVGTG-MMIYTSPQLAAVSALVVPAMAG 281
Cdd:cd18563 80 RDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMI-IGIGvVLFSLNWKLALLVLIPVPLVVW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 282 MAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGN 361
Cdd:cd18563 159 GSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 362 FIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18563 239 LGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
447-676 |
6.29e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 147.58 E-value: 6.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFP--TRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDlrTVNPQ--W-LRN 521
Cdd:TIGR04520 3 VENVSFSYPesEKP---ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEEnlWeIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 522 NIGAVSQEP------------VLFSCsirENIlyGANPGETPspERLQQVIEDANVSQFTDQLPDgldtlvgqrgmMLSG 589
Cdd:TIGR04520 78 KVGMVFQNPdnqfvgatveddVAFGL---ENL--GVPREEMR--KRVDEALKLVGMEDFRDREPH-----------LLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 590 GQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLI--QGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGS 667
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
....*....
gi 23397593 668 YNELMGIQE 676
Cdd:TIGR04520 220 PREIFSQVE 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
456-666 |
9.44e-40 |
|
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: 145.35 E-value: 9.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 456 TRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwlRNNIGAVSQEPVLF-S 534
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFpH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENILYGANPGETPSPERLQQVIEDAnvsqftDQLpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEAT 614
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKAEIRARVRELL------ELV--GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 615 SALDAVSENLVQNALDNLI--QGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQG 666
Cdd:cd03259 159 SALDAKLREELREELKELQreLGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
448-672 |
1.31e-39 |
|
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: 146.34 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVS 527
Cdd:COG1120 5 ENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 528 QEPVL-FSCSIRENILYGANP----GETPSPERLQQV---IEDANVSQFTDQLpdgLDTLvgqrgmmlSGGQKQRVAIAR 599
Cdd:COG1120 82 QEPPApFGLTVRELVALGRYPhlglFGRPSAEDREAVeeaLERTGLEHLADRP---VDEL--------SGGERQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 600 ALIKNPAILILDEATSALDavsenlVQNALD--NLI------QGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNE 670
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLD------LAHQLEvlELLrrlareRGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEE 224
|
..
gi 23397593 671 LM 672
Cdd:COG1120 225 VL 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
447-671 |
2.64e-39 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 144.65 E-value: 2.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPESA-VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRN---N 522
Cdd:cd03258 4 LKNVSKVFGDTGGKVtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKarrR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 523 IGAVSQEPVLFSC-SIRENILYGANPGETPSPERLQQV---IEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIA 598
Cdd:cd03258 84 IGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVlelLELVGLEDKADAYPA-----------QLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 599 RALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNEL 671
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
447-665 |
6.07e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 143.65 E-value: 6.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPES-AVLTDFSLNLMPGTTTAVVGRSGSGKTT----IALLMlrlyDPQGGTVHLDGIDLRTVNP----Q 517
Cdd:COG1136 7 LRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTllniLGGLD----RPTSGEVLIDGQDISSLSErelaR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 518 WLRNNIGAVSQE----PVLfscSIRENILYGANPGETPSPERLQQVIEdanvsqFTDQLpdGLDTLVGQRGMMLSGGQKQ 593
Cdd:COG1136 83 LRRRHIGFVFQFfnllPEL---TALENVALPLLLAGVSRKERRERARE------LLERV--GLGDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 594 RVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRNADQIAVLSDGKIVEQ 665
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
447-661 |
7.11e-38 |
|
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: 138.15 E-value: 7.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAV 526
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQepvlfscsirenilyganpgetpsperlqqviedanvsqftdqlpdgldtlvgqrgmmLSGGQKQRVAIARALIKNPA 606
Cdd:cd00267 79 PQ----------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 607 ILILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLSTIRNA-DQIAVLSDGK 661
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
168-685 |
7.39e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 152.05 E-value: 7.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 168 YSVLLFGIFVLGGFA-NFARVHLFGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDtlmVGtSLSQNVSD 246
Cdd:PLN03232 951 FYIVVYALLGFGQVAvTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKD---IG-DIDRNVAN 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 247 G-----------LRSVAMIGvgtgmmIYTSPQLAAVSALVVPAMAgmAIVY----GRYVRRITKVELDK-YAEimkFAEE 310
Cdd:PLN03232 1027 LmnmfmnqlwqlLSTFALIG------TVSTISLWAIMPLLILFYA--AYLYyqstSREVRRLDSVTRSPiYAQ---FGEA 1095
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 311 RFG--NVKTVKTFCReqqeVAAFDGK-LDEALQIGYKETRA-RAIFFGLTGFCGNFIII----SVLYYGGTlvlQDSLTI 382
Cdd:PLN03232 1096 LNGlsSIRAYKAYDR----MAKINGKsMDNNIRFTLANTSSnRWLTIRLETLGGVMIWLtatfAVLRNGNA---ENQAGF 1168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 383 GALTAFML-YAGYVAISMNGLSNFYSQLNKGIGASERIWEILDRECSIP-IDKGVVPLEK-PV-GEVGFQNVFFTFptRP 458
Cdd:PLN03232 1169 ASTMGLLLsYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATaIIENNRPVSGwPSrGSIKFEDVHLRY--RP 1246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 E-SAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSI 537
Cdd:PLN03232 1247 GlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTV 1326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 538 RENIlygaNPGETPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSAL 617
Cdd:PLN03232 1327 RFNI----DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 618 DAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGIQEGVFRELVAS 685
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
123-419 |
7.79e-38 |
|
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: 142.61 E-value: 7.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSaamakLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLR 202
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSG-----LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 203 SRLYRSMLMQEVGWFDTKGTGELINRLSNDTlmvgTSLSQNVSDGLRSVAM-----IGVgTGMMIYTSPQLAAVSALVVP 277
Cdd:cd18545 77 QDLFSHLQKLSFSFFDSRPVGKILSRVINDV----NSLSDLLSNGLINLIPdlltlVGI-VIIMFSLNVRLALVTLAVLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 278 AMAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTG 357
Cdd:cd18545 152 LLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 358 FCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18545 232 LISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
127-419 |
1.82e-37 |
|
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: 141.47 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 127 IGCLVVSSAITMSVPLFLGKVIDV-VFNKSgmdsaaMAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLRSRL 205
Cdd:cd18550 5 LLLILLSALLGLLPPLLLREIIDDaLPQGD------LGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 206 YRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAIV 285
Cdd:cd18550 79 YAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 286 YGRYVRRITKVELDKYAEIMKFAEERF--GNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFI 363
Cdd:cd18550 159 VGRRRRKLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 364 IISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18550 239 PALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
447-665 |
3.44e-37 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 138.37 E-value: 3.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPES-AVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwlrnnIGA 525
Cdd:cd03293 3 VRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 526 VSQEPVLFS-CSIRENILYGANPGETPSPERLQQV---IEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIARAL 601
Cdd:cd03293 78 VFQQDALLPwLTVLDNVALGLELQGVPKAEARERAeelLELVGLSGFENAYPH-----------QLSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLS-TIRNADQIAVLS--DGKIVEQ 665
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSarPGRIVAE 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
447-662 |
3.54e-37 |
|
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: 138.39 E-value: 3.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPES-AVLTDFSLNLMPGTTTAVVGRSGSGKTT---IALLMLRlydPQGGTVHLDGIDLRTVNPQWL--- 519
Cdd:cd03255 3 LKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 520 -RNNIGAVSQE----PVLfscSIRENILYGANPGETPSPERLQQVIEdanvsqFTDQ--LPDGLDTLVGQrgmmLSGGQK 592
Cdd:cd03255 80 rRRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEE------LLERvgLGDRLNHYPSE----LSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 593 QRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNL--IQGRTVLTIAHRLSTIRNADQIAVLSDGKI 662
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
123-419 |
4.26e-37 |
|
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: 140.72 E-value: 4.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVID-VVFNKSGMDSAAMAKLGEYS---------VLLFGIFVLGGFANFARVHLFGN 192
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDdVLGDKPLPGLLGLAPLLGPDplallllaaAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 193 AALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVS 272
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 273 ALVVPAMAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIF 352
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 353 FGLTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
447-672 |
4.62e-37 |
|
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: 138.97 E-value: 4.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPesAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAV 526
Cdd:cd03295 3 FENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEPVLFS-CSIRENIlyGANPG--ETPSPERLQQVIE-----DANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIA 598
Cdd:cd03295 81 IQQIGLFPhMTVEENI--ALVPKllKWPKEKIRERADEllalvGLDPAEFADRYPH-----------ELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 599 RALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRL-STIRNADQIAVLSDGKIVEQGSYNELM 672
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
123-419 |
6.92e-37 |
|
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: 139.93 E-value: 6.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDvvfnkSGMDSAAMAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLR 202
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGID-----SGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 203 SRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGM 282
Cdd:cd18546 76 LRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 283 AIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEalqigYKETRAR-----AIFFGLTG 357
Cdd:cd18546 156 TRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDD-----YRDARLRaqrlvAIYFPGVE 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 358 FCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18546 231 LLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
447-667 |
7.86e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.97 E-value: 7.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAV 526
Cdd:PRK13632 10 VENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEP--VLFSCSIRENILYGANPGETPsPERLQQVIEDanVSQFTdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKN 604
Cdd:PRK13632 89 FQNPdnQFIGATVEDDIAFGLENKKVP-PKKMKDIIDD--LAKKV-----GMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 605 PAILILDEATSALDAVSENLVQNALDNLIQGR--TVLTIAHRLSTIRNADQIAVLSDGKIVEQGS 667
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
447-664 |
1.10e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 138.30 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPES-AVLTDFSLNLMPGTTTAVVGRSGSGKTTIallmLR----LYDPQGGTVHLDGIDLRTVNPQwlrn 521
Cdd:COG1116 10 LRGVSKRFPTGGGGvTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRliagLEKPTSGEVLVDGKPVTGPGPD---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 522 nIGAVSQEPVLFS-CSIRENILYGANPGETPSPERLQQV---IEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAI 597
Cdd:COG1116 82 -RGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERArelLELVGLAGFEDAYPH-----------QLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 598 ARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAH------RLstirnADQIAVLSD--GKIVE 664
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
467-673 |
4.92e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 138.33 E-value: 4.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 467 SLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQ---WLRNNIGAVSQEPvlfscsirenilY 543
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRelrPLRRRMQMVFQDP------------Y 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 544 GA-NP---------------GETPSPERLQQVIEdanvsqftdqLPD--GLDTLVGQR-GMMLSGGQKQRVAIARALIKN 604
Cdd:COG4608 106 ASlNPrmtvgdiiaeplrihGLASKAERRERVAE----------LLElvGLRPEHADRyPHEFSGGQRQRIGIARALALN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 605 PAILILDEATSALDaVSenlVQ----NALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELMG 673
Cdd:COG4608 176 PKLIVCDEPVSALD-VS---IQaqvlNLLEDLQDelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYA 247
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
453-671 |
1.24e-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: 137.11 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 453 TFPTRPESA-VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQG---GTVHLDGIDLRTVNPQWLR----NNIG 524
Cdd:COG0444 10 YFPTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRkirgREIQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 525 AVSQEPvlFSC---------SIRENILYGanpGETPSPERLQQVIE--DAnVsqftdQLPDGLDTLvGQRGMMLSGGQKQ 593
Cdd:COG0444 90 MIFQDP--MTSlnpvmtvgdQIAEPLRIH---GGLSKAEARERAIEllER-V-----GLPDPERRL-DRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 594 RVAIARALIKNPAILILDEATSALDaVSenlVQ----NALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQG 666
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALD-VT---IQaqilNLLKDLQRelGLAILFITHDLGVVAEiADRVAVMYAGRIVEEG 233
|
....*
gi 23397593 667 SYNEL 671
Cdd:COG0444 234 PVEEL 238
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
438-666 |
2.42e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 135.14 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 438 LEKPVGEVgfQNVFFTFPTRPESAvLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDL--RTVn 515
Cdd:PRK13635 1 MKEEIIRV--EHISFRYPDAATYA-LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseETV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 516 pqW-LRNNIGAVSQEP--VLFSCSIRENILYGANPGETPSPE---RLQQVIEDANVSQFTDQLPDgldtlvgqrgmMLSG 589
Cdd:PRK13635 77 --WdVRRQVGMVFQNPdnQFVGATVQDDVAFGLENIGVPREEmveRVDQALRQVGMEDFLNREPH-----------RLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23397593 590 GQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLI--QGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQG 666
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
261-671 |
2.67e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 143.96 E-value: 2.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 261 MIYTSPQLAAVS---ALVVPAMAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDE 337
Cdd:PLN03232 432 MVLLYQQLGVASlfgSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNE 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 338 ALQIgykeTRARAIFFGLTGFCGNFI--IISVLYYGGTLVLQDSLTIG-ALTAFMLYAgYVAISMNGLSNFYSQLNKGIG 414
Cdd:PLN03232 512 ELSW----FRKAQLLSAFNSFILNSIpvVVTLVSFGVFVLLGGDLTPArAFTSLSLFA-VLRSPLNMLPNLLSQVVNANV 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 415 ASERIWEILDRECSIPIDKGvvPLEKPVGEVGFQNVFFTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLML 494
Cdd:PLN03232 587 SLQRIEELLLSEERILAQNP--PLQPGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 495 rlydpqGGTVHLDGIDLRtvnpqwLRNNIGAVSQEPVLFSCSIRENILYGANPgetpSPERLQQVIEDANVSQFTDQLPD 574
Cdd:PLN03232 665 ------GELSHAETSSVV------IRGSVAYVPQVSWIFNATVRENILFGSDF----ESERYWRAIDVTALQHDLDLLPG 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 575 GLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDA-VSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQ 653
Cdd:PLN03232 729 RDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDR 808
|
410
....*....|....*...
gi 23397593 654 IAVLSDGKIVEQGSYNEL 671
Cdd:PLN03232 809 IILVSEGMIKEEGTFAEL 826
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
447-667 |
6.69e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 135.59 E-value: 6.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPES-AVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRN---N 522
Cdd:COG1135 4 LENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAarrK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 523 IGAVSQEPVLF-SCSIRENILYganPGE---TPSPERLQQVIEdanvsqftdqLpdgLDtLVG----------QrgmmLS 588
Cdd:COG1135 84 IGMIFQHFNLLsSRTVAENVAL---PLEiagVPKAEIRKRVAE----------L---LE-LVGlsdkadaypsQ----LS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 589 GGQKQRVAIARALIKNPAILILDEATSALDAVSenlVQNALDnLIQ------GRTVLTIAHRLSTIRN-ADQIAVLSDGK 661
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPET---TRSILD-LLKdinrelGLTIVLITHEMDVVRRiCDRVAVLENGR 218
|
....*.
gi 23397593 662 IVEQGS 667
Cdd:COG1135 219 IVEQGP 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
443-685 |
8.04e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 142.57 E-value: 8.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 443 GEVGFQNVFFTFptRPE-SAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRN 521
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 522 NIGAVSQEPVLFSCSIRENIlygaNPGETPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARAL 601
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNL----DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGIQEGVFRE 681
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSK 1469
|
....
gi 23397593 682 LVAS 685
Cdd:PLN03130 1470 MVQS 1473
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
456-661 |
8.05e-35 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 130.38 E-value: 8.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 456 TRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQW--LRNNIGAVSQEPVLF 533
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 534 S-CSIRENILYGanpgetpsperlqqviedanvsqftdqlpdgldtlvgqrgmmLSGGQKQRVAIARALIKNPAILILDE 612
Cdd:cd03229 89 PhLTVLENIALG------------------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 23397593 613 ATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLS-TIRNADQIAVLSDGK 661
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
465-667 |
1.62e-34 |
|
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: 138.28 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 465 DFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLyDPQGGTVHLDGIDLRTVNP---QWLRNNIGAVSQEPvlFSC-----S 536
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRralRPLRRRMQVVFQDP--FGSlsprmT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENI---LYGANPGETPSpERLQQVIEdanvsqftdQLPD-GLDtlvgqRGMM------LSGGQKQRVAIARALIKNPA 606
Cdd:COG4172 381 VGQIIaegLRVHGPGLSAA-ERRARVAE---------ALEEvGLD-----PAARhrypheFSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 607 ILILDEATSALDaVSenlVQNALDNLIQ------GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGS 667
Cdd:COG4172 446 LLVLDEPTSALD-VS---VQAQILDLLRdlqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
138-419 |
3.06e-34 |
|
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: 132.08 E-value: 3.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 138 MSVPLFLGKVIDVVFNKSGMDSAAmaklgeYSVLLFGIFVLGG-FANFARVHLFGNAALRIVRSLRSRLYRSMLMQEVGW 216
Cdd:cd18590 13 TFIPYYTGRVIDILGGEYQHNAFT------SAIGLMCLFSLGSsLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 217 FDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRS-VAMIGVgTGMMIYTSPQLAAVSALVVPAMAGMAIVYGRYVRRITK 295
Cdd:cd18590 87 FEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSlVKTLGM-LGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 296 VELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIIISVLYYGGTLV 375
Cdd:cd18590 166 AVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLI 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 23397593 376 LQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18590 246 QSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
448-662 |
3.81e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 128.28 E-value: 3.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTvNPQWLRNNIGAVS 527
Cdd:cd03230 4 RNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 528 QEPVLFS-CSIRENILYganpgetpsperlqqviedanvsqftdqlpdgldtlvgqrgmmlSGGQKQRVAIARALIKNPA 606
Cdd:cd03230 80 EEPSLYEnLTVRENLKL--------------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 607 ILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIRN-ADQIAVLSDGKI 662
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
453-663 |
1.28e-33 |
|
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: 127.76 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 453 TFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGidlRTVNPQWLRNNIGAVSQEP-- 530
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQDVdy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 531 VLFSCSIRENILYGANPGETpSPERLQQVIEDANVSQFTDQLPdgldtlvgqrgMMLSGGQKQRVAIARALIKNPAILIL 610
Cdd:cd03226 83 QLFTDSVREELLLGLKELDA-GNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 611 DEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTI-RNADQIAVLSDGKIV 663
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
462-685 |
1.49e-33 |
|
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: 128.61 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwlRNNIGAVSQEPVLF-SCSIREN 540
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 ILYGANPGETPSPERLQQVIEDANVSqftdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAV 620
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEML--------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 621 SENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEqgsynelMGIQEGVFR----ELVAS 685
Cdd:cd03299 164 TKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQ-------VGKPEEVFKkpknEFVAE 228
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
120-418 |
1.68e-33 |
|
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: 130.26 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 120 KWVLTAGIGCLVVSSAITMSVPLFLGKVIDVVFnksgmDSAAMAKLGEYSVLLFGIFVLGGFANFARV---HLFGnaaLR 196
Cdd:cd18549 1 KKLFFLDLFCAVLIAALDLVFPLIVRYIIDDLL-----PSKNLRLILIIGAILLALYILRTLLNYFVTywgHVMG---AR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 197 IVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVV 276
Cdd:cd18549 73 IETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 277 PAMAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEalqigYKETRAR-----AI 351
Cdd:cd18549 153 PLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDR-----FLESKKKaykamAY 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 352 FFGLTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASER 418
Cdd:cd18549 228 FFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
447-667 |
2.28e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 131.37 E-value: 2.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIallmLR----LYDPQGGTVHLDGIDLRTVNPQwlRNN 522
Cdd:COG3842 8 LENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTL----LRmiagFETPDSGRILLDGRDVTGLPPE--KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 523 IGAVSQEPVLFS-CSIRENILYGANPGETPSPERLQQVIEdanvsqFTDQLpdGLDTLVGQRGMMLSGGQKQRVAIARAL 601
Cdd:COG3842 79 VGMVFQDYALFPhLTVAENVAFGLRMRGVPKAEIRARVAE------LLELV--GLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 602 IKNPAILILDEATSALDAvseNL---VQNALDNLIQ--GRTVLTIAHRLS---TIrnADQIAVLSDGKIVEQGS 667
Cdd:COG3842 151 APEPRVLLLDEPLSALDA---KLreeMREELRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
123-419 |
2.58e-33 |
|
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: 129.52 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVVfnksgMDSAAMAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLR 202
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGP-----IAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 203 SRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQnVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGM 282
Cdd:cd18543 76 TDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 283 AIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNF 362
Cdd:cd18543 155 ARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPEL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 363 IIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18543 235 GLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
463-666 |
3.75e-33 |
|
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: 126.64 E-value: 3.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNL---MPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDG---------IDLrtvNPQwlRNNIGAVSQEP 530
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkINL---PPQ--QRKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 531 VLFS-CSIRENILYGAnPGETPSPERLQqviedanVSQFTDQLpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILI 609
Cdd:cd03297 85 ALFPhLNVRENLAFGL-KRKRNREDRIS-------VDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 610 LDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQG 666
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
448-666 |
4.16e-33 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 125.63 E-value: 4.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVS 527
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 528 QepvlfscsirenilyganpgetpsperlqqVIEDANVSQFTDQlpdGLDTLvgqrgmmlSGGQKQRVAIARALIKNPAI 607
Cdd:cd03214 80 Q------------------------------ALELLGLAHLADR---PFNEL--------SGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 608 LILDEATSALDAVSenlvQNALDNLIQ------GRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQG 666
Cdd:cd03214 119 LLLDEPTSHLDIAH----QIELLELLRrlarerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
447-691 |
5.81e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 5.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVnpqwlRNNIGAV 526
Cdd:COG1121 9 LENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEPVL---FSCSIRENILYGANP--GETPSP-----ERLQQVIEDANVSQFtdqlpdgLDTLVGQrgmmLSGGQKQRVA 596
Cdd:COG1121 81 PQRAEVdwdFPITVRDVVLMGRYGrrGLFRRPsradrEAVDEALERVGLEDL-------ADRPIGE----LSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 597 IARALIKNPAILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIR-NADQIAVLsDGKIVEQGSYNElmgi 674
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVReYFDRVLLL-NRGLVAHGPPEE---- 224
|
250
....*....|....*..
gi 23397593 675 qegVFRELVASQAFGSR 691
Cdd:COG1121 225 ---VLTPENLSRAYGGP 238
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
462-666 |
1.55e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 126.30 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTiaLL-----MLRLYDPQ--GGTVHLDGIDL--RTVNPQWLRNNIGAVSQEPVL 532
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKST--LLrclnrMNDLIPGArvEGEILLDGEDIydPDVDVVELRRRVGMVFQKPNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 533 FSCSIRENILYGANPGETPSPERLQQVIEDA--NVSQFtDQLPDGLDtlvgQRGMMLSGGQKQRVAIARALIKNPAILIL 610
Cdd:COG1117 104 FPKSIYDNVAYGLRLHGIKSKSELDEIVEESlrKAALW-DEVKDRLK----KSALGLSGGQQQRLCIARALAVEPEVLLM 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 611 DEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQG 666
Cdd:COG1117 179 DEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEFG 235
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
128-419 |
4.10e-32 |
|
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: 126.05 E-value: 4.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 128 GCLVVSSAITMSVPLFLGKVIDVVFNK---SGMDSA--AMAKLGEYSVLLFgiFVLGGfanfarvhLFGNAALRIVRSLR 202
Cdd:cd18589 3 GLVVLSSLGEMAIPYYTGRMTDWIMNKdapEAFTAAitVMSLLTIASAVSE--FVCDL--------IYNITMSRIHSRLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 203 SRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGM 282
Cdd:cd18589 73 GLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 283 AIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNF 362
Cdd:cd18589 153 PKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 363 IIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18589 233 LKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
448-671 |
5.94e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 127.19 E-value: 5.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIallmLR----LYDPQGGTVHLDGIDLRT-VNPQwlRNN 522
Cdd:COG1118 6 RNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTL----LRiiagLETPDSGRIVLNGRDLFTnLPPR--ERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 523 IGAVSQEPVLF-SCSIRENILYGANPGETPSPERLQQV---IEDANVSQFTDQLPdgldtlvGQrgmmLSGGQKQRVAIA 598
Cdd:COG1118 77 VGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVeelLELVQLEGLADRYP-------SQ----LSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 599 RALIKNPAILILDEATSALDAvsenLVQNAL-DNLIQ-----GRTVLTIAH-RLSTIRNADQIAVLSDGKIVEQGSYNEL 671
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDA----KVRKELrRWLRRlhdelGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
462-667 |
7.91e-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: 123.95 E-value: 7.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTiallMLR----LYDPQGGTVHLDGIDL--RTVNPQWLRNNIGAVSQEPVLFS- 534
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKST----LLRcinlLEEPDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENILYGanpgetpsPERLQ-----QVIEDA-------NVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIARALI 602
Cdd:COG1126 92 LTVLENVTLA--------PIKVKkmskaEAEERAmellervGLADKADAYPA-----------QLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 603 KNPAILILDEATSALD--------AVSENLVQnaldnliQGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGS 667
Cdd:COG1126 153 MEPKVMLFDEPTSALDpelvgevlDVMRDLAK-------EGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
465-672 |
1.22e-31 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 124.29 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 465 DFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRN----NIGAVSQEPVLF-SCSIRE 539
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 540 NILYGANPGETPSPERLQ---QVIEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIARALIKNPAILILDEATSA 616
Cdd:cd03294 122 NVAFGLEVQGVPRAEREEraaEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 23397593 617 LDAVSENLVQNALDNLI--QGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNELM 672
Cdd:cd03294 191 LDPLIRREMQDELLRLQaeLQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
125-419 |
2.01e-31 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 124.05 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 125 AGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDsaAMAKLGeysVLLFGIFVLGGFANFARVHLFGNAALRIVRSLRSR 204
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIIDEGIANGDLS--YILRTG---LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 205 LYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAI 284
Cdd:cd18548 78 LFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 285 VYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFII 364
Cdd:cd18548 158 LIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 365 ISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18548 238 VAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
123-392 |
3.12e-31 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 124.22 E-value: 3.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMD----------SAAMAKLGEYSVLLFGIFVLGGFANFARVHLFGN 192
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFlplvpaslgpADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 193 AALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVS 272
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 273 ALVVPAMAGMAIvygRYVRRITKveldKYAEIMKFA-------EERFGNVKTVKTFCREQQEVAAFDGKLDEalqigYKE 345
Cdd:cd18565 161 LLPVPLIIAGTY---WFQRRIEP----RYRAVREAVgdlnarlENNLSGIAVIKAFTAEDFERERVADASEE-----YRD 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 346 TRARAI-----FFGLTGFCGNFIIISVLYYGGTLVLQD------SLTIGALTAFMLYA 392
Cdd:cd18565 229 ANWRAIrlraaFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYT 286
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
444-666 |
3.73e-31 |
|
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: 120.35 E-value: 3.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 444 EVGFQNVFFT---FPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTI--ALLMLRLYDPQGGTVHLDGIDLRtvnPQW 518
Cdd:cd03213 3 TLSFRNLTVTvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRPLD---KRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 519 LRNNIGAVSQEPVLFSC-SIRENILYGANpgetpsperLQQviedanvsqftdqlpdgldtlvgqrgmmLSGGQKQRVAI 597
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLMFAAK---------LRG----------------------------LSGGERKRVSI 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 598 ARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLST--IRNADQIAVLSDGKIVEQG 666
Cdd:cd03213 123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
447-682 |
4.41e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 122.09 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPEsaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNP---QWLRNNI 523
Cdd:COG3638 5 LRNLSKRYPGGTP--ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 524 GAVSQEPVLFS-CSIRENILYGAnPGETPSPERL-----QQVIEDAnvSQFTDQLpdGLDTLVGQRGMMLSGGQKQRVAI 597
Cdd:COG3638 83 GMIFQQFNLVPrLSVLTNVLAGR-LGRTSTWRSLlglfpPEDRERA--LEALERV--GLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 598 ARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELmgi 674
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDGRVVFDGPPAEL--- 234
|
....*...
gi 23397593 675 QEGVFREL 682
Cdd:COG3638 235 TDAVLREI 242
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
448-671 |
5.29e-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: 120.69 E-value: 5.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRPESAVlTDFSLNLMPGTTTAVVGRSGSGKTTIaLLMLR-LYDPQGGTVHLDGIDLRTvNPQWLRNNIGAV 526
Cdd:cd03263 4 RNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTT-LKMLTgELRPTSGTAYINGYSIRT-DRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEPVLFS-CSIRENILYGAnpgetpspeRLQ---QVIEDANVSQFTDQ--LPDGLDTLVGQrgmmLSGGQKQRVAIARA 600
Cdd:cd03263 81 PQFDALFDeLTVREHLRFYA---------RLKglpKSEIKEEVELLLRVlgLTDKANKRART----LSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 601 LIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNEL 671
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
466-675 |
9.75e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 120.63 E-value: 9.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 466 FSLNLMPGTTTAVVGRSGSGKTTiaLLML--RLYDPQGGTVHLDGIDLRTVNPqwlrnnigavSQEPV--------LFS- 534
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKST--LLNLiaGFLPPDSGRILWNGQDLTALPP----------AERPVsmlfqennLFPh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENILYGANPGETPSPE---RLQQVIEDANVSQFTDQLPdgldtlvGQrgmmLSGGQKQRVAIARALIKNPAILILD 611
Cdd:COG3840 86 LTVAQNIGLGLRPGLKLTAEqraQVEQALERVGLAGLLDRLP-------GQ----LSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23397593 612 EATSALDAvseNLVQNALDnLI------QGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNELMGIQ 675
Cdd:COG3840 155 EPFSALDP---ALRQEMLD-LVdelcreRGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
447-671 |
1.22e-30 |
|
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: 120.37 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTrpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRN---NI 523
Cdd:cd03256 3 VENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 524 GAVSQEPVLFS-CSIRENILYGAnPGETP---SPERLQQVIEDANVSQFTDQLpdGLDTLVGQRGMMLSGGQKQRVAIAR 599
Cdd:cd03256 81 GMIFQQFNLIErLSVLENVLSGR-LGRRStwrSLFGLFPKEEKQRALAALERV--GLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 600 ALIKNPAILILDEATSALDAVSENLVQNAL--DNLIQGRTVLTIAHRLSTIR-NADQIAVLSDGKIVEQGSYNEL 671
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAEL 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
445-667 |
2.14e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.06 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 445 VGFQNVFFTFPTRPEsAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLM--LRLYDPQGGT-VHLDGIDLRTVNPQWLRN 521
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLIngLLLPDDNPNSkITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 522 NIGAVSQEP--VLFSCSIRENILYGANPGETPSPERL---QQVIEDANVSQFTDQLPDGLdtlvgqrgmmlSGGQKQRVA 596
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIkivRDVLADVGMLDYIDSEPANL-----------SGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397593 597 IARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGS 667
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
270-687 |
3.04e-30 |
|
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: 128.14 E-value: 3.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 270 AVSALVVPAMAGMAIVYGRYVRRITKVELDKyaeiMKFAEERFGNVKTVKTFCREqqevAAFDGKLDEALQIGYKETRAR 349
Cdd:TIGR00957 465 AVMVLMVPLNAVMAMKTKTYQVAHMKSKDNR----IKLMNEILNGIKVLKLYAWE----LAFLDKVEGIRQEELKVLKKS 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 350 AIFFGLTGF---CGNFIIISVLYYGGTLVLQDSLtIGALTAFMLYAGY--VAISMNGLSNFYSQLNKGIGASERIWEILD 424
Cdd:TIGR00957 537 AYLHAVGTFtwvCTPFLVALITFAVYVTVDENNI-LDAEKAFVSLALFniLRFPLNILPMVISSIVQASVSLKRLRIFLS 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 425 RECSIPIDKGVVPLEKPVG-EVGFQNVFFTFpTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGT 503
Cdd:TIGR00957 616 HEELEPDSIERRTIKPGEGnSITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 504 VHLDGidlrtvnpqwlrnNIGAVSQEPVLFSCSIRENILYGanpgETPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQR 583
Cdd:TIGR00957 695 VHMKG-------------SVAYVPQQAWIQNDSLRENILFG----KALNEKYYQQVLEACALLPDLEILPSGDRTEIGEK 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 584 GMMLSGGQKQRVAIARALIKNPAILILDEATSALDA-VSENLVQNAL--DNLIQGRTVLTIAHRLSTIRNADQIAVLSDG 660
Cdd:TIGR00957 758 GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGG 837
|
410 420
....*....|....*....|....*..
gi 23397593 661 KIVEQGSYNELMGiQEGVFRELVASQA 687
Cdd:TIGR00957 838 KISEMGSYQELLQ-RDGAFAEFLRTYA 863
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
463-672 |
5.91e-30 |
|
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: 121.75 E-value: 5.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLN----LMPGTTTAVVGRSGSGKTTIallmLR----LYDPQGGTVHLDGIDLR-TVNPQWL---RNNIGAVSQEP 530
Cdd:COG4148 11 RGGFTLDvdftLPGRGVTALFGPSGSGKTTL----LRaiagLERPDSGRIRLGGEVLQdSARGIFLpphRRRIGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 531 VLFS-CSIRENILYGA-NPGETPSPERLQQVIEdanvsqftdQLpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAIL 608
Cdd:COG4148 87 RLFPhLSVRGNLLYGRkRAPRAERRISFDEVVE---------LL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 609 ILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNELM 672
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLERLRDelDIPILYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVL 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
447-667 |
9.19e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.68 E-value: 9.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPT-RPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWL---RNN 522
Cdd:PRK11153 4 LKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaRRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 523 IGAVSQE-PVLFSCSIRENIlygANPGE---TPSPERLQQVIEdanvsqftdqlpdgLDTLVG----------QrgmmLS 588
Cdd:PRK11153 84 IGMIFQHfNLLSSRTVFDNV---ALPLElagTPKAEIKARVTE--------------LLELVGlsdkadrypaQ----LS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 589 GGQKQRVAIARALIKNPAILILDEATSALDAVSenlVQNALDNLIQ-----GRTVLTIAHRLSTIRN-ADQIAVLSDGKI 662
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPAT---TRSILELLKDinrelGLTIVLITHEMDVVKRiCDRVAVIDAGRL 219
|
....*
gi 23397593 663 VEQGS 667
Cdd:PRK11153 220 VEQGT 224
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
120-419 |
1.14e-29 |
|
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: 119.09 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 120 KWVLTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDsaamaKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVR 199
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDIN-----LLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 200 SLRSRLYRSMLMQEVGWFDTKGTGELINRLsNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAM 279
Cdd:cd18570 76 RLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 280 AGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFC 359
Cdd:cd18570 155 ILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLI 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 360 GNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18570 235 SLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
447-678 |
1.46e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.32 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTrPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAV 526
Cdd:PRK13648 10 FKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEPV-LFSCSI-RENILYGANPGETPSPE---RLQQVIEDANVSQFTDQLPDGLdtlvgqrgmmlSGGQKQRVAIARAL 601
Cdd:PRK13648 89 FQNPDnQFVGSIvKYDVAFGLENHAVPYDEmhrRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 602 IKNPAILILDEATSALDAVSE----NLVQNALDNliQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGIQEG 677
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARqnllDLVRKVKSE--HNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
.
gi 23397593 678 V 678
Cdd:PRK13648 236 L 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
463-673 |
1.78e-29 |
|
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: 120.22 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNL---MPGT-TTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDG---------IDLRTVnpqwlRNNIGAVSQE 529
Cdd:TIGR02142 9 LGDFSLDAdftLPGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgIFLPPE-----KRRIGYVFQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 530 PVLFS-CSIRENILYG---ANPGETP-SPERLQQVIedanvsqftdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKN 604
Cdd:TIGR02142 84 ARLFPhLSVRGNLRYGmkrARPSERRiSFERVIELL--------------GIGHLLGRLPGRLSGGEKQRVAIGRALLSS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 605 PAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNELMG 673
Cdd:TIGR02142 150 PRLLLMDEPLAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
448-671 |
2.49e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 117.88 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRPESA---VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQW-LRNNI 523
Cdd:PRK13633 8 KNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 524 GAVSQEP--VLFSCSIRENILYGA-NPGETPSP--ERLQQVIEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIA 598
Cdd:PRK13633 88 GMVFQNPdnQIVATIVEEDVAFGPeNLGIPPEEirERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 599 RALIKNPAILILDEATSALDAVSENLVQNALDNL--IQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
355-672 |
3.20e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 124.85 E-value: 3.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 355 LTGFCGNFI--IISVLYYGGTLVLQDSLTIG-ALTAFMLYAgYVAISMNGLSNFYSQLNKGIGASERIWEILDRECSIPI 431
Cdd:PLN03130 525 FNSFILNSIpvLVTVVSFGVFTLLGGDLTPArAFTSLSLFA-VLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLL 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 432 DKgvVPLEKPVGEVGFQNVFFTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLdgidl 511
Cdd:PLN03130 604 PN--PPLEPGLPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV----- 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 512 rtvnpqwLRNNIGAVSQEPVLFSCSIRENILYGAnPGEtpsPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQ 591
Cdd:PLN03130 677 -------IRGTVAYVPQVSWIFNATVRDNILFGS-PFD---PERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQ 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 592 KQRVAIARALIKNPAILILDEATSALDA-VSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNE 670
Cdd:PLN03130 746 KQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEE 825
|
..
gi 23397593 671 LM 672
Cdd:PLN03130 826 LS 827
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
462-666 |
3.77e-29 |
|
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: 115.37 E-value: 3.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTtAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTvNPQWLRNNIGAVSQEPVLF-SCSIRE- 539
Cdd:cd03264 15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYpNFTVREf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 540 ----NILYGANPGEtpSPERLQQVIEDANVSQFtdqlpdgLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:cd03264 93 ldyiAWLKGIPSKE--VKARVDEVLELVNLGDR-------AKKKIGS----LSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 23397593 616 ALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQG 666
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
463-671 |
4.16e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 116.41 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYD--PQ---GGTVHLDGIDL---RTVNPQwLRNNIGAVSQEPVLFS 534
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIyspRTDTVD-LRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENILYGANPGETPSPERLQQVIEDANV-SQFTDQLPDGL-DTLVGqrgmmLSGGQKQRVAIARALIKNPAILILDE 612
Cdd:PRK14239 100 MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKgASIWDEVKDRLhDSALG-----LSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 613 ATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
447-664 |
4.18e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.53 E-value: 4.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPEsaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQ---WLRNNI 523
Cdd:COG2884 4 FENVSKRYPGGRE--ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 524 GAVSQE-PVLFSCSIRENILY-----GANPGETPspERLQQVIEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAI 597
Cdd:COG2884 82 GVVFQDfRLLPDRTVYENVALplrvtGKSRKEIR--RRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 598 ARALIKNPAILILDEATSALD-AVSENLVQ-----NALdnliqGRTVLtIA-HRLSTIRNADQ-IAVLSDGKIVE 664
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDpETSWEIMElleeiNRR-----GTTVL-IAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
157-691 |
4.62e-29 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 124.51 E-value: 4.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 157 MDSAAMAKLGEYSVLL--FGIFVLGGFANFARVHLFGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTL 234
Cdd:PTZ00243 987 MWSTRSFKLSAATYLYvyLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDID 1066
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 235 MVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPqlaavsaLVVPAMAGMAIVY----------GRYVRRITKVeldKYAEI 304
Cdd:PTZ00243 1067 ILDNTLPMSYLYLLQCLFSICSSILVTSASQP-------FVLVALVPCGYLYyrlmqfynsaNREIRRIKSV---AKSPV 1136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 305 MKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIIISVLYYG--GTLVLQDSLTI 382
Cdd:PTZ00243 1137 FTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGviGTMLRATSQEI 1216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 383 GALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERIWEILD---RECSIPIDKGVVPLEKPVG---EVGFQNVffTFPT 456
Cdd:PTZ00243 1217 GLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDevpHEDMPELDEEVDALERRTGmaaDVTGTVV--IEPA 1294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 457 RPESA-------------------------VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDL 511
Cdd:PTZ00243 1295 SPTSAaphpvqagslvfegvqmryreglplVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI 1374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 512 RTVNPQWLRNNIGAVSQEPVLFSCSIRENIlygaNPGETPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQ 591
Cdd:PTZ00243 1375 GAYGLRELRRQFSMIPQDPVLFDGTVRQNV----DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQ 1450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 592 KQRVAIARALIKNPAILIL-DEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNE 670
Cdd:PTZ00243 1451 RQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRE 1530
|
570 580
....*....|....*....|.
gi 23397593 671 LMGIQEGVFRELVasQAFGSR 691
Cdd:PTZ00243 1531 LVMNRQSIFHSMV--EALGRS 1549
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
449-660 |
5.05e-29 |
|
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: 115.12 E-value: 5.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 449 NVFFTFPtrPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVH----LDGIDLRTVNPQWLRNNIG 524
Cdd:cd03290 5 NGYFSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 525 AVSQEPVLFSCSIRENILYGanpgetpSP---ERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARAL 601
Cdd:cd03290 83 YAAQKPWLLNATVEENITFG-------SPfnkQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 602 IKNPAILILDEATSALDA-VSENLVQNALDNLIQG--RTVLTIAHRLSTIRNADQIAVLSDG 660
Cdd:cd03290 156 YQNTNIVFLDDPFSALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
456-661 |
1.96e-28 |
|
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: 112.96 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 456 TRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTiallMLR----LYDPQGGTVHLDGIDLRTVNPQWLRNnIGAVSQEPV 531
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTT----LLRilagLLPPSAGEVLWNGEPIRDAREDYRRR-LAYLGHADG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 532 LF-SCSIRENI-LYGANPGETPSPERLQQVIEDANvsqftdqLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILI 609
Cdd:COG4133 86 LKpELTVRENLrFWAALYGLRADREAIDEALEAVG-------LAGLADLPVRQ----LSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 23397593 610 LDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIRNADQIAvLSDGK 661
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLaRGGAVLLTTHQPLELAAARVLD-LGDFK 206
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
447-666 |
3.40e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 112.63 E-value: 3.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVnpqwlRNNIGAV 526
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEPVL---FSCSIRENILYGANPGETPSP-------ERLQQVIEDANVSQFTDQlpdgldtLVGQrgmmLSGGQKQRVA 596
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLYGHKGLFRrlskadkAKVDEALERVGLSELADR-------QIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 597 IARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLSTI-RNADQIAVLsDGKIVEQG 666
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVlEYFDRVLLL-NRTVVASG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
462-671 |
3.48e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 116.33 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTiallMLR----LYDPQGGTVHLDGIDLRTVNPQwlRNNIGAVSQEPVLF-SCS 536
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKST----LLRmiagLEDPTSGEILIGGRDVTDLPPK--DRNIAMVFQSYALYpHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENILYG---ANpgeTPSPERLQQVIEDANVSQFTDQLpdglDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDEA 613
Cdd:COG3839 92 VYENIAFPlklRK---VPKAEIDRRVREAAELLGLEDLL----DRKPKQ----LSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 614 TSALDAVS-ENL------VQNALdnliqGRTV----------LTIahrlstirnADQIAVLSDGKIVEQGSYNEL 671
Cdd:COG3839 161 LSNLDAKLrVEMraeikrLHRRL-----GTTTiyvthdqveaMTL---------ADRIAVMNDGRIQQVGTPEEL 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
324-660 |
7.09e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 118.76 E-value: 7.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 324 EQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIII------SVLYYGGTLvlqdslTIGALT----AFmlyaG 393
Cdd:COG4178 240 EAAERRRLRRRFDAVIANWRRLIRRQRNLTFFTTGYGQLAVIfpilvaAPRYFAGEI------TLGGLMqaasAF----G 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 394 YVAISMNGLSNFYSQLNKGIGASERIWEILD--RECSIPIDKGVVPLEKPVGEVGFQNVffTFPTRPESAVLTDFSLNLM 471
Cdd:COG4178 310 QVQGALSWFVDNYQSLAEWRATVDRLAGFEEalEAADALPEAASRIETSEDGALALEDL--TLRTPDGRPLLEDLSLSLK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 472 PGTTTAVVGRSGSGKTTiallMLR----LYDPQGGTVHLdgidlrtvnPQwlRNNIGAVSQEPVLFSCSIRENILYgANP 547
Cdd:COG4178 388 PGERLLITGPSGSGKST----LLRaiagLWPYGSGRIAR---------PA--GARVLFLPQRPYLPLGTLREALLY-PAT 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 548 GETPSPERLQQVIEDANVSQFTDQLPDGLDtlvgqRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQN 627
Cdd:COG4178 452 AEAFSDAELREALEAVGLGHLAERLDEEAD-----WDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
330 340 350
....*....|....*....|....*....|...
gi 23397593 628 ALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDG 660
Cdd:COG4178 527 LLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
447-682 |
9.29e-28 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 112.39 E-value: 9.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTrpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNP---QWLRNNI 523
Cdd:TIGR02315 4 VENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkklRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 524 GAVSQEPVLFS-CSIRENILYGAnPGETPSPERLQQVIEDANVSQFTDQLPD-GLDTLVGQRGMMLSGGQKQRVAIARAL 601
Cdd:TIGR02315 82 GMIFQHYNLIErLTVLENVLHGR-LGYKPTWRSLLGRFSEEDKERALSALERvGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELmgiQEGV 678
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKedGITVIINLHQVDLAKKyADRIVGLKAGEIVFDGAPSEL---DDEV 237
|
....
gi 23397593 679 FREL 682
Cdd:TIGR02315 238 LRHI 241
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
460-685 |
1.07e-27 |
|
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: 113.03 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 460 SAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGgTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRE 539
Cdd:cd03289 17 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 540 NIlygaNPGETPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDA 619
Cdd:cd03289 96 NL----DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 620 VSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGiQEGVFRELVAS 685
Cdd:cd03289 172 ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN-EKSHFKQAISP 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
462-662 |
1.79e-27 |
|
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: 110.70 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQW--LRNNIGAVSQEPVLFS-CSIR 538
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKVGMVFQQFNLFPhLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 539 ENILYG--------ANPGETPSPERLQQViedanvsqftdQLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILIL 610
Cdd:cd03262 95 ENITLApikvkgmsKAEAEERALELLEKV-----------GLADKADAYPAQ----LSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 611 DEATSALDAvseNLVQNALDNLIQ----GRTVLTIAHRLSTIRN-ADQIAVLSDGKI 662
Cdd:cd03262 160 DEPTSALDP---ELVGEVLDVMKDlaeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
459-672 |
2.70e-27 |
|
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: 110.22 E-value: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNP-QWLRNNIGAVSQEPVLF-SCS 536
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGIGYVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENILYGA-NPGETPSPERLQQVIEdanvsqftdQLPDgLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:cd03224 92 VEENLLLGAyARRRAKRKARLERVYE---------LFPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23397593 616 AL--DAVSEnlVQNALDNLI-QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELM 672
Cdd:cd03224 162 GLapKIVEE--IFEAIRELRdEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
461-666 |
1.05e-26 |
|
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: 108.61 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 461 AVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTvNPQWLRNNIGAVSQEPVLFS-CSIRE 539
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDrLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 540 NI-----LYGANPGETPSpeRLQQVIEDANVSQFTDQlpdgldtlvgqRGMMLSGGQKQRVAIARALIKNPAILILDEAT 614
Cdd:cd03266 98 NLeyfagLYGLKGDELTA--RLEELADRLGMEELLDR-----------RVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23397593 615 SALDAVSENLVQNALDNL-IQGRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQG 666
Cdd:cd03266 165 TGLDVMATRALREFIRQLrALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
465-666 |
1.16e-26 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 108.35 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 465 DFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwlRNNIGAVSQEPVLFS-CSIRENILY 543
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 544 GANPGETPSPERLQQVieDANVSQFtdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSEN 623
Cdd:cd03298 94 GLSPGLKLTAEDRQAI--EVALARV------GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 23397593 624 LVQNALDNLIQGR--TVLTIAHRLSTIRN-ADQIAVLSDGKIVEQG 666
Cdd:cd03298 166 EMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
447-672 |
1.22e-26 |
|
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: 109.40 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTfptRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIallmLRL---YDPQ--GGTVHLDGIDLRTVNPQWLRN 521
Cdd:COG1119 6 LRNVTVR---RGGKTILDDISWTVKPGEHWAILGPNGAGKSTL----LSLitgDLPPtyGNDVRLFGERRGGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 522 NIGAVS---QEPVLFSCSIRENILYGAN----PGETPSPE---RLQQVIEDANVSQFTDQLpdgLDTLvgqrgmmlSGGQ 591
Cdd:COG1119 79 RIGLVSpalQLRFPRDETVLDVVLSGFFdsigLYREPTDEqreRARELLELLGLAHLADRP---FGTL--------SQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 592 KQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRNA-DQIAVLSDGKIVEQGSY 668
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPK 227
|
....
gi 23397593 669 NELM 672
Cdd:COG1119 228 EEVL 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
461-685 |
1.78e-26 |
|
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: 109.12 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 461 AVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLR-----------NNIGAVSQE 529
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRafrrdvqlvfqDSPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 530 PVLfSCSIRENILYGANPGETPSPERLQQVIEDANVSqftdqlPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILI 609
Cdd:TIGR02769 105 MTV-RQIIGEPLRHLTSLDESEQKARIAELLDMVGLR------SEDADKLPRQ----LSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23397593 610 LDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNELMGIQEGVFRELVAS 685
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNLQSA 252
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
120-409 |
1.91e-26 |
|
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: 109.99 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 120 KWVLTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSaamakLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVR 199
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLAT-----LYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 200 SLRSRLYRSMLMQEVGWFDTKGTGELINRLSN-DTL---MVGTSLSQnVSDGLRSVAMIGVgtgMMIYtSPQLAAVSALV 275
Cdd:cd18782 76 ELGGTIIDHLLRLPLGFFDKRPVGELSTRISElDTIrgfLTGTALTT-LLDVLFSVIYIAV---LFSY-SPLLTLVVLAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 276 VPAMAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGL 355
Cdd:cd18782 151 VPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 23397593 356 TGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQL 409
Cdd:cd18782 231 SQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQF 284
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
462-666 |
2.03e-26 |
|
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: 107.30 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDlrTVNPQWLRNNIGAVSQEPVLF-SCSIREN 540
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS--YQKNIEALRRIGALIEAPGFYpNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 ILYGANPGETPSpERLQQVIEDANVSQFTDQLpdgldtlVGQrgmmLSGGQKQRVAIARALIKNPAILILDEATSALDAV 620
Cdd:cd03268 93 LRLLARLLGIRK-KRIDEVLDVVGLKDSAKKK-------VKG----FSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23397593 621 SENLVQNALDNLI-QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQG 666
Cdd:cd03268 161 GIKELRELILSLRdQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
120-419 |
2.34e-26 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 109.49 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 120 KWVLTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSaamakLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVR 199
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDG-----LTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 200 SLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAM 279
Cdd:cd18540 76 DLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 280 AGMAI-------VYGRYVR----RITKveldKYAE-IMkfaeerfgNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETR 347
Cdd:cd18540 156 AVVSIyfqkkilKAYRKVRkinsRITG----AFNEgIT--------GAKTTKTLVREEKNLREFKELTEEMRRASVRAAR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 348 ARAIFFGLTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18540 224 LSALFLPIVLFLGSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
448-688 |
2.75e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.05 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRPESavLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVS 527
Cdd:PRK13647 8 EDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 528 QEP--VLFSCSIRENILYGA-NPGETPSP--ERLQQVIEDANVSQFTDQLPdgldtlvgqrgMMLSGGQKQRVAIARALI 602
Cdd:PRK13647 86 QDPddQVFSSTVWDDVAFGPvNMGLDKDEveRRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 603 KNPAILILDEATSALDAVSENLVQNALDNL-IQGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSyNELMG----IQE 676
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTdediVEQ 233
|
250
....*....|..
gi 23397593 677 GVFRELVASQAF 688
Cdd:PRK13647 234 AGLRLPLVAQIF 245
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
459-684 |
3.13e-26 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 107.61 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWL-RNNIGAVSQEPVLFS-CS 536
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPrLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENILYGAnpgeTPSPERLQQVIEDAnvsqfTDQLPdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATsa 616
Cdd:TIGR03410 92 VEENLLTGL----AALPRRSRKIPDEI-----YELFP-VLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT-- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 617 lDAVSENLVQ---NALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELmgIQEGVfRELVA 684
Cdd:TIGR03410 160 -EGIQPSIIKdigRVIRRLRAegGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL--DEDKV-RRYLA 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
457-667 |
5.45e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 109.28 E-value: 5.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 457 RPESAV--LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQ---WLRNNIGAVSQEPv 531
Cdd:PRK11308 23 KPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIVFQNP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 532 lfscsirenilYGA-NPGET---------------PSPERLQQVIED-ANV---SQFTDQLPDgldtlvgqrgmMLSGGQ 591
Cdd:PRK11308 102 -----------YGSlNPRKKvgqileepllintslSAAERREKALAMmAKVglrPEHYDRYPH-----------MFSGGQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23397593 592 KQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGS 667
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQelGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
466-672 |
6.02e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 106.59 E-value: 6.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 466 FSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwlRNNIGAVSQEPVLFS-CSIRENILYG 544
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 545 ANPGETPSPE---RLQQVIEDANVSQFTDQLPdgldtlvGQrgmmLSGGQKQRVAIARALIKNPAILILDEATSALDAVS 621
Cdd:PRK10771 96 LNPGLKLNAAqreKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 622 ENLVQNALDNLIQGR--TVLTIAHRLStirNADQIA----VLSDGKIVEQGSYNELM 672
Cdd:PRK10771 165 RQEMLTLVSQVCQERqlTLLMVSHSLE---DAARIAprslVVADGRIAWDGPTDELL 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
462-672 |
8.50e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 114.11 E-value: 8.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVhldgidlrtvnpqWLRNNIGAVSQEPVLFSCSIRENI 541
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 542 LYGanpgETPSPERLQQVIEdanVSQF---TDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALD 618
Cdd:PTZ00243 742 LFF----DEEDAARLADAVR---VSQLeadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 619 A-VSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELM 672
Cdd:PTZ00243 815 AhVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM 869
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
462-667 |
1.10e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.78 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTiallMLRL----YDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVL-FSCS 536
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKST----LLRAlsgeLSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENILYGANPGeTPSPERLQQVIEDAnvsqfTDQLpdGLDTLVGQRGMMLSGGQKQRVAIARALI------KNPAILIL 610
Cdd:PRK13548 93 VEEVVAMGRAPH-GLSRAEDDALVAAA-----LAQV--DLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 611 DEATSALDAVSENLVQNALDNLI--QGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGS 667
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQLAheRGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
462-672 |
1.10e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 106.64 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVL-FSCSIREN 540
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 ILYGANP-----GetpspeRLQQviED-ANVSQFTDQLpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEAT 614
Cdd:PRK11231 97 VAYGRSPwlslwG------RLSA--EDnARVNQAMEQT--RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 615 SALDaVSEnlvQNALDNLI-----QGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNELM 672
Cdd:PRK11231 167 TYLD-INH---QVELMRLMrelntQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
454-664 |
1.67e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 106.31 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 454 FPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVN-PQW--LRNNIGAVSQEP 530
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNrAQRkaFRRDIQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 531 V-------LFSCSIRENILYGANPGETPSPERLQQVIEDANVSqftdqlPDGLDTLVGQrgmmLSGGQKQRVAIARALIK 603
Cdd:PRK10419 99 IsavnprkTVREIIREPLRHLLSLDKAERLARASEMLRAVDLD------DSVLDKRPPQ----LSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 604 NPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTI-RNADQIAVLSDGKIVE 664
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
462-658 |
3.20e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.41 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCSIRENI 541
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 542 LYganP----GETPSPERLQqviedANVSQFtdQLPdglDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSAL 617
Cdd:PRK10247 102 IF---PwqirNQQPDPAIFL-----DDLERF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 23397593 618 DAVSENLVQNALDNLI--QGRTVLTIAHRLSTIRNADQIAVLS 658
Cdd:PRK10247 169 DESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
107-672 |
3.42e-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: 111.93 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 107 SQYGRLLSLTKSEKWVLtagIGCLVV---SSAITMSVPLFLGKVIDVVFNKSGMDSAAMAKLGEYSVLL--------FGI 175
Cdd:TIGR01271 854 NTYLRYITTNRNLVFVL---IFCLVIflaEVAASLLGLWLITDNPSAPNYVDQQHANASSPDVQKPVIItptsayyiFYI 930
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 176 FV--------LGGFANFARVHLFgnaaLRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSD- 246
Cdd:TIGR01271 931 YVgtadsvlaLGFFRGLPLVHTL----LTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDf 1006
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 247 ---GLRSVAMIGVGTGMMIYTSpqLAAVSALVVPAMAGMAIVygRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCR 323
Cdd:TIGR01271 1007 iqlTLIVLGAIFVVSVLQPYIF--IAAIPVAVIFIMLRAYFL--RTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGR 1082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 324 EqqevAAFDGKLDEALQIgyketrARAIFF----GLTGFCGNFIIISVLYYGGTLVLQDSLT------IGALtafmlyag 393
Cdd:TIGR01271 1083 Q----SYFETLFHKALNL------HTANWFlylsTLRWFQMRIDIIFVFFFIAVTFIAIGTNqdgegeVGII-------- 1144
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 394 yVAISMNGLSNFYSQLNKGIGAS------ERIWEILD--RECSIPIDKG-------VVPLEKP--------VGEVGFQNV 450
Cdd:TIGR01271 1145 -LTLAMNILSTLQWAVNSSIDVDglmrsvSRVFKFIDlpQEEPRPSGGGgkyqlstVLVIENPhaqkcwpsGGQMDVQGL 1223
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 451 FFTFpTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGgTVHLDGIDLRTVNPQWLRNNIGAVSQEP 530
Cdd:TIGR01271 1224 TAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEG-EIQIDGVSWNSVTLQTWRKAFGVIPQKV 1301
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 531 VLFSCSIRENIlygaNPGETPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILIL 610
Cdd:TIGR01271 1302 FIFSGTFRKNL----DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLL 1377
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 611 DEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELM 672
Cdd:TIGR01271 1378 DEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
462-671 |
5.29e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 5.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTialLMLRL---YDPQGGTVHLDGIDLRTVNP-QWLRNNIGAVSQEPVLFSC-S 536
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKST---LMKILsgvYQPDSGEILLDGEPVRFRSPrDAQAAGIAIIHQELNLVPNlS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENILYGANPGETPSP------ERLQQVIEDANVSqftdqLPdgLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILIL 610
Cdd:COG1129 96 VAENIFLGREPRRGGLIdwramrRRARELLARLGLD-----ID--PDTPVGD----LSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 611 DEATSALDAV-SENLVqnaldNLI-----QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNEL 671
Cdd:COG1129 165 DEPTASLTEReVERLF-----RIIrrlkaQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
462-670 |
6.12e-25 |
|
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: 103.86 E-value: 6.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwlRNNIGAVSQEPVLFS-CSIREN 540
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPhLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 ILYGANPGETPSPERLQQVIEDANVSQftdqlpdgLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAV 620
Cdd:cd03300 93 IAFGLRLKKLPKAEIKERVAEALDLVQ--------LEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 621 SENLVQNALDNLIQ--GRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGS----YNE 670
Cdd:cd03300 165 LRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTpeeiYEE 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
462-667 |
6.14e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 107.34 E-value: 6.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwlRNNIGAVSQEPVLFS-CSIREN 540
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFPhMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 ILYGANPGETPSPERLQQVIEDANVSQftdqlpdgLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAV 620
Cdd:PRK09452 107 VAFGLRMQKTPAAEITPRVMEALRMVQ--------LEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 23397593 621 SENLVQNALDNLiQ---GRTVLTIAH-RLSTIRNADQIAVLSDGKIVEQGS 667
Cdd:PRK09452 179 LRKQMQNELKAL-QrklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
462-667 |
7.39e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.43 E-value: 7.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTiallMLRL----YDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVL-FSCS 536
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKST----LLKLltgeLTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLaFPFT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENILYGANPGETPSPERlQQVIEDAnVSQFtdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALI-------KNPAILI 609
Cdd:COG4559 92 VEEVVALGRAPHGSSAAQD-RQIVREA-LALV------GLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 610 LDEATSALD--------AVSENLVQnaldnliQGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGS 667
Cdd:COG4559 164 LDEPTSALDlahqhavlRLARQLAR-------RGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGT 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
462-663 |
8.16e-25 |
|
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: 101.35 E-value: 8.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQ-WLRNNIGAVSQepvlfscsiren 540
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 ilyganpgetpsperlqqviedanvsqftdqlpdgldtlvgqrgmmLSGGQKQRVAIARALIKNPAILILDEATSALDAV 620
Cdd:cd03216 83 ----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 23397593 621 SENLVQNALDNLI-QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIV 663
Cdd:cd03216 117 EVERLFKVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
448-676 |
1.70e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 103.63 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVS 527
Cdd:PRK13642 8 ENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 528 QEP--VLFSCSIRENILYGANPGETPSPERLQQVIE---DANVSQFTDQLPdgldtlvgqrgMMLSGGQKQRVAIARALI 602
Cdd:PRK13642 88 QNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEallAVNMLDFKTREP-----------ARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 603 KNPAILILDEATSALDAVSENLVQNALDNLIQGR--TVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGIQE 676
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
459-667 |
2.03e-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: 107.85 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQ----GGTVHLDGIDLRTVNPQWLR----NNIGAVSQEP 530
Cdd:COG4172 22 TVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERELRrirgNRIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 531 V-----LFScsIRENIlyganpGET-------PSPERLQQVIEdanvsqftdqlpdgLDTLVG-------------Qrgm 585
Cdd:COG4172 102 MtslnpLHT--IGKQI------AEVlrlhrglSGAAARARALE--------------LLERVGipdperrldayphQ--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 586 mLSGGQKQRVAIARALIKNPAILILDEATSALDAVsenlVQ----NALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLS 658
Cdd:COG4172 157 -LSGGQRQRVMIAMALANEPDLLIADEPTTALDVT----VQaqilDLLKDLQRelGMALLLITHDLGVVRRfADRVAVMR 231
|
....*....
gi 23397593 659 DGKIVEQGS 667
Cdd:COG4172 232 QGEIVEQGP 240
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
448-673 |
3.35e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.89 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGiDLRTVNPQW-LRNNIGAV 526
Cdd:PRK13650 8 KNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEENVWdIRHKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEP--VLFSCSIRENILYG-ANPGETPSP--ERLQQVIEDANVSQFTDQLPdgldtlvgqrgMMLSGGQKQRVAIARAL 601
Cdd:PRK13650 87 FQNPdnQFVGATVEDDVAFGlENKGIPHEEmkERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 602 IKNPAILILDEATSALDAvsenlvQNALDnLIQ---------GRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELM 672
Cdd:PRK13650 156 AMRPKIIILDEATSMLDP------EGRLE-LIKtikgirddyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELF 228
|
.
gi 23397593 673 G 673
Cdd:PRK13650 229 S 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
462-671 |
3.75e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 103.26 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNpqwlRNNIGAVSQEPVLF-SCSIREN 540
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMKVGEQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 ILY-----GANPGEtpSPERLQQVIEdanvsQFtdQLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:COG4152 92 LVYlarlkGLSKAE--AKRRADEWLE-----RL--GLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 616 ALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNEL 671
Cdd:COG4152 159 GLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
459-667 |
4.93e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.71 E-value: 4.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGtVHLDGIDLRTVNPQWL---RNNIGAVSQEPvlfsc 535
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGE-IWFDGQPLHNLNRRQLlpvRHRIQVVFQDP----- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 536 sirenilYGA-NPgetpspeRL--QQVIEDA--------NVSQFTDQLPD-----GLDTLVGQR-GMMLSGGQKQRVAIA 598
Cdd:PRK15134 372 -------NSSlNP-------RLnvLQIIEEGlrvhqptlSAAQREQQVIAvmeevGLDPETRHRyPAEFSGGQRQRIAIA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 599 RALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTV--LTIAHRLSTIRN-ADQIAVLSDGKIVEQGS 667
Cdd:PRK15134 438 RALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQGD 509
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
462-666 |
5.08e-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: 100.41 E-value: 5.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwlRNNIGAVSQEPVLF-SCSIREN 540
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVFQNYALYpHMTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 ILYGANPGETPSPERLQQVIEDANVSQftdqlpdgLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAV 620
Cdd:cd03301 93 IAFGLKLRKVPKDEIDERVREVAELLQ--------IEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 23397593 621 SENLVQNALDNLIQ--GRTVLTIAH-RLSTIRNADQIAVLSDGKIVEQG 666
Cdd:cd03301 165 LRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
463-671 |
1.16e-23 |
|
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: 100.49 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwlRNNIGAVSQEPVLFS-CSIRENI 541
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 542 LYG-------ANPGETPSPERLQQVIEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIARALIKNPAILILDEAT 614
Cdd:cd03296 96 AFGlrvkprsERPPEAEIRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 615 SALDA-VSENL---VQNALDNLiqGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNEL 671
Cdd:cd03296 165 GALDAkVRKELrrwLRRLHDEL--HVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
454-686 |
2.03e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 100.30 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 454 FPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLR--------------------T 513
Cdd:COG4167 20 LFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygdykyrckhirmifqdpntS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 514 VNPqwlRNNIGAVSQEPVLFSCSIRENilyganpgetpspERLQQVIEdanvsqftdqlpdgldTLvGQRGM-------- 585
Cdd:COG4167 100 LNP---RLNIGQILEEPLRLNTDLTAE-------------EREERIFA----------------TL-RLVGLlpehanfy 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 586 --MLSGGQKQRVAIARALIKNPAILILDEATSALDAVsenlVQNALDNLI------QGRTVLTIAHRLSTIRN-ADQIAV 656
Cdd:COG4167 147 phMLSSGQKQRVALARALILQPKIIIADEALAALDMS----VRSQIINLMlelqekLGISYIYVSQHLGIVKHiSDKVLV 222
|
250 260 270
....*....|....*....|....*....|.
gi 23397593 657 LSDGKIVEQGSYNELMG-IQEGVFRELVASQ 686
Cdd:COG4167 223 MHQGEVVEYGKTAEVFAnPQHEVTKRLIESH 253
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
463-692 |
2.91e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.80 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLR----NNIGAVSQEPVLFS-CSI 537
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 538 RENILYGANPGETPSPERLQQVIE---DANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIARALIKNPAILILDEAT 614
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDalrQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 615 SALDAVSENLVQNALDNL--IQGRTVLTIAHRL-STIRNADQIAVLSDGKIVEQGSYNELMG-----IQEGVFRELVASQ 686
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNnpandYVRTFFRGVDISQ 272
|
....*.
gi 23397593 687 AFGSRN 692
Cdd:PRK10070 273 VFSAKD 278
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
459-672 |
4.74e-23 |
|
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: 98.52 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWL-RNNIGAVSQEPVLF-SCS 536
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFpSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENILYGANPGetPSPERLQQVIEDAnvsqfTDQLPDgLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSA 616
Cdd:COG0410 95 VEENLLLGAYAR--RDRAEVRADLERV-----YELFPR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23397593 617 LdavSENLVQ---NALDNLI-QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELM 672
Cdd:COG0410 167 L---APLIVEeifEIIRRLNrEGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELL 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
459-671 |
7.41e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.58 E-value: 7.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRL---YDPQ---GGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVL 532
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 533 FS-CSIRENILYGANPGETPSPERLQQVIEDA-NVSQFTDQLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILIL 610
Cdd:PRK14246 102 FPhLSIYDNIAYPLKSHGIKEKREIKKIVEEClRKVGLWKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 611 DEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
126-419 |
9.64e-23 |
|
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: 99.66 E-value: 9.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 126 GIGCLVVSSAITMSVPLFLGKVIDVvFNKSGMDSAAMAKLGE----------------YSVLLFGIFVLGGFANFARVHL 189
Cdd:cd18558 4 GILCAIIHGGLLPAFMVIFGDMTDS-FTNGGMTNITGNSSGLnssagpfekleeemtlYAYYYLIIGAIVLITAYIQGSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 190 FGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLA 269
Cdd:cd18558 83 WGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 270 AVSALVVPAMAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRAR 349
Cdd:cd18558 163 LVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITF 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 350 AIFFGLTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18558 243 NISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
447-662 |
9.98e-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: 96.71 E-value: 9.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPtrPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGID---LRTVNPQWLRNNI 523
Cdd:cd03292 3 FINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 524 GAVSQE-PVLFSCSIRENILY-----GANPGETPspERLQQVIEDANVSQFTDQLPdgldtlvgqrgMMLSGGQKQRVAI 597
Cdd:cd03292 81 GVVFQDfRLLPDRNVYENVAFalevtGVPPREIR--KRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 598 ARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQ--IAVLSDGKI 662
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
449-688 |
1.19e-22 |
|
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: 98.39 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 449 NVFFTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGidlrtvnpqwlrnNIGAVSQ 528
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 529 EPVLFSCSIRENILYGANPGETpspeRLQQVIEDANVSQFTDQLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAIL 608
Cdd:cd03291 106 FSWIMPGTIKENIIFGVSYDEY----RYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 609 ILDEATSALDAVSENLV-QNALDNLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSYNELMGIQEGVFRELVASQA 687
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDT 261
|
.
gi 23397593 688 F 688
Cdd:cd03291 262 F 262
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
112-612 |
1.31e-22 |
|
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: 102.18 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 112 LLSLTKSEKWVLTAGIGCLVVSSAITMSVPLFLGKVIdvvfnkSGMDSAAMAKLGEYSVLLFGIFVLGGFANFARVHLfg 191
Cdd:COG4615 4 LRLLLRESRWLLLLALLLGLLSGLANAGLIALINQAL------NATGAALARLLLLFAGLLVLLLLSRLASQLLLTRL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 192 naALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVgTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAV 271
Cdd:COG4615 76 --GQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 272 SALVvpaMAGMAIVYGRYVRRITKvELDKYAEimkfAEER-FGNVKTVKTFCRE----QQEVAAFdgkLDEALQ---IGY 343
Cdd:COG4615 153 TLVL---LGLGVAGYRLLVRRARR-HLRRARE----AEDRlFKHFRALLEGFKElklnRRRRRAF---FDEDLQptaERY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 344 KETRARAIFFgltgFCGNFIIISVLYYG--GTLV----LQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASE 417
Cdd:COG4615 222 RDLRIRADTI----FALANNWGNLLFFAliGLILfllpALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 418 RIWEI---LDRECSIPIDKGVVPLEKPVGEVGFQNVFFTFPTRPESAVLT----DFSLNlmPGTTTAVVGRSGSGKTTIA 490
Cdd:COG4615 298 KIEELelaLAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDEGFTlgpiDLTIR--RGELVFIVGGNGSGKSTLA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 491 LLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFScsiReniLYGanPGETPSPERLQQVIED---ANVSQ 567
Cdd:COG4615 376 KLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD---R---LLG--LDGEADPARARELLERlelDHKVS 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 23397593 568 FTDqlpDGLDTLvgqrgmMLSGGQKQRVAIARALIKNPAILILDE 612
Cdd:COG4615 448 VED---GRFSTT------DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
456-666 |
1.47e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 100.69 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 456 TRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVL-FS 534
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENILYGANP------GETPSPER-LQQVIEDANVSQFTDQLPDGLdtlvgqrgmmlSGGQKQRVAIARALIKNPAI 607
Cdd:PRK09536 92 FDVRQVVEMGRTPhrsrfdTWTETDRAaVERAMERTGVAQFADRPVTSL-----------SGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 608 LILDEATSALD---AVSE-NLVQNALDNliqGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQG 666
Cdd:PRK09536 161 LLLDEPTASLDinhQVRTlELVRRLVDD---GKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
141-690 |
1.49e-22 |
|
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: 103.45 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 141 PLFLGKVIDVV--FNKSGMDSAAMAKLGeYSVLLFGIFVLGGFANFARVHLfgNAALRIvrSLRSRLYRSMLMQEVGWFD 218
Cdd:TIGR01271 100 PLLLGRIIASYdpFNAPEREIAYYLALG-LCLLFIVRTLLLHPAIFGLHHL--GMQMRI--ALFSLIYKKTLKLSSRVLD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 219 TKGTGELINRLSN--DTLMVGTSLSQNVSDGLRSVAMIgVGTGMMIYTSPQLAAVSALVVPAM--AGMAIVYGRYVRRit 294
Cdd:TIGR01271 175 KISTGQLVSLLSNnlNKFDEGLALAHFVWIAPLQVILL-MGLIWELLEVNGFCGLGFLILLALfqACLGQKMMPYRDK-- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 295 kvELDKYAEIMKFAEERFGNVKTVKTFCREQqevaAFDGKLDEALQIGYKETRAraiffglTGFCGNFIIiSVLYYGGTL 374
Cdd:TIGR01271 252 --RAGKISERLAITSEIIENIQSVKAYCWEE----AMEKIIKNIRQDELKLTRK-------IAYLRYFYS-SAFFFSGFF 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 375 VLQDSLTIGALT-AFMLYAGYVAISMN-------------GLSNFYSQLnkgiGASERIWEILDRE-----------CSI 429
Cdd:TIGR01271 318 VVFLSVVPYALIkGIILRRIFTTISYCivlrmtvtrqfpgAIQTWYDSL----GAITKIQDFLCKEeyktleynlttTEV 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 430 PIDKGVVPLEKPVGEV---------------GFQNVFFTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLML 494
Cdd:TIGR01271 394 EMVNVTASWDEGIGELfekikqnnkarkqpnGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 495 RLYDPQGGTVHLDGidlrtvnpqwlrnNIGAVSQEPVLFSCSIRENILYGANPGETpspeRLQQVIEDANVSQFTDQLPD 574
Cdd:TIGR01271 474 GELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNIIFGLSYDEY----RYTSVIKACQLEEDIALFPE 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 575 GLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSE-NLVQNALDNLIQGRTVLTIAHRLSTIRNADQ 653
Cdd:TIGR01271 537 KDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkEIFESCLCKLMSNKTRILVTSKLEHLKKADK 616
|
570 580 590
....*....|....*....|....*....|....*..
gi 23397593 654 IAVLSDGKIVEQGSYNELMGIQEGVFRELVASQAFGS 690
Cdd:TIGR01271 617 ILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFDN 653
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
462-671 |
1.52e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.51 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDL---RTVNPQW-----LRNNIGAVSQEPVLF 533
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQKglirqLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 534 SC-SIRENILYG-----ANPGETpSPERLQQVIEDANVSQFTDQLPdgldtlvgQRgmmLSGGQKQRVAIARALIKNPAI 607
Cdd:PRK11264 98 PHrTVLENIIEGpvivkGEPKEE-ATARARELLAKVGLAGKETSYP--------RR---LSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 608 LILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
467-671 |
1.64e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 99.01 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 467 SLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNP-QWL--RNNIGAVSQEPvLFSCSIRENIly 543
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdEWRavRSDIQMIFQDP-LASLNPRMTI-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 544 G---ANPGETPSPERLQQVIEDaNVSQFTDQ---LPDgldtLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSAL 617
Cdd:PRK15079 118 GeiiAEPLRTYHPKLSRQEVKD-RVKAMMLKvglLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23397593 618 DaVSenlVQNALDNLIQ------GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK15079 193 D-VS---IQAQVVNLLQqlqremGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
457-671 |
1.91e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 102.05 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 457 RPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTialLM--LRLYDPQG----GTVHLDGidlRTVNPQWLRNNIGAVSQEP 530
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTT---LMnaLAFRSPKGvkgsGSVLLNG---MPIDAKEMRAISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 531 VLF-SCSIRENILYGAN---PGETPSPE---RLQQVIEDANvsqftdqLPDGLDTLVGQRGMM--LSGGQKQRVAIARAL 601
Cdd:TIGR00955 109 LFIpTLTVREHLMFQAHlrmPRRVTKKEkreRVDEVLQALG-------LRKCANTRIGVPGRVkgLSGGERKRLAFASEL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLST--IRNADQIAVLSDGKIVEQGSYNEL 671
Cdd:TIGR00955 182 LTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQkGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
462-671 |
2.06e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.91 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYD--PQG---GTVHLDGIDLRTVNPQWLRNNIGAVSQEP-VLFSC 535
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 536 SIRENILYGAN-----PGETPSPERLQQVIEDAnvsQFTDQLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILIL 610
Cdd:PRK14247 98 SIFENVALGLKlnrlvKSKKELQERVRWALEKA---QLWDEVKDRLDAPAGK----LSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 611 DEATSALDAVSENLVQNALDNLIQGRTVLTIAH-RLSTIRNADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
460-671 |
3.99e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 98.25 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 460 SAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwlRNNIGAVSQEPVLFS-CSIR 538
Cdd:PRK11432 19 NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPhMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 539 ENILYGANPGETPSPERLQQV---IEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:PRK11432 97 ENVGYGLKMLGVPKEERKQRVkeaLELVDLAGFEDRYVD-----------QISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 616 ALDAvseNLVQNALDNL--IQGR---TVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK11432 166 NLDA---NLRRSMREKIreLQQQfniTSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
462-666 |
5.38e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 95.46 E-value: 5.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIaLLMLRLYD-PQGGTVHLDG--IDL-RTVNP---QWLRNNIGAVSQE----P 530
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSL-LRVLNLLEtPDSGQLNIAGhqFDFsQKPSEkaiRLLRQKVGMVFQQynlwP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 531 VLfscSIRENILyganpgETP----------SPERLQQVIEDANVSQFTDQLPdgldtlvgqrgMMLSGGQKQRVAIARA 600
Cdd:COG4161 96 HL---TVMENLI------EAPckvlglskeqAREKAMKLLARLRLTDKADRFP-----------LHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 601 LIKNPAILILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQG 666
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKvASQVVYMEKGRIIEQG 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
462-672 |
5.64e-22 |
|
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: 95.20 E-value: 5.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwLRNNIGAVS--QEPVLF-SCSIR 538
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 539 ENILYGANPGETPSPERLQQVIEDANVSQFTDQ------LPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDE 612
Cdd:cd03219 94 ENVMVAAQARTGSGLLLARARREEREARERAEEllervgLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 613 ATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELM 672
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
447-667 |
5.87e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 5.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTrpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDlrTVNP---QWLRNNI 523
Cdd:PRK13644 4 LENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFsklQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 524 GAVSQEP--VLFSCSIRENILYGANPGETPSPE---RLQQVIEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIA 598
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEirkRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 599 RALIKNPAILILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGS 667
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
462-666 |
5.97e-22 |
|
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: 95.03 E-value: 5.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTT-IALLMLRLYDPQ--GGTVHLDGidlRTVNPQWLRNNIGAVSQEPVLFSC-SI 537
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTlLDAISGRVEGGGttSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 538 RENILYGAN---PGETPSPERlQQVIEDANVSQFTDqlpdgldTLVGQRGMM-LSGGQKQRVAIARALIKNPAILILDEA 613
Cdd:cd03234 99 RETLTYTAIlrlPRKSSDAIR-KKRVEDVLLRDLAL-------TRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 614 TSALDAVSENLVQNALDNLIQ-GRTVLTIAH--RLSTIRNADQIAVLSDGKIVEQG 666
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
462-664 |
1.38e-21 |
|
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: 94.04 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTiaLLMLR--LYDPQGGTVHLDGIDLRTVN----PQWLRNNIGAVSQ-EPVLFS 534
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKST--LLGLLagLDRPTSGTVRLAGQDLFALDedarARLRARHVGFVFQsFQLLPT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENI-----LYGANPGETPSPERLQQViedanvsqftdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILI 609
Cdd:COG4181 105 LTALENVmlpleLAGRRDARARARALLERV---------------GLGHRLDHYPAQLSGGEQQRVALARAFATEPAILF 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 610 LDEATSALDAVSENLVQNALDNL--IQGRTVLTIAHRLSTIRNADQIAVLSDGKIVE 664
Cdd:COG4181 170 ADEPTGNLDAATGEQIIDLLFELnrERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
447-668 |
2.49e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGiDLRtvnpqwlrnnIGAV 526
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEPVLFS-CSIRENILYGANP--------------GETPSPE-----RLQQVIE-------DANVSQFTDQL---PDGL 576
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAElraleaeleeleakLAEPDEDlerlaELQEEFEalggweaEARAEEILSGLgfpEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 577 DTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDEATSALDAVS----ENLVQNaldnlIQGrTVLTIAH-R--LSTIr 649
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKN-----YPG-TVLVVSHdRyfLDRV- 215
|
250 260
....*....|....*....|
gi 23397593 650 nADQIAVLSDGKIVE-QGSY 668
Cdd:COG0488 216 -ATRILELDRGKLTLyPGNY 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
445-667 |
2.84e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.43 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 445 VGFQNVFFTFP--TRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLR--TVNP--QW 518
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstSKNKdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 519 LRNNIGAVSQ--EPVLFSCSIRENILYGanpgetpsPERLQQVIEDANVSQFTDQLPDGLD-TLVGQRGMMLSGGQKQRV 595
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG--------PQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 596 AIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGS 667
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
462-671 |
7.24e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.66 E-value: 7.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNP-QWLRNNIGAVSQEPVLF-SCSIRE 539
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPaKAHQLGIYLVPQEPLLFpNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 540 NILYGAnPGETPSPERLQQVIEDANVsqftdQLpdGLDTLVGqrgmMLSGGQKQRVAIARALIKNPAILILDEATSALDA 619
Cdd:PRK15439 106 NILFGL-PKRQASMQKMKQLLAALGC-----QL--DLDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23397593 620 V-SENLVQNALDNLIQGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK15439 174 AeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
445-673 |
7.93e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 93.31 E-value: 7.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 445 VGFQNVFFTFP--TRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGID---------LRT 513
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 514 VnpqwlRNNIGAVSQ--EPVLFSCSIRENILYGanpgetpsPERLQQVIEDANVSQFTDQLPDGLD-TLVGQRGMMLSGG 590
Cdd:PRK13646 83 V-----RKRIGMVFQfpESQLFEDTVEREIIFG--------PKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 591 QKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLI--QGRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQGS 667
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTS 229
|
....*.
gi 23397593 668 YNELMG 673
Cdd:PRK13646 230 PKELFK 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
465-663 |
7.99e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 96.25 E-value: 7.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 465 DFSLNLMPGTTTAVVGRSGSGKTTialLM--LR-LYDPQGGTVHLDGIDLRTVNPQ-WLRNNIGAVSQEPVLF-SCSIRE 539
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKST---LMkiLYgLYQPDSGEILIDGKPVRIRSPRdAIALGIGMVHQHFMLVpNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 540 NILYGANPGETPSP------ERLQQVIEDANvsqftdqLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDEA 613
Cdd:COG3845 100 NIVLGLEPTKGGRLdrkaarARIRELSERYG-------LDVDPDAKVED----LSVGEQQRVEILKALYRGARILILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 23397593 614 TSAL-DAVSENLVQnALDNLI-QGRTVLTIAHRLSTIR-NADQIAVLSDGKIV 663
Cdd:COG3845 169 TAVLtPQEADELFE-ILRRLAaEGKSIIFITHKLREVMaIADRVTVLRRGKVV 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
459-681 |
8.28e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 93.19 E-value: 8.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDL--RTVNPQWLRNNIGAVSQEP--VLFS 534
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENILYG-ANPGETPSpERLQQVIEDANVSqftdqlpdGLD--TLVGQRGMMLSGGQKQRVAIARALIKNPAILILD 611
Cdd:PRK13637 99 ETIEKDIAFGpINLGLSEE-EIENRVKRAMNIV--------GLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397593 612 EATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTI-RNADQIAVLSDGKIveqgsynELMGIQEGVFRE 681
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKC-------ELQGTPREVFKE 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
463-676 |
1.10e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.60 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDG--IDLRTVNPQWLRNNIGAVSQEP--VLFSCSIR 538
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 539 ENILYGANPGETPSPE---RLQQVIEDANVSQFTDQlPDgldtlvgqrgMMLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:PRK13636 102 QDVSFGAVNLKLPEDEvrkRVDNALKRTGIEHLKDK-PT----------HCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 616 ALD--AVSE--NLVQNALDNLiqGRTVLTIAHRLSTIR-NADQIAVLSDGKIVEQGSYNELMGIQE 676
Cdd:PRK13636 171 GLDpmGVSEimKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
465-671 |
1.28e-20 |
|
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: 90.89 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 465 DFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTvNPQWLRNNIGAVSQEPVL-FSCSIRENILY 543
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVdDELTGWENLYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 544 GANPGETPSPERLQQVIEdanVSQFTDqLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDEATSALDAVSEN 623
Cdd:cd03265 97 HARLYGVPGAERRERIDE---LLDFVG-LLEAADRLVKT----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 23397593 624 LVQNALDNLI--QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNEL 671
Cdd:cd03265 169 HVWEYIEKLKeeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
454-643 |
1.42e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 91.68 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 454 FPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIdlRTVNPQWLRnniGAVSQ-EPVL 532
Cdd:PRK11248 11 YGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK--PVEGPGAER---GVVFQnEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 533 FSCSIRENILYGANPGETPSPERLQQVIED-ANVsqftdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILD 611
Cdd:PRK11248 83 PWRNVQDNVAFGLQLAGVEKMQRLEIAHQMlKKV---------GLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....
gi 23397593 612 EATSALDAVSENLVQNALDNLIQ--GRTVLTIAH 643
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQetGKQVLLITH 187
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
476-670 |
1.77e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 93.40 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 476 TAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGidlRTVNPQ----WL---RNNIGAVSQEPVLFS-CSIRENILYGANP 547
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG---RVLFDAekgiCLppeKRRIGYVFQDARLFPhYKVRGNLRYGMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 548 getpsperlqqviedANVSQFtDQLPD--GLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLV 625
Cdd:PRK11144 104 ---------------SMVAQF-DKIVAllGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 23397593 626 QNALDNLiqGRTV----LTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNE 670
Cdd:PRK11144 168 LPYLERL--AREInipiLYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
462-672 |
2.22e-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: 90.68 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNP-QWLRNNIGAVSQEPVLF-SCSIRE 539
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFrKLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 540 NI---LYGANPGETPSPERLQQVIEDANvsqftdqlpdgLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSA 616
Cdd:cd03218 95 NIlavLEIRGLSKKEREEKLEELLEEFH-----------ITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 617 LDAVSENLVQNALDNLIQ-GRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNELM 672
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDrGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
465-671 |
2.55e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.36 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 465 DFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPqwLRNNIGAVSQEPVLFS-CSIRENILY 543
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQSYALFPhMTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 544 GANPGETPSPE---RLQQVIEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIARALIKNPAILILDEATSALDAV 620
Cdd:PRK11607 115 GLKQDKLPKAEiasRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23397593 621 SENLVQNALDNLIQ--GRTVLTIAH-RLSTIRNADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK11607 184 LRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
141-395 |
3.35e-20 |
|
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: 91.41 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 141 PLFLGKVIDVVFNKSGMDSAAmaklgeysVLLFGIFVLGGFA---NFARVHLFGNAALRIVRSLRSRLYRSMLMQEVGWF 217
Cdd:cd18588 22 PLFFQVIIDKVLVHRSLSTLD--------VLAIGLLVVALFEavlSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 218 DTKGTGELINRLSN-DTL---MVGTSLSQnVSDGLRSVAMIGVgtgmMIYTSPQLAAVSALVVPAMAGMAIVYGRYVRRI 293
Cdd:cd18588 94 ESRQVGDTVARVRElESIrqfLTGSALTL-VLDLVFSVVFLAV----MFYYSPTLTLIVLASLPLYALLSLLVTPILRRR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 294 TKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIIISVLYYGGT 373
Cdd:cd18588 169 LEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAY 248
|
250 260
....*....|....*....|..
gi 23397593 374 LVLQDSLTIGALTAFMLYAGYV 395
Cdd:cd18588 249 LVMDGELTIGQLIAFNMLAGQV 270
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
462-666 |
8.60e-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: 88.11 E-value: 8.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNpqwlRNNIGAVSQEPVLF-SCSIREN 540
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 ILYGANPGETPSPERLQQVIEDANVSQFTDQLPDGLDTlvgqrgmmLSGGQKQRVAIARALIKNPAILILDEATSALDAV 620
Cdd:cd03269 91 LVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEE--------LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23397593 621 SENLVQNALDNLI-QGRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQG 666
Cdd:cd03269 163 NVELLKDVIRELArAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
460-666 |
1.02e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.92 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 460 SAVLTDFSLNLMPGTTTAVVGRSGSGKTTIaLLMLRLYD-PQGGTVHLDG--IDL-RTVNPQ---WLRNNIGAVSQE--- 529
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSSL-LRVLNLLEmPRSGTLNIAGnhFDFsKTPSDKairELRRNVGMVFQQynl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 530 -PVLfscSIRENILyganpgETP----------SPERLQQVIEDANVSQFTDQLPdgldtlvgqrgMMLSGGQKQRVAIA 598
Cdd:PRK11124 94 wPHL---TVQQNLI------EAPcrvlglskdqALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 599 RALIKNPAILILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQG 666
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
463-659 |
1.31e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.07 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYD-----PQGGTVHLDGIDL--RTVNPQWLRNNIGAVSQEPVLFSC 535
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 536 SIRENILYGA--NPGETPSPERLQQVIEDAnvsQFTDQLPDGLDtlvgQRGMMLSGGQKQRVAIARALIKNPAILILDEA 613
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMDELVERSLRQA---ALWDEVKDKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 23397593 614 TSALDAVSENLVQNALDNLIQGRTVLTIAHrlstirNADQIAVLSD 659
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTH------NMQQAARVSD 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
445-672 |
1.38e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 88.61 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 445 VGFQNVFFTFPtrpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTiallMLR----LYDPQGGTVHLDGIDLR--TVNPQW 518
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKST----LLRcinkLEEITSGDLIVDGLKVNdpKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 519 LRNNIGAVSQEPVLF-SCSIRENILYGanpgetpsPERLQQVIEDANVSQFTDQLPD-GLDTLVGQRGMMLSGGQKQRVA 596
Cdd:PRK09493 75 IRQEAGMVFQQFYLFpHLTALENVMFG--------PLRVRGASKEEAEKQARELLAKvGLAERAHHYPSELSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 597 IARALIKNPAILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELM 672
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
462-670 |
1.43e-19 |
|
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: 88.94 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTT-IALLMlRLYDPQGGTVHLDGIDLRTVNPqWLRNNIGaVS---QEPVLF-SCS 536
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTlFNLIT-GFYRPTSGRILFDGRDITGLPP-HRIARLG-IArtfQNPRLFpELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENILYGANPGETPSPERL-----QQVIEDANVSQFTDQLPD--GLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILI 609
Cdd:COG0411 96 VLENVLVAAHARLGRGLLAAllrlpRARREEREARERAEELLErvGLADRADEPAGNLSYGQQRRLEIARALATEPKLLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23397593 610 LDEATSALDAV-SENLVQnaldnLIQ------GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNE 670
Cdd:COG0411 176 LDEPAAGLNPEeTEELAE-----LIRrlrderGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
438-671 |
1.59e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.94 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 438 LEKPVGEVGFQNVFFTFPTRpesAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQG-----GTVHLDGIDL- 511
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 512 -RTVNPQWLRNNIGAVSQEPVLFSCSIRENILYGAN-PGETPSPErLQQVIEDANVSQftdQLPDGLDTLVGQRGMMLSG 589
Cdd:PRK14258 78 eRRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKiVGWRPKLE-IDDIVESALKDA---DLWDEIKHKIHKSALDLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 590 GQKQRVAIARALIKNPAILILDEATSALDAVS----ENLVQNAldNLIQGRTVLTIAHrlstirNADQIAVLSD------ 659
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQSL--RLRSELTMVIVSH------NLHQVSRLSDftaffk 225
|
250
....*....|....*...
gi 23397593 660 ------GKIVEQGSYNEL 671
Cdd:PRK14258 226 gnenriGQLVEFGLTKKI 243
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
463-672 |
1.72e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 88.36 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYdPQGGTVHLDGIDLRTVNPQ-------WLRNNIGAVSQEPVLFSC 535
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAelarhraYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 536 SireniLYGANPGETPSPERLqqviedanVSQFTDQLpdGLDTLVGQRGMMLSGGQKQRVAIARALIK-----NP--AIL 608
Cdd:COG4138 91 A-----LHQPAGASSEAVEQL--------LAQLAEAL--GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptiNPegQLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 609 ILDEATSALDAVSenlvQNALDNLI-----QGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNELM 672
Cdd:COG4138 156 LLDEPMNSLDVAQ----QAALDRLLrelcqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
463-619 |
1.81e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.15 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQ---GGTVHLDGIDLRTVNPQwlRNNIGAVSQEPVLFS-CSIR 538
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 539 ENILYGAnPGETPSPER---LQQVIEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:COG4136 95 ENLAFAL-PPTIGRAQRrarVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
....
gi 23397593 616 ALDA 619
Cdd:COG4136 163 KLDA 166
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
449-671 |
1.89e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 88.98 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 449 NVFFTFPTrpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWL--RNNIGAV 526
Cdd:PRK13639 6 DLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEP--VLFSCSIRENILYGA-NPG--ETPSPERLQQVIEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIARAL 601
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVAFGPlNLGlsKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNL-IQGRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
448-663 |
2.37e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.22 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTF--PTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTiallMLRL----YDPQGGTVHLDGIDLrTVNPQWLR- 520
Cdd:COG1101 5 KNLSKTFnpGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAiagsLPPDSGSILIDGKDV-TKLPEYKRa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 521 NNIGAVSQEPVLFSC---SIRENILYGANPGETPSperLQQVIEDANVSQFTDQ-------LPDGLDTLVGQrgmmLSGG 590
Cdd:COG1101 80 KYIGRVFQDPMMGTApsmTIEENLALAYRRGKRRG---LRRGLTKKRRELFRELlatlglgLENRLDTKVGL----LSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 591 QKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGR--TVLTIAHRLS-TIRNADQIAVLSDGKIV 663
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
440-670 |
2.82e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 440 KPVGEVgfQNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLdGIDLRtvnpqwl 519
Cdd:COG0488 313 KKVLEL--EGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 520 rnnIGAVSQEpvlfscsiRENIlygaNPGETPSPErLQQVIEDANVSQFTDQL------PDGLDTLVGQrgmmLSGGQKQ 593
Cdd:COG0488 380 ---IGYFDQH--------QEEL----DPDKTVLDE-LRDGAPGGTEQEVRGYLgrflfsGDDAFKPVGV----LSGGEKA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 594 RVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLiQGrTVLTIAH-R--LSTIrnADQIAVLSDGKIVE-QGSYN 669
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYD 515
|
.
gi 23397593 670 E 670
Cdd:COG0488 516 D 516
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
131-409 |
3.24e-19 |
|
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: 88.67 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 131 VVSSAITMSVPLFLGKVIDVVFNKSGMDSAAMAKLGeysvlLFGIFVLGGFANFARVHLFGNAALRIVRSLRSRLYRSML 210
Cdd:cd18567 12 LALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIG-----FGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 211 MQEVGWFDTKGTGELINRL-SNDTL--MVGTSLSQNVSDGLRSVAMIGVgtgMMIYtSPQLAAVSALVVPAMAGMAIVYG 287
Cdd:cd18567 87 RLPLSYFEKRHLGDIVSRFgSLDEIqqTLTTGFVEALLDGLMAILTLVM---MFLY-SPKLALIVLAAVALYALLRLALY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 288 RYVRRITKVELDKYA-------EIMKfaeerfgNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCG 360
Cdd:cd18567 163 PPLRRATEEQIVASAkeqshflETIR-------GIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLF 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 23397593 361 NFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQL 409
Cdd:cd18567 236 GLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDKLFEL 284
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
463-660 |
4.74e-19 |
|
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: 86.75 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLrnnigAVSQEPVLFS-CSIRENI 541
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 542 LYGANPGETPSPERLQQVIEDANVSQFtdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVS 621
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALV------GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 23397593 622 ENLVQNALDNLIQ--GRTVLTIAHRL-STIRNADQIAVLSDG 660
Cdd:TIGR01184 150 RGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
455-643 |
5.35e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 87.22 E-value: 5.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 455 PTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTvnPQWLRnniGAVSQEPVLFS 534
Cdd:COG4525 15 GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADR---GVVFQKDALLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 -CSIRENILYGANPGETPSPERLQQVieDANVSQFtdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEA 613
Cdd:COG4525 90 wLNVLDNVAFGLRLRGVPKAERRARA--EELLALV------GLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190
....*....|....*....|....*....|..
gi 23397593 614 TSALDAVSENLVQNALDNLIQ--GRTVLTIAH 643
Cdd:COG4525 162 FGALDALTREQMQELLLDVWQrtGKGVFLITH 193
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
460-681 |
5.95e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.99 E-value: 5.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 460 SAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwlRNNIGAVSQEPVLFS-CSIR 538
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRhMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 539 ENILYGANpgETPSPERLQQVIEDANVSQFTDQLPdgLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALD 618
Cdd:PRK10851 93 DNIAFGLT--VLPRRERPNAAAIKAKVTQLLEMVQ--LAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 619 AVSENLVQNALDNL---IQGRTVLTIAHRLSTIRNADQIAVLSDGKIvEQgsynelMGIQEGVFRE 681
Cdd:PRK10851 169 AQVRKELRRWLRQLheeLKFTSVFVTHDQEEAMEVADRVVVMSQGNI-EQ------AGTPDQVWRE 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
451-667 |
6.16e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 88.37 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 451 FFTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGI-------DLRTVNPQW----- 518
Cdd:PRK13631 30 VFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdkknNHELITNPYskkik 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 519 ----LRNNIGAVSQEP--VLFSCSIRENILYGanpgetpsPERLQQVIEDAN--VSQFTDQLpdGLDTLVGQRG-MMLSG 589
Cdd:PRK13631 110 nfkeLRRRVSMVFQFPeyQLFKDTIEKDIMFG--------PVALGVKKSEAKklAKFYLNKM--GLDDSYLERSpFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 590 GQKQRVAIARALIKNPAILILDEATSALDAVSEN-LVQNALDNLIQGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGS 667
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGT 259
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
454-657 |
7.21e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.98 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 454 FPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwlrnnigaVSQEPVLF 533
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 534 SCSIRENILYGANPGETPSpERLQqvIED-ANVSQFTDQLpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDE 612
Cdd:NF040873 71 PLTVRDLVAMGRWARRGLW-RRLT--RDDrAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 23397593 613 ATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIRNADQIAVL 657
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
462-671 |
8.55e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.07 E-value: 8.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDP-----QGGTVHLDG---IDLRTVNPqwLRNNIGAVSQEPVLF 533
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGrsiFNYRDVLE--FRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 534 SCSIRENILYGANPGETpSPERLQQVIEDANVSQFTdqLPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEA 613
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKL-VPRKEFRGVAQARLTEVG--LWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 23397593 614 TSALDAVSENLVQNALDNLIQGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
435-666 |
1.15e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 90.30 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 435 VVPLEkPVGEVgfQNVFFTFPTRP--------ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHL 506
Cdd:PRK10261 307 VVDGE-PILQV--RNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 507 DGIDLRTVNP---QWLRNNIGAVSQEPV-------LFSCSIRENI-LYGANPGETpSPERLQQVIEDANVsqftdqLPDG 575
Cdd:PRK10261 384 NGQRIDTLSPgklQALRRDIQFIFQDPYasldprqTVGDSIMEPLrVHGLLPGKA-AAARVAWLLERVGL------LPEH 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 576 ldtlVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTI-RNAD 652
Cdd:PRK10261 457 ----AWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVeRISH 532
|
250
....*....|....
gi 23397593 653 QIAVLSDGKIVEQG 666
Cdd:PRK10261 533 RVAVMYLGQIVEIG 546
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
445-667 |
1.47e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.71 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 445 VGFQNVFFTF-PTRP-ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQW---- 518
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 519 LRNNIGAVSQEP--VLFSCSIRENILYGAN-------PGETPSPERLQQViedANVSQFTDQLPdgldtlvgqrgMMLSG 589
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQnfgipkeKAEKIAAEKLEMV---GLADEFWEKSP-----------FELSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 590 GQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGS 667
Cdd:PRK13643 148 GQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
459-662 |
1.70e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.88 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVnpqwlRNNIGAVSQEPVLFSC-SI 537
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPWkKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 538 RENILYGANPGETPSPER-LQQViedanvsqftdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSA 616
Cdd:PRK11247 99 IDNVGLGLKGQWRDAALQaLAAV---------------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 23397593 617 LDAVSENLVQNALDNLIQ--GRTVLTIAHRLS-TIRNADQIAVLSDGKI 662
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
462-671 |
1.99e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.99 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRL-------YdPQGgTVHLDGIDLRTVNPQWLR----NNIGAVSQEP 530
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvvY-PSG-DIRFHGESLLHASEQTLRgvrgNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 531 VLfSCSIRENI---------LYGANPGETPSPERLQqVIEDANVSQFTDQLPDgldtlvgqRGMMLSGGQKQRVAIARAL 601
Cdd:PRK15134 102 MV-SLNPLHTLekqlyevlsLHRGMRREAARGEILN-CLDRVGIRQAAKRLTD--------YPHQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
461-677 |
2.46e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.81 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 461 AVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTvNPQWLRNNIGAVSQEPVL-FSCSIRE 539
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLdLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 540 NIL-YGANPGEtpSPERLQQVIedANVSQFTdQLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDEATSALD 618
Cdd:PRK13536 134 NLLvFGRYFGM--STREIEAVI--PSLLEFA-RLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23397593 619 AVSENLVQNALDNLI-QGRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNELMGIQEG 677
Cdd:PRK13536 205 PHARHLIWERLRSLLaRGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEHIG 265
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
462-672 |
2.57e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.42 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVL-FSCSIREN 540
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 ILYGANPGEtPSPERLQQVIEDANVSQFTdqlPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAV 620
Cdd:PRK10253 102 VARGRYPHQ-PLFTRWRKEDEEAVTKAMQ---ATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 621 SENLVQNALDNL--IQGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNELM 672
Cdd:PRK10253 178 HQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
135-409 |
4.60e-18 |
|
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: 85.25 E-value: 4.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 135 AITMSVPLFLGKVIDVVFNKSGMDSaamakLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLRSRLYRSMLMQEV 214
Cdd:cd18555 16 LLTLLIPILTQYVIDNVIVPGNLNL-----LNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 215 GWFDTKGTGELINRLsNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAIVYGRYVRRIT 294
Cdd:cd18555 91 SFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 295 KVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTG---FCGNFIIisvLYYG 371
Cdd:cd18555 170 QEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSsiqFIAPLLI---LWIG 246
|
250 260 270
....*....|....*....|....*....|....*...
gi 23397593 372 GTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQL 409
Cdd:cd18555 247 AYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQF 284
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
448-663 |
5.73e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 88.24 E-value: 5.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRPES-AVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWL----RNN 522
Cdd:PRK10535 8 KDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 523 IGAVSQEPVLFS-CSIRENILYGANPGETPSPERLQQVIEdanvsqFTDQLpdGLDTLVGQRGMMLSGGQKQRVAIARAL 601
Cdd:PRK10535 88 FGFIFQRYHLLShLTAAQNVEVPAVYAGLERKQRLLRAQE------LLQRL--GLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIRNADQIAVLSDGKIV 663
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
444-671 |
6.84e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 84.69 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 444 EVGFQNVFFTF-PTRP-ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTI-----ALLMlrlydPQGGTVHL--DGIDLRTV 514
Cdd:PRK13634 2 DITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLlqhlnGLLQ-----PTSGTVTIgeRVITAGKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 515 NPQW--LRNNIGAVSQ--EPVLFSCSIRENILYG-ANPG--ETPSPERLQQVIEDAnvsqftdqlpdGLDTLVGQRG-MM 586
Cdd:PRK13634 77 NKKLkpLRKKVGIVFQfpEHQLFEETVEKDICFGpMNFGvsEEDAKQKAREMIELV-----------GLPEELLARSpFE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 587 LSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIV 663
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVF 225
|
....*...
gi 23397593 664 EQGSYNEL 671
Cdd:PRK13634 226 LQGTPREI 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
462-660 |
9.34e-18 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 82.87 E-value: 9.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIaLLML-RLYDPQGGTVHLD----GIDLRTVNP-QWL---RNNIGAVSQ---- 528
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTL-LKCIyGNYLPDSGSILVRhdggWVDLAQASPrEILalrRRTIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 529 -----------EPV----------------LFScsiRENIlyganpgetpsPERLqqviedANVSQFTdqlpdgldtlvg 581
Cdd:COG4778 105 iprvsaldvvaEPLlergvdreeararareLLA---RLNL-----------PERL------WDLPPAT------------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 582 qrgmmLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTI-RNADQIAVLSD 659
Cdd:COG4778 153 -----FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKaRGTAIIGIFHDEEVReAVADRVVDVTP 227
|
.
gi 23397593 660 G 660
Cdd:COG4778 228 F 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
459-677 |
1.17e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.47 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwLRNNIGAVSQ----EPvlfS 534
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGVVPQfdnlDP---D 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENIL-----YGANPGEtpSPERLQQVIEDAnvsqftdQLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILI 609
Cdd:PRK13537 95 FTVRENLLvfgryFGLSAAA--ARALVPPLLEFA-------KLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 610 LDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNELMGIQEG 677
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESEIG 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
447-676 |
1.39e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 83.73 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTF-PTRP-ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDG--IDLRTVNP--QWLR 520
Cdd:PRK13641 5 FENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETGNKnlKKLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 521 NNIGAVSQ--EPVLFSCSIRENILYGA-NPGETPSPERLQQViedanvsQFTDQLpdGLDT-LVGQRGMMLSGGQKQRVA 596
Cdd:PRK13641 85 KKVSLVFQfpEAQLFENTVLKDVEFGPkNFGFSEDEAKEKAL-------KWLKKV--GLSEdLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 597 IARALIKNPAILILDEATSALDAVS-ENLVQNALDNLIQGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELMGI 674
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSD 235
|
..
gi 23397593 675 QE 676
Cdd:PRK13641 236 KE 237
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
459-673 |
1.76e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.71 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNP-------------QWLRNNIGA 525
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknqlRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 526 VSQEPVLFS-CSIRENILYGANP--GETPSPERLQQVIEDANVsqftdqlpdGLDTLV-GQRGMMLSGGQKQRVAIARAL 601
Cdd:PRK10619 97 VFQHFNLWShMTVLENVMEAPIQvlGLSKQEARERAVKYLAKV---------GIDERAqGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELMG 673
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
457-672 |
2.21e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 82.95 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 457 RPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTiallMLRLY--------DPQG----GTVHLDGIDLRTVNPQWL--RNN 522
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKST----LLKALagdltgggAPRGarvtGDVTLNGEPLAAIDAPRLarLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 523 IGAVSQEPVlFSCSIRENILYGANPGETPSPErlqQVIEDANVSQFTDQLPDGlDTLVGQRGMMLSGGQKQRVAIARAL- 601
Cdd:PRK13547 87 VLPQAAQPA-FAFSAREIVLLGRYPHARRAGA---LTHRDGEIAWQALALAGA-TALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 602 --------IKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNE 670
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPAD 241
|
..
gi 23397593 671 LM 672
Cdd:PRK13547 242 VL 243
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
457-671 |
2.52e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.06 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 457 RPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDG----------IDLRTVNPQWLRNNIGA- 525
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHVRGAd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 526 ---VSQEPVlfsCSIRENILYGANPGETPspeRLQQVI--EDA--NVSQFTDQ--LPDGlDTLVGQRGMMLSGGQKQRVA 596
Cdd:PRK10261 106 mamIFQEPM---TSLNPVFTVGEQIAESI---RLHQGAsrEEAmvEAKRMLDQvrIPEA-QTILSRYPHQLSGGMRQRVM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 597 IARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGRT--VLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
131-419 |
2.57e-17 |
|
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: 83.24 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 131 VVSSAITMSVPLFLGKVID-VVFNKSGMDSAAMAKLGEYSVLLFGIF-VLGGFANFARVHLFGNAALRIVRSLRSRLYRS 208
Cdd:cd18554 9 LVRFGIPLLLPLILKYIVDdVIQGSSLTLDEKVYKLFTIIGIMFFIFlILRPPVEYYRQYFAQWIANKILYDIRKDLFDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 209 MLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAIVYGR 288
Cdd:cd18554 89 LQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 289 YVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIIISVL 368
Cdd:cd18554 169 RLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVI 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 23397593 369 YYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18554 249 GFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
460-662 |
2.98e-17 |
|
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: 80.17 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 460 SAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNP-QWLRNNIGAVSQEP----VLFS 534
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENILYGAnpgetpsperlqqviedanvsqftdqlpdgldtlvgqrgmMLSGGQKQRVAIARALIKNPAILILDEAT 614
Cdd:cd03215 93 LSVAENIALSS----------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 615 SALD--AVSE--NLVQNALDnliQGRTVLTIahrlST-----IRNADQIAVLSDGKI 662
Cdd:cd03215 133 RGVDvgAKAEiyRLIRELAD---AGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
465-685 |
3.86e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 81.67 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 465 DFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDP----QGGTVHLDGidlRTVNPQWLRNNIGAvsqepvlfscSIREN 540
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDG---KPVAPCALRGRKIA----------TIMQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 ILYGANPGETPSP---ERLQQVIEDANVSQFTDQLPD-GLD---TLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEA 613
Cdd:PRK10418 88 PRSAFNPLHTMHTharETCLALGKPADDATLTAALEAvGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 614 TSALDAVSENLVQNALDNLIQGRT--VLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNELMGI-QEGVFRELVAS 685
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNApKHAVTRSLVSA 243
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
462-666 |
4.04e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.43 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQG-----GTVHLDGIDLRT--VNPQWLRNNIGAVSQEPVLFS 534
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSpdVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 -CSIRENILYGAN-PGETPSPERLQQVIEDA-NVSQFTDQLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILD 611
Cdd:PRK14267 99 hLTIYDNVAIGVKlNGLVKSKKELDERVEWAlKKAALWDEVKDRLNDYPSN----LSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 612 EATSALDAVSENLVQNALDNLIQGRTVLTIAHR-LSTIRNADQIAVLSDGKIVEQG 666
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
462-673 |
6.53e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 6.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQW---LRNN-IGAVSQ-EPVLFSCS 536
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENI-----LYGANPGE--TPSPERLQQViedanvsqftdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILI 609
Cdd:PRK11629 104 ALENVampllIGKKKPAEinSRALEMLAAV---------------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 610 LDEATSALDAVSENLVQNALD--NLIQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQGSyneLMG 673
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGelNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS---LMG 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
445-659 |
7.56e-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: 78.35 E-value: 7.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 445 VGFQNVffTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLdgidlrtvnPQwlRNNIG 524
Cdd:cd03223 1 IELENL--SLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PE--GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 525 AVSQEPVLFSCSIRENILYganpgetPSperlqqviedanvsqftdqlpdgldtlvgqrGMMLSGGQKQRVAIARALIKN 604
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-------PW-------------------------------DDVLSGGEQQRLAFARLLLHK 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 605 PAILILDEATSALDAVSENLVQNALDNLiqGRTVLTIAHRLSTIRNADQIAVLSD 659
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLLKEL--GITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
443-676 |
9.08e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.21 E-value: 9.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 443 GEVGFQNVFFTFPTRP--ESAVLTDFSLNLMPGTTTAVVGRSGSGKTT-IALLMLRLYDPQGGTVHLD---GIDLRTVNP 516
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTmIQLTNGLIISETGQTIVGDyaiPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 517 -QWLRNNIGAVSQEP--VLFSCSIRENILYG-ANPGETPS------PERLQQViedanvsqftdQLPDgldTLVGQRGMM 586
Cdd:PRK13645 85 vKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpVNLGENKQeaykkvPELLKLV-----------QLPE---DYVKRSPFE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 587 LSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNL--IQGRTVLTIAHRLSTI-RNADQIAVLSDGKIV 663
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVI 230
|
250
....*....|...
gi 23397593 664 EQGSYNELMGIQE 676
Cdd:PRK13645 231 SIGSPFEIFSNQE 243
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
462-663 |
1.27e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.14 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNP-QWLRNNIGAVS----QEPVLFSCS 536
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPedrkGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENILYgANPGETPSPERLQQVIEDANVSQFTDQL---PDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDEA 613
Cdd:COG1129 347 IRENITL-ASLDRLSRGGLLDRRRERALAEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 614 TSALD--AVSEnlVQNALDNLI-QGRTVLTIahrlST-----IRNADQIAVLSDGKIV 663
Cdd:COG1129 422 TRGIDvgAKAE--IYRLIRELAaEGKAVIVI----SSelpelLGLSDRILVMREGRIV 473
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
462-676 |
2.23e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.36 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDG-----IDLRT-VNPQwL--RNNIgavsqepvLF 533
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvsalLELGAgFHPE-LtgRENI--------YL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 534 SCSIrenilYGANPGETpsPERLQQVIEDANVSQFtdqlpdgLDTLVGqrgmMLSGGQKQRVAIARALIKNPAILILDEA 613
Cdd:COG1134 112 NGRL-----LGLSRKEI--DEKFDEIVEFAELGDF-------IDQPVK----TYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 614 TSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGS-------YNELMGIQE 676
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELReSGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDpeeviaaYEALLAGRE 245
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
459-667 |
2.89e-16 |
|
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: 77.57 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRL--YDPQGGTVHLDGIDLRTVNPQ-WLRNNIGAVSQEPVLFsc 535
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEeRARLGIFLAFQYPPEI-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 536 sirenilyganPGETpsperLQQVIEDANVSqftdqlpdgldtlvgqrgmmLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:cd03217 90 -----------PGVK-----NADFLRYVNEG--------------------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 616 ALDAVSENLVQNALDNLI-QGRTVLTIAH--RLSTIRNADQIAVLSDGKIVEQGS 667
Cdd:cd03217 134 GLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD 188
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
465-666 |
3.10e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.20 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 465 DFSLNLMPGTTTAVVGRSGSGKTTI-ALLMLRLyDPQGGTVHLDGIDLRTVNPQWL---------RNNIGAVSQEPvlfS 534
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLlNALSARL-APDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHP---R 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENILYGANPGEtpspeRLQQV-------IEDAnVSQFTDQL---PDGLDTLVGQrgmmLSGGQKQRVAIARALIKN 604
Cdd:PRK11701 100 DGLRMQVSAGGNIGE-----RLMAVgarhygdIRAT-AGDWLERVeidAARIDDLPTT----FSGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23397593 605 PAILILDEATSALDaVSenlVQNALDNLIQGRT------VLTIAHRLSTIRN-ADQIAVLSDGKIVEQG 666
Cdd:PRK11701 170 PRLVFMDEPTGGLD-VS---VQARLLDLLRGLVrelglaVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
462-671 |
3.23e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.53 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLrTVNPQWLR--NNIGAVSQEPVLF-SCSIR 538
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLPMHKRarLGIGYLPQEASIFrKLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 539 ENIL-----YGANPGEtpSPERLQQVIEDanvsqFtdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEA 613
Cdd:COG1137 97 DNILavlelRKLSKKE--REERLEELLEE-----F------GITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397593 614 TSALD--AVSEnlVQNALDNLIQ-GRTVLTIAH--RlSTIRNADQIAVLSDGKIVEQGSYNEL 671
Cdd:COG1137 164 FAGVDpiAVAD--IQKIIRHLKErGIGVLITDHnvR-ETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
462-666 |
3.37e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.74 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTI-----ALLMlrlydPQGGTVHL----DGIDLRTVNPQW-------------- 518
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFiehlnALLL-----PDTGTIEWifkdEKNKKKTKEKEKvleklviqktrfkk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 519 ------LRNNIGAVSQ--EPVLFSCSIRENILYGANPGETPSPE---RLQQVIEDAnvsqftdqlpdGLDTLVGQRG-MM 586
Cdd:PRK13651 97 ikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEakkRAAKYIELV-----------GLDESYLQRSpFE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 587 LSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNL-IQGRTVLTIAHRL-STIRNADQIAVLSDGKIVE 664
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIK 245
|
..
gi 23397593 665 QG 666
Cdd:PRK13651 246 DG 247
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
463-689 |
4.20e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.44 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYdPQGGTVHLDGIDLRTVNPQ-------WLRNNIGAVSQEPVLFSC 535
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAelarhraYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 536 SireniLYGANPGETpspERLQQVIEDanVSQFTdQLPDGLDTLVGQrgmmLSGGQKQRVAIARALIK-----NPA--IL 608
Cdd:PRK03695 91 T-----LHQPDKTRT---EAVASALNE--VAEAL-GLDDKLGRSVNQ----LSGGEWQRVRLAAVVLQvwpdiNPAgqLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 609 ILDEATSALDaVSEnlvQNALDNLI-----QGRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNELMgiqegvfREL 682
Cdd:PRK03695 156 LLDEPMNSLD-VAQ---QAALDRLLselcqQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL-------TPE 224
|
....*..
gi 23397593 683 VASQAFG 689
Cdd:PRK03695 225 NLAQVFG 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
467-689 |
4.25e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.06 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 467 SLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPV-----------LFSC 535
Cdd:PRK15112 33 SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisqILDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 536 SIRENIlyganpgETPSPERLQQVIEdanVSQFTDQLPDGldtlVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:PRK15112 113 PLRLNT-------DLEPEQREKQIIE---TLRQVGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 616 ALDAVSENLVQNALDNL--IQGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNE-LMGIQEGVFRELVASQaFG 689
Cdd:PRK15112 179 SLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADvLASPLHELTKRLIAGH-FG 255
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
462-666 |
7.05e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.80 E-value: 7.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIA-LLMLR-LYDPQGGTVHLDGIDL-------RTvnpqwlRNNIGAVSQEPVL 532
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAkVLMGHpKYEVTSGSILLDGEDIlelspdeRA------RAGIFLAFQYPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 533 FS-CSIRE--NILYGANPGETPSPERLQQVIEDAnvsqfTDQLpdGLDTLVGQRGMM--LSGGQKQRVAIARALIKNPAI 607
Cdd:COG0396 89 IPgVSVSNflRTALNARRGEELSAREFLKLLKEK-----MKEL--GLDEDFLDRYVNegFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 608 LILDEATSALD-----AVSENLvqNALDNliQGRTVLTIAH--RLSTIRNADQIAVLSDGKIVEQG 666
Cdd:COG0396 162 AILDETDSGLDidalrIVAEGV--NKLRS--PDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
461-665 |
1.29e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 76.74 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 461 AVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQW---LR-NNIGAVSQEPVLF-SC 535
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRaKHVGFVFQSFMLIpTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 536 SIRENI-----LYGANpgETPSPERLQQVIEDANVSQFTDQLPdgldtlvgqrgMMLSGGQKQRVAIARALIKNPAILIL 610
Cdd:PRK10584 104 NALENVelpalLRGES--SRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 611 DEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRNADQIAVLSDGKIVEQ 665
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
448-672 |
1.75e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRpesAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVS 527
Cdd:PRK10575 15 RNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 528 QE-PVLFSCSIRENILYGANPGE-------TPSPERLQQVIEDANVSQFTDQLPDGLdtlvgqrgmmlSGGQKQRVAIAR 599
Cdd:PRK10575 92 QQlPAAEGMTVRELVAIGRYPWHgalgrfgAADREKVEEAISLVGLKPLAHRLVDSL-----------SGGERQRAWIAM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 600 ALIKNPAILILDEATSALDAVSENLVQNALDNLIQGR--TVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNELM 672
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
462-666 |
1.97e-15 |
|
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: 76.03 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGidlrtvNPQWLrnnIG-AVSQEPVLfscSIREN 540
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSL---LGlGGGFNPEL---TGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 I-----LYGAnpgetpSPERLQQVIEDanVSQFTDqLPDGLDTLVGqrgmMLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:cd03220 105 IylngrLLGL------SRKEIDEKIDE--IIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 23397593 616 ALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQG 666
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLkQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
170-419 |
2.40e-15 |
|
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: 77.22 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 170 VLLFGIFVLGGF---ANFARVHLFGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLS-NDTL---MVGTSLsQ 242
Cdd:cd18568 43 LILIGLLIVGIFqilLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQeNQKIrrfLTRSAL-T 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 243 NVSDGLrsvaMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFC 322
Cdd:cd18568 122 TILDLL----MVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 323 REQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGL 402
Cdd:cd18568 198 AERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLAL 277
|
250
....*....|....*..
gi 23397593 403 SNFYSQLNKGIGASERI 419
Cdd:cd18568 278 VGLWDELQETRISVERL 294
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
447-660 |
4.36e-15 |
|
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: 74.20 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPES-AVLTDFSLNLMPGTTTAVVGRSGSGKTTIaLLMLRLYDPQG---GTVHLDGIDLrtvnPQWLRNN 522
Cdd:cd03232 6 WKNLNYTVPVKGGKrQLLNNISGYVKPGTLTALMGESGAGKTTL-LDVLAGRKTAGvitGEILINGRPL----DKNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 523 IGAVSQEPVLFSCS-IRENILYGANpgetpsperlqqviedanvsqftdqlpdgldtlvgQRGmmLSGGQKQRVAIARAL 601
Cdd:cd03232 81 TGYVEQQDVHSPNLtVREALRFSAL-----------------------------------LRG--LSVEQRKRLTIGVEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLS--TIRNADQIAVLSDG 660
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQAAYNIVRFLKKLAdSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
467-673 |
4.97e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 78.31 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 467 SLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVH-------LDGIDLRTVNPQWLRNNIGAVSQEPVLFS-CSIR 538
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQEYDLYPhRTVL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 539 ENiLYGANPGETPSP-ERLQQVI-------EDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIARALIKNPAILIL 610
Cdd:TIGR03269 384 DN-LTEAIGLELPDElARMKAVItlkmvgfDEEKAEEILDKYPD-----------ELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 611 DEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELMG 673
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
462-672 |
5.77e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.93 E-value: 5.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLrTVNP--QWLRNNIGAVSQEPVLFS-CSIR 538
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI-SLLPlhARARRGIGYLPQEASIFRrLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 539 ENILYGANPGETPSPE----RLQQVIEDANVSQFTDQLpdgldtlvgqrGMMLSGGQKQRVAIARALIKNPAILILDEAT 614
Cdd:PRK10895 97 DNLMAVLQIRDDLSAEqredRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 615 SALDAVSENLVQNALDNLI-QGRTVLTIAHRL-STIRNADQIAVLSDGKIVEQGSYNELM 672
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
447-661 |
6.30e-15 |
|
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: 72.10 E-value: 6.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGidlrtvnpqwlRNNIGAV 526
Cdd:cd03221 3 LENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQepvlfscsirenilyganpgetpsperlqqviedanvsqftdqlpdgldtlvgqrgmmLSGGQKQRVAIARALIKNPA 606
Cdd:cd03221 69 EQ----------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 607 ILILDEATSALDAVSENLVQNALDNLiQGrTVLTIAHRLSTIRN-ADQIAVLSDGK 661
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEY-PG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
456-636 |
1.36e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.98 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 456 TRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIG---AVsqEPVL 532
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGhrnAM--KPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 533 fscSIRENILYGA---NPGETPSPERLQQViedanvsqftdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILI 609
Cdd:PRK13539 89 ---TVAENLEFWAaflGGEELDIAAALEAV---------------GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180
....*....|....*....|....*..
gi 23397593 610 LDEATSALDAVSENLVQnaldNLIQGR 636
Cdd:PRK13539 151 LDEPTAALDAAAVALFA----ELIRAH 173
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
463-666 |
1.64e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQW-LRNNIGAVSQE-PVLFSCSIREN 540
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 541 ILYGANPGETPSPERL---QQVIEDANVSQFTDQLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDEATSAL 617
Cdd:PRK09700 101 LYIGRHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 23397593 618 -DAVSENL--VQNALDNliQGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQG 666
Cdd:PRK09700 177 tNKEVDYLflIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
476-667 |
1.69e-14 |
|
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: 77.75 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 476 TAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTvNPQWLRNNIGAVSQEPVLFS-CSIRENILYGAN-PGETPSP 553
Cdd:TIGR01257 959 TAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILFYAQlKGRSWEE 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 554 ERLQQ--VIEDAnvsqftdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDN 631
Cdd:TIGR01257 1038 AQLEMeaMLEDT-----------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK 1106
|
170 180 190
....*....|....*....|....*....|....*..
gi 23397593 632 LIQGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGS 667
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
477-671 |
1.98e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.07 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 477 AVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEP--VLFSCSIRENILYG-ANPG--ETP 551
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQDIAFGpINLGldEET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 552 SPERLQQVIEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDN 631
Cdd:PRK13652 114 VAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLND 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 23397593 632 LIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK13652 183 LPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
457-645 |
2.12e-14 |
|
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: 72.39 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 457 RPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCS 536
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENILYGANPGETpsperlqqviEDANVSQFTDQ--LPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDEAT 614
Cdd:TIGR01189 90 ALENLHFWAAIHGG----------AQRTIEDALAAvgLTGFEDLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|...
gi 23397593 615 SALDAVSENLVQNALDNLIQ--GRTVLTIAHRL 645
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLArgGIVLLTTHQDL 188
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
468-667 |
2.88e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.51 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 468 LNLMPGTTTAVVGRSGSGKTTIALLMLRL----------YDPQGGTVHLDGIDLRTVNPQwlRNNIGAVSQEPVLFS-CS 536
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGRLARDIRKS--RANTGYIFQQFNLVNrLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENILYGAnPGETP---------SPERLQQVIEDANVSqftdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAI 607
Cdd:PRK09984 103 VLENVLIGA-LGSTPfwrtcfswfTREQKQRALQALTRV--------GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397593 608 LILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGS 667
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
465-671 |
3.10e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 74.68 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 465 DFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwlRNNIGAVSQEPVLFS-CSIRENILY 543
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMVFQSYALYPhLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 544 GANPGETPSPERLQQVIEDANVSQftdqlpdgLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSEN 623
Cdd:PRK11000 99 GLKLAGAKKEEINQRVNQVAEVLQ--------LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 23397593 624 LVQNALDNLIQ--GRTVLTIAH-RLSTIRNADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK11000 171 QMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
439-666 |
3.61e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 72.37 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 439 EKPVGEVGFQNVFFTfPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQW 518
Cdd:cd03267 14 SKEPGLIGSLKSLFK-RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 519 LRNnIGAV-SQE-------PVLFSCSIRENIlYGANPGETpsperlqqvieDANVSQFTD--QLPDGLDTLVGQrgmmLS 588
Cdd:cd03267 93 LRR-IGVVfGQKtqlwwdlPVIDSFYLLAAI-YDLPPARF-----------KKRLDELSEllDLEELLDTPVRQ----LS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 589 GGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQGR--TVLTIAHRLSTI-RNADQIAVLSDGKIVEQ 665
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRLLYD 235
|
.
gi 23397593 666 G 666
Cdd:cd03267 236 G 236
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
459-676 |
5.87e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.73 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDG--IDLRTVNPQWLRNNIGAVSQEP--VLFS 534
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENILYGAnpgetpspeRLQQVIEDANVSQFTDQLpdgldTLVGQRGMM------LSGGQKQRVAIARALIKNPAIL 608
Cdd:PRK13638 93 TDIDSDIAFSL---------RNLGVPEAEITRRVDEAL-----TLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 609 ILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELMGIQE 676
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
457-643 |
6.45e-14 |
|
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: 70.98 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 457 RPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVSQEPVLFSCS 536
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENILYGANPGETpspERLQQVIEDANVSQFTDqLPdgldtlVGQrgmmLSGGQKQRVAIARALIKNPAILILDEATSA 616
Cdd:cd03231 90 VLENLRFWHADHSD---EQVEEALARVGLNGFED-RP------VAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*...
gi 23397593 617 LDAVSENLVQNAL-DNLIQGRTVLTIAH 643
Cdd:cd03231 156 LDKAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
467-686 |
1.06e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 73.90 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 467 SLNLMPGTTTAVVGRSGSGKTTIALLM---LRLYDPQ-----GGTVHLDGIDL-RTVNPQWLRNNIGAVSQEPVLFSCSI 537
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALageLPLLSGErqsqfSHITRLSFEQLqKLVSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 538 RENILyganpGETPSPERLQQVIEdanvsQFtdqlpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSAL 617
Cdd:PRK10938 103 AEIIQ-----DEVKDPARCEQLAQ-----QF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23397593 618 DAVSENLVQNALDNLI-QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELMgiQEGVFRELVASQ 686
Cdd:PRK10938 167 DVASRQQLAELLASLHqSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEIL--QQALVAQLAHSE 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
463-661 |
1.09e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYdPQG---GTVHLDGIDLRTVN-PQWLRNNIGAVSQEPVLFS-CSI 537
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNiRDTERAGIAIIHQELALVKeLSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 538 RENILYGANPgeTPSperlqQVIEDANVSQFTDQLPD--GLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:PRK13549 100 LENIFLGNEI--TPG-----GIMDYDAMYLRAQKLLAqlKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 23397593 616 ALDAvSENLVqnaLDNLI-----QGRTVLTIAHRLSTIRN-ADQIAVLSDGK 661
Cdd:PRK13549 173 SLTE-SETAV---LLDIIrdlkaHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
463-664 |
1.66e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.29 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTialLMLRL---YdPQG---GTVHLDGidlrtvNPQWLRN-------NIGAVSQE 529
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKST---LMKVLsgvY-PHGsyeGEILFDG------EVCRFKDirdsealGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 530 ----PVLfscSIRENILYGaNpgetpspERLQQ-VIEDANVSQFTDQLPD--GL----DTLVGQRGMmlsgGQKQRVAIA 598
Cdd:NF040905 87 laliPYL---SIAENIFLG-N-------ERAKRgVIDWNETNRRARELLAkvGLdespDTLVTDIGV----GKQQLVEIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397593 599 RALIKNPAILILDEATSAL-DAVSENLVqnaldNLI-----QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVE 664
Cdd:NF040905 152 KALSKDVKLLILDEPTAALnEEDSAALL-----DLLlelkaQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
458-643 |
1.97e-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: 73.43 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 458 PESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLrlydpqggtvhldGIDLRTVNPQWLRNNI--GAVSQEPVL-FS 534
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVDKDFNGEARPQPGIkvGYLPQEPQLdPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENILYG---------------ANPGEtPSPE---------RLQQVIE-------DANVSQFTDQL--PDGlDTLVG 581
Cdd:TIGR03719 83 KTVRENVEEGvaeikdaldrfneisAKYAE-PDADfdklaaeqaELQEIIDaadawdlDSQLEIAMDALrcPPW-DADVT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 582 QrgmmLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLiQGrTVLTIAH 643
Cdd:TIGR03719 161 K----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
463-663 |
2.17e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.90 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGID---LRTVNPQWLRNNIGAVSQEP-VLFSCSIR 538
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 539 EN-----ILYGAnpgetpSPERLQQviedaNVSQFTDQLpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEA 613
Cdd:PRK10908 98 DNvaiplIIAGA------SGDDIRR-----RVSAALDKV--GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 23397593 614 TSALD-AVSENLVQNALDNLIQGRTVLTIAHRLSTI-RNADQIAVLSDGKIV 663
Cdd:PRK10908 165 TGNLDdALSEGILRLFEEFNRVGVTVLMATHDIGLIsRRSYRMLTLSDGHLH 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
447-664 |
2.32e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPtrpesAV--LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNpqwLRNNIG 524
Cdd:PRK11288 7 FDGIGKTFP-----GVkaLDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAS---TTAALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 525 A----VSQE----PVLfscSIRENILYGAnpgetpSPERLQQVIEDANVSQFTDQLPD-GLDTLVGQRGMMLSGGQKQRV 595
Cdd:PRK11288 79 AgvaiIYQElhlvPEM---TVAENLYLGQ------LPHKGGIVNRRLLNYEAREQLEHlGVDIDPDTPLKYLSIGQRQMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397593 596 AIARALIKNPAILILDEATSALDA-VSENL--VQNALDNliQGRTVLTIAHRLSTI-RNADQIAVLSDGKIVE 664
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSArEIEQLfrVIRELRA--EGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
459-678 |
3.39e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.99 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTiallmlrLYDPQGGTVHLDG------IDLRTVNPQWLRNnIGAVSQEPVL 532
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKST-------LLNALAGRIQGNNftgtilANNRKPTKQILKR-TGFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 533 FS-CSIRENILYGAN---PGETPSPERLQqvIEDANVSQFTdqLPDGLDTLVGQ---RGmmLSGGQKQRVAIARALIKNP 605
Cdd:PLN03211 152 YPhLTVRETLVFCSLlrlPKSLTKQEKIL--VAESVISELG--LTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 606 AILILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLST--IRNADQIAVLSDGKIVEQGSYNELMGIQEGV 678
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQkGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMAYFESV 301
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
123-421 |
3.73e-13 |
|
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: 70.61 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 123 LTAGIGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSAAMakLGEYSVLLFGIFVlggFANFARVHLFGNAALRIVRSLR 202
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYY--LGVYAALLVLASV---LLVLLRWLLFVLAGLRASRRLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 203 SRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGM 282
Cdd:cd18580 76 DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 283 AIVYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEAlqigykeTRARAIFFGLT------ 356
Cdd:cd18580 156 QRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDAS-------QRAFYLLLAVQrwlglr 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 357 -GFCGNFIIISVlyyGGTLVLQDSLTIGALTAF-MLYAGYVAISMNGLSNFYSQLNKGIGASERIWE 421
Cdd:cd18580 229 lDLLGALLALVV---ALLAVLLRSSISAGLVGLaLTYALSLTGSLQWLVRQWTELETSMVSVERILE 292
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
425-663 |
8.19e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.21 E-value: 8.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 425 RECSIPIDKGVVPLEKPVGEVgfQNVffTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTV 504
Cdd:COG3845 240 REVLLRVEKAPAEPGEVVLEV--ENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSI 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 505 HLDGIDLRTVNP-QWLRNNIGAVSQEP-----VLfSCSIRENILYGA--NPGETPSP--------ERLQQVIEDANVSqf 568
Cdd:COG3845 316 RLDGEDITGLSPrERRRLGVAYIPEDRlgrglVP-DMSVAENLILGRyrRPPFSRGGfldrkairAFAEELIEEFDVR-- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 569 tdqlPDGLDTLVGqrgmMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLST 647
Cdd:COG3845 393 ----TPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDE 464
|
250
....*....|....*..
gi 23397593 648 IRN-ADQIAVLSDGKIV 663
Cdd:COG3845 465 ILAlSDRIAVMYEGRIV 481
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
462-653 |
2.05e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.04 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTiaLLMLRLYD-PQGGTVHLDGIDLR-----TVnpqW-LRNNIGAVSQEPVL-- 532
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKST--LLSLITGDhPQGYSNDLTLFGRRrgsgeTI---WdIKKHIGYVSSSLHLdy 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 533 -FSCSIRENIL---------YGAnpgetpSPERLQQViedanVSQFTDQLpdGLDTLVGQRGMM-LSGGQKQRVAIARAL 601
Cdd:PRK10938 350 rVSTSVRNVILsgffdsigiYQA------VSDRQQKL-----AQQWLDIL--GIDKRTADAPFHsLSWGQQRLALIVRAL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 602 IKNPAILILDEATSALDAVSENLVQNALDNLI-QGRTVL------------TIAHRLSTIRNADQ 653
Cdd:PRK10938 417 VKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETQLlfvshhaedapaCITHRLEFVPDGDI 481
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
463-663 |
4.49e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.08 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYdPQG---GTVHLDGIDLRTVN-PQWLRNNIGAVSQEPVLF-SCSI 537
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNiRDTERAGIVIIHQELTLVpELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 538 RENILYGA----NPGETPSPE---RLQQVIEDANVSQFTDQLPdgldtlVGQRGmmlsGGQKQRVAIARALIKNPAILIL 610
Cdd:TIGR02633 96 AENIFLGNeitlPGGRMAYNAmylRAKNLLRELQLDADNVTRP------VGDYG----GGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 611 DEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLSTIRN-ADQIAVLSDGKIV 663
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
472-649 |
7.53e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 63.55 E-value: 7.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 472 PGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVH-LDGIDLRTVNPQWLRNnigavsqepvlfscsirenilyganpget 550
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 551 psperlqqviedanvsqftdqlpdgldTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALD 630
Cdd:smart00382 52 ---------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104
|
170 180
....*....|....*....|....*.
gi 23397593 631 NLI-------QGRTVLTIAHRLSTIR 649
Cdd:smart00382 105 LRLllllkseKNLTVILTTNDEKDLG 130
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
463-682 |
8.22e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.89 E-value: 8.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTT-----AVVGRSGSGKTTIALLMLRLYDPQGGTVhldGIDLRTVN--PQWLRNNigavsqepvlFSC 535
Cdd:cd03237 10 LGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSykPQYIKAD----------YEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 536 SIREnILYGANPGETPSPERLQQVIEdanvsqftdqlPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:cd03237 77 TVRD-LLSSITKDFYTHPYFKTEIAK-----------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 616 ALDAVSENLVQNALDNLIQG--RTVLTIAHRLSTIRN-ADQIAVLsDGKIVEQGSYNELMGIQEGVFREL 682
Cdd:cd03237 145 YLDVEQRLMASKVIRRFAENneKTAFVVEHDIIMIDYlADRLIVF-EGEPSVNGVANPPQSLRSGMNRFL 213
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
457-619 |
8.52e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.83 E-value: 8.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 457 RPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTiallMLR----LYDPQGGTVHLDGIDLRTVNPQWLRN--NIG---AVs 527
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTS----LLRilagLARPDAGEVLWQGEPIRRQRDEYHQDllYLGhqpGI- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 528 qEPVLfscSIRENILYGANPGETPSPERLQQVIEDANVSQFTDqLPdgldtlVGQrgmmLSGGQKQRVAIARALIKNPAI 607
Cdd:PRK13538 86 -KTEL---TALENLRFYQRLHGPGDDEALWEALAQVGLAGFED-VP------VRQ----LSAGQQRRVALARLWLTRAPL 150
|
170
....*....|..
gi 23397593 608 LILDEATSALDA 619
Cdd:PRK13538 151 WILDEPFTAIDK 162
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
462-643 |
8.59e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.22 E-value: 8.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDP-QGGTVHLDGIdlrtvnpqwlrnNIGAVSQEPVL-FSCSIRE 539
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEfEGEARPAPGI------------KVGYLPQEPQLdPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 540 NILYGAnpGET----------------PSPE---------RLQQVIE-------DANVSQFTD--QLPDGlDTLVGQrgm 585
Cdd:PRK11819 90 NVEEGV--AEVkaaldrfneiyaayaePDADfdalaaeqgELQEIIDaadawdlDSQLEIAMDalRCPPW-DAKVTK--- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 586 mLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLiQGrTVLTIAH 643
Cdd:PRK11819 164 -LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY-PG-TVVAVTH 218
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
136-419 |
1.35e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 66.07 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 136 ITMSVPLFLGKVIDVVFNKSGMDSAAMAKLGeysvlLFGIFVLGGFANFARVHLFGNAALRIVRSLRSRLYRSMLMQEVG 215
Cdd:cd18566 17 LALATPLFILQVYDRVIPNESIPTLQVLVIG-----VVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 216 WFDTKGTGELINRLsNDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAIVYGRYVRRITK 295
Cdd:cd18566 92 FFEREPSGAHLERL-NSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 296 VELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIIISVLYYGGTLV 375
Cdd:cd18566 171 ERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 23397593 376 LQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18566 251 INGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
463-671 |
3.08e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRN-NIGAVSQE----PVLfscSI 537
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEaGIGIIHQElnliPQL---TI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 538 RENILYGANPGETPSPERLQQVIEDANVSQFTDQLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDEATSAL 617
Cdd:PRK10762 97 AENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 618 -DAVSENL--VQNALDNliQGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK10762 173 tDTETESLfrVIRELKS--QGRGIVYISHRLKEIFEiCDDVTVFRDGQFIAEREVADL 228
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
127-391 |
3.09e-11 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 64.83 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 127 IGCLVVSSAITMSVPLFLGKVIDVVFNKSGMDSAAMAKLgeysVLLFGIF-VLGGFANFARVHLFGNAALRIVRSLRSRL 205
Cdd:cd18582 2 LLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLL----LLAYGLArILSSLFNELRDALFARVSQRAVRRLALRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 206 YRSMLMQEVGWFDTKGTGEL---INRLSNDTLMVGTSLSQNVsdgLRSVAMIGVGTGMMIYT-SPQLAAVsalvvpaMAG 281
Cdd:cd18582 78 FRHLHSLSLRFHLSRKTGALsraIERGTRGIEFLLRFLLFNI---LPTILELLLVCGILWYLyGWSYALI-------TLV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 282 MAIVYGRYVRRITKVELdKYAEIMKFAEERFG--------NVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAiff 353
Cdd:cd18582 148 TVALYVAFTIKVTEWRT-KFRREMNEADNEANakavdsllNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLA--- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 23397593 354 gLTGFCGNFII----ISVLYYGGTLVLQDSLTIGALTAFMLY 391
Cdd:cd18582 224 -LLNIGQALIIslglTAIMLLAAQGVVAGTLTVGDFVLVNTY 264
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
587-683 |
6.29e-11 |
|
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: 65.21 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 587 LSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIV 663
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDlSDKAIWLENGEIK 248
|
90 100
....*....|....*....|
gi 23397593 664 EQGSYNELMgiqeGVFRELV 683
Cdd:TIGR03269 249 EEGTPDEVV----AVFMEGV 264
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
428-646 |
6.59e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 66.02 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 428 SIPIDKGVVPLEKPVGeVGFQNV--FFTFPTRPESAVLTDFSLNLM--------PGTTTAVVGRSGSGKTTialLMLRLY 497
Cdd:PLN03140 852 GVAPKRGMVLPFTPLA-MSFDDVnyFVDMPAEMKEQGVTEDRLQLLrevtgafrPGVLTALMGVSGAGKTT---LMDVLA 927
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 498 DPQGGTvHLDGiDLRTV---NPQWLRNNIGAVSQEPVLFS--CSIRENILYGAN---PGETPSPERLQQVIEDANVSQFt 569
Cdd:PLN03140 928 GRKTGG-YIEG-DIRISgfpKKQETFARISGYCEQNDIHSpqVTVRESLIYSAFlrlPKEVSKEEKMMFVDEVMELVEL- 1004
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 570 DQLPDGLDTLVGQRGmmLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLS 646
Cdd:PLN03140 1005 DNLKDAIVGLPGVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPS 1080
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
447-664 |
7.28e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.38 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 447 FQNVFFTFPTrpESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAV 526
Cdd:PRK10522 325 LRNVTFAYQD--NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEPVLFscsirENILYGAnpGETPSPERLQQVIEdanvsqfTDQLPDGLdTLVGQR--GMMLSGGQKQRVAIARALIKN 604
Cdd:PRK10522 403 FTDFHLF-----DQLLGPE--GKPANPALVEKWLE-------RLKMAHKL-ELEDGRisNLKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 605 PAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRNADQIAVLSDGKIVE 664
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
449-673 |
9.88e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.52 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 449 NVFFTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTT----IALLMLRLYDPQGGTVHLDGIDLRTVNPQwLRNNIG 524
Cdd:TIGR00956 63 RKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKH-YRGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 525 AVSQEPVLF-SCSIRENILYGANPgETPSpERLQQVIEDANVSQFTD------QLPDGLDTLVGQ---RGmmLSGGQKQR 594
Cdd:TIGR00956 142 YNAETDVHFpHLTVGETLDFAARC-KTPQ-NRPDGVSREEYAKHIADvymatyGLSHTRNTKVGNdfvRG--VSGGERKR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 595 VAIARALIKNPAILILDEATSALDAVSENLVQNALdnliqgRTVLTIAHRLSTI------RNA----DQIAVLSDGKIVE 664
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRAL------KTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIY 291
|
250
....*....|....*
gi 23397593 665 QGS------YNELMG 673
Cdd:TIGR00956 292 FGPadkakqYFEKMG 306
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
438-648 |
1.37e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 438 LEKPVGEVGF--QNVFFTFPTRPESAVLTD-FSLNLMPGTTTAVVGRSGSGKTTialLMLRLYDPQGGTVHLDGIdlRTV 514
Cdd:TIGR00956 751 MEKESGEDIFhwRNLTYEVKIKKEKRVILNnVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGD--RLV 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 515 NPQWLRNN----IGAVSQEPV-LFSCSIRENILYGA---NPGETPSPERLQQVIEDANVSQFTDQlpdgLDTLVGQRGMM 586
Cdd:TIGR00956 826 NGRPLDSSfqrsIGYVQQQDLhLPTSTVRESLRFSAylrQPKSVSKSEKMEYVEEVIKLLEMESY----ADAVVGVPGEG 901
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 587 LSGGQKQRVAIARALIKNPAILI-LDEATSALDAVSE----NLVQNALDNliqGRTVLTIAHRLSTI 648
Cdd:TIGR00956 902 LNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAwsicKLMRKLADH---GQAILCTIHQPSAI 965
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
465-618 |
1.90e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 465 DFSLNLMPGTTTAVVGRSGSGKTTialLMLRLYDP---QGGTVHLDGIDLRTVNPQ-WLRNNIGAVSQEP----VLFSCS 536
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTE---LMKVLYGAlprTSGYVTLDGHEVVTRSPQdGLANGIVYISEDRkrdgLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENILYGANPGETPSPERLQQVIEDANVSQFTD----QLPdGLDTLVGqrgmMLSGGQKQRVAIARALIKNPAILILDE 612
Cdd:PRK10762 347 VKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRlfniKTP-SMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDE 421
|
....*.
gi 23397593 613 ATSALD 618
Cdd:PRK10762 422 PTRGVD 427
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
437-662 |
1.92e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.11 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 437 PLEKPVGEV-GFQNVFFTFPTRPESAVLTDFSLNLmpGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTV----------- 504
Cdd:PLN03073 500 PDDRPGPPIiSFSDASFGYPGGPLLFKNLNFGIDL--DSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavf 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 505 ---HLDGIDLrTVNPqwlrnnigavsqepvlfscsirenILYGAN--PGetpSPE-RLQQVIEDANVSqftdqlpdglDT 578
Cdd:PLN03073 578 sqhHVDGLDL-SSNP------------------------LLYMMRcfPG---VPEqKLRAHLGSFGVT----------GN 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 579 LVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSA--LDAVsENLVQNALdnLIQGrTVLTIAHRLSTIRNA-DQIA 655
Cdd:PLN03073 620 LALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHldLDAV-EALIQGLV--LFQG-GVLMVSHDEHLISGSvDELW 695
|
....*..
gi 23397593 656 VLSDGKI 662
Cdd:PLN03073 696 VVSEGKV 702
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
462-672 |
2.54e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.05 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTiaLLMLRLYDPQG--GTVHLDGIDLrtvnPQW-----LRNNIGAVSQEPVLFS 534
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTT--LLGTLCGDPRAtsGRIVFDGKDI----TDWqtakiMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 -CSIRENILYGanpGETPSPERLQQVIEdanvsQFTDQLPDGLDTLVgQRGMMLSGGQKQRVAIARALIKNPAILILDEA 613
Cdd:PRK11614 94 rMTVEENLAMG---GFFAERDQFQERIK-----WVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 614 TSALDAVsenLVQNALDNLIQ----GRTVLTIAHRLS-TIRNADQIAVLSDGKIVEQGSYNELM 672
Cdd:PRK11614 165 SLGLAPI---IIQQIFDTIEQlreqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
456-671 |
2.73e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.70 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 456 TRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWL---RNNIGAVSQEPVL 532
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 533 FS-CSIRENILYganpgetpsPERLQQviedanvsqftdQLPDGL--DTL------VGQRG---MM---LSGGQKQRVAI 597
Cdd:PRK11831 96 FTdMNVFDNVAY---------PLREHT------------QLPAPLlhSTVmmkleaVGLRGaakLMpseLSGGMARRAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 598 ARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
451-666 |
3.43e-10 |
|
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: 59.97 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 451 FFTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTiaLLM-----LRLYDPQGGTVHLDGIDLRTVNPQWLRNNIgA 525
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST--LLKalanrTEGNVSVEGDIHYNGIPYKEFAEKYPGEII-Y 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 526 VSQE----PVL-------FSCSIRENilyganpgetpsperlqQVIedanvsqftdqlpdgldtlvgqRGmmLSGGQKQR 594
Cdd:cd03233 88 VSEEdvhfPTLtvretldFALRCKGN-----------------EFV----------------------RG--ISGGERKR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 595 VAIARALIKNPAILILDEATSALDAVSenlvqnALDnLIQGRTVLTIAHRLSTIRNA-----------DQIAVLSDGKIV 663
Cdd:cd03233 127 VSIAEALVSRASVLCWDNSTRGLDSST------ALE-ILKCIRTMADVLKTTTFVSLyqasdeiydlfDKVLVLYEGRQI 199
|
...
gi 23397593 664 EQG 666
Cdd:cd03233 200 YYG 202
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
479-619 |
4.07e-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: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 479 VGRSGSGKTTIallmLR----LYDPQGGTVHLDGidlRTVNPQWLRN-NIGAVSQEPVLFS-CSIRENILYGANPGETPS 552
Cdd:PRK11650 36 VGPSGCGKSTL----LRmvagLERITSGEIWIGG---RVVNELEPADrDIAMVFQNYALYPhMSVRENMAYGLKIRGMPK 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 553 PERLQQVIEDANVSQftdqlpdgLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDA 619
Cdd:PRK11650 109 AEIEERVAEAARILE--------LEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
473-671 |
4.34e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 61.68 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 473 GTTTAVVGRSGSGKTTIALLMLRLYDPQG----GTVHLDGIDLRTVNPQWLRNNIGA----VSQEPV--LFSC-----SI 537
Cdd:PRK11022 33 GEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLQRISEKERRNLVGAevamIFQDPMtsLNPCytvgfQI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 538 RENILY--GANpgetpSPERLQQVIEDANVSQFTDqlPDG-LDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDEAT 614
Cdd:PRK11022 113 MEAIKVhqGGN-----KKTRRQRAIDLLNQVGIPD--PASrLDVYPHQ----LSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 615 SALDAVSENLVQNALDNLIQGR--TVLTIAHRLSTI-RNADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKEnmALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
467-672 |
7.47e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.97 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 467 SLNLMPGTTTAVVGRSGSGKTTIALLMLRL----YDPQGGTVHLDGIDLRTVNPQWLR----NNIGAVSQEPVlfSC-SI 537
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRklvgHNVSMIFQEPQ--SClDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 538 RENI---LYGANPGETPSPE-------RLQQVIEDANVSQFTDQlpdglDTLVGQRGMMLSGGQKQRVAIARALIKNPAI 607
Cdd:PRK15093 105 SERVgrqLMQNIPGWTYKGRwwqrfgwRKRRAIELLHRVGIKDH-----KDAMRSFPYELTEGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 608 LILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELM 672
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELV 247
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
445-645 |
8.07e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 445 VGFQNVFFTFPTRpesAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVhldgidlrtVNPQWLRnnIG 524
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 525 AVSQ----EPVLfscsirenilyganPGETPSPERLQQVIEDANVSQFTDQLPDGldTLVGQRGMMLSGGQKQRVAIARA 600
Cdd:PRK09544 71 YVPQklylDTTL--------------PLTVNRFLRLRPGTKKEDILPALKRVQAG--HLIDAPMQKLSGGETQRVLLARA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 23397593 601 LIKNPAILILDEATSALDAVSenlvQNALDNLI-QGRT-----VLTIAHRL 645
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNG----QVALYDLIdQLRReldcaVLMVSHDL 181
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
458-649 |
1.23e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 61.30 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 458 PESAVLT-DFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTvhldgidlRTVNPqwlRNNIGAVSQEPVLFSCS 536
Cdd:TIGR00954 462 PNGDVLIeSLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGR--------LTKPA---KGKLFYVPQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 537 IRENILYganpgetpsPERLQQVIE----DANVSQFTDQLPdgLDTLVgQRGM----------MLSGGQKQRVAIARALI 602
Cdd:TIGR00954 531 LRDQIIY---------PDSSEDMKRrglsDKDLEQILDNVQ--LTHIL-EREGgwsavqdwmdVLSGGEKQRIAMARLFY 598
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 23397593 603 KNPAILILDEATSALDAVSENLVQNALDNLiqGRTVLTIAHRLSTIR 649
Cdd:TIGR00954 599 HKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWK 643
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
127-413 |
1.24e-09 |
|
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: 59.93 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 127 IGCLVVSSAITMSVPLFLGKVID-VVFNKSGMDSAAMAKLGEYSVLLFGIFVLGGFANFarvhLFGNAALRIVRSLRSRL 205
Cdd:cd18560 2 LLLLILGKACNVLAPLFLGRAVNaLTLAKVKDLESAVTLILLYALLRFSSKLLKELRSL----LYRRVQQNAYRELSLKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 206 YRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDGLRSVAMIGVGTGM-MIYTSPQLAAVSALvvpamagMAI 284
Cdd:cd18560 78 FAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVfAFHFGAWLALIVFL-------SVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 285 VYGRYVRRITKVELdKYAEIMKFAEER--------FGNVKTVKTFCREQQEVAAFDGKLDEalqigYKETRARAIF-FGL 355
Cdd:cd18560 151 LYGVFTIKVTEWRT-KFRRAANKKDNEahdiavdsLLNFETVKYFTNEKYEVDRYGEAVKE-----YQKSSVKVQAsLSL 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 356 TGFCGNFII----ISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQLNKGI 413
Cdd:cd18560 225 LNVGQQLIIqlglTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
467-671 |
1.53e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 59.23 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 467 SLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVnPQWLRNNIGAVS--QEPVLF-SCSIRENILY 543
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIARMGVVRtfQHVRLFrEMTVIENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 544 --------GANPG--ETPSPERLQ-QVIEDAnvSQFTDQLpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDE 612
Cdd:PRK11300 104 aqhqqlktGLFSGllKTPAFRRAEsEALDRA--ATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 613 ATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNEL 671
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
439-671 |
2.52e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 59.33 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 439 EKPVGEVGFQNVFFTFPTRPESAVlTDFSLNLMPGTTTAVVGRSGSGKTTiALLMLR--LYdPQGGTVHLDGIDlrtvnP 516
Cdd:COG4586 15 EKEPGLKGALKGLFRREYREVEAV-DDISFTIEPGEIVGFIGPNGAGKST-TIKMLTgiLV-PTSGEVRVLGYV-----P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 517 QWLRN----NIGAV----SQ----EPVLFSCSI-REniLYGAnpgetpSPERLQQviedaNVSQFTDQLpdGLDTLVGQR 583
Cdd:COG4586 87 FKRRKefarRIGVVfgqrSQlwwdLPAIDSFRLlKA--IYRI------PDAEYKK-----RLDELVELL--DLGELLDTP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 584 GMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDG 660
Cdd:COG4586 152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRerGTTILLTSHDMDDIEAlCDRVIVIDHG 231
|
250
....*....|.
gi 23397593 661 KIVEQGSYNEL 671
Cdd:COG4586 232 RIIYDGSLEEL 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
458-663 |
3.35e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 458 PESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDG--IDLRTvNPQWLRNNIGAVSQE-PVLFS 534
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKS-SKEALENGISMVHQElNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENILYGANPGETPsperlqqVIEDANVSQFTDQLPDGLDTLVGQRGMM--LSGGQKQRVAIARALIKNPAILILDE 612
Cdd:PRK10982 88 RSVMDNMWLGRYPTKGM-------FVDQDKMYRDTKAIFDELDIDIDPRAKVatLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 613 ATSALdavSENLVqNALDNLI-----QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIV 663
Cdd:PRK10982 161 PTSSL---TEKEV-NHLFTIIrklkeRGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
131-408 |
5.23e-09 |
|
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: 57.91 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 131 VVSSAITMSV-----PLFLGKVIDVVFNKSGMDSAAMAKLGEYSVLLF-GIFvlggfaNFARVHLFGNAALRIVRSLRSR 204
Cdd:cd18783 7 VAIASLILHVlalapPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFeGIL------GYLRRYLLLVATTRIDARLALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 205 LYRSMLMQEVGWFDTKGTGELINRLSnDTLMVGTSLSQNVSDGLRSVAMIGVGTGMMIYTSPQLAavsaLVVPAMAGM-- 282
Cdd:cd18783 81 TFDRLLSLPIDFFERTPAGVLTKHMQ-QIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLA----LVVLAFSALia 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 283 ---AIVYGRYVRRITKV---ELDKYAEIMkfaeERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLT 356
Cdd:cd18783 156 liiLAFLPPFRRRLQALyraEGERQAFLV----ETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLT 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 357 GFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVA---ISMNGLSNFYSQ 408
Cdd:cd18783 232 GPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAgplVQLAGLVQEYQE 286
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
430-662 |
9.67e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 9.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 430 PIDKGVVPLEKPVGEvGFQNVfftfptrpesavltdfSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGI 509
Cdd:PRK15439 263 AAGAPVLTVEDLTGE-GFRNI----------------SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 510 DLRTVNPQwLRNNIGAV-----SQEPVLF-SCSIRENI--LYGANPGETPSPERlqqviEDANVSQFTDQLP---DGLDT 578
Cdd:PRK15439 326 EINALSTA-QRLARGLVylpedRQSSGLYlDAPLAWNVcaLTHNRRGFWIKPAR-----ENAVLERYRRALNikfNHAEQ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 579 LVGQrgmmLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIRN-ADQIAV 656
Cdd:PRK15439 400 AART----LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAaQNVAVLFISSDLEEIEQmADRVLV 475
|
....*.
gi 23397593 657 LSDGKI 662
Cdd:PRK15439 476 MHQGEI 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
554-663 |
1.08e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 554 ERLQQVIEDANVSQFTDQLPDGLDTLvGQRGMM----LSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNAL 629
Cdd:PRK11147 121 AKLQEQLDHHNLWQLENRINEVLAQL-GLDPDAalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL 199
|
90 100 110
....*....|....*....|....*....|....*
gi 23397593 630 DNLiQGRTVLtIAHRLSTIRN-ADQIAVLSDGKIV 663
Cdd:PRK11147 200 KTF-QGSIIF-ISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
556-671 |
1.73e-08 |
|
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: 58.10 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 556 LQQVIEDAnvSQFTDQLPD---GLDTLV---------GQRGMMLSGGQKQRVAIARALIK---NPAILILDEATSALDAV 620
Cdd:TIGR00630 789 LDMTVEEA--YEFFEAVPSisrKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFD 866
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 621 SENLVQNALDNLI-QGRTVLTIAHRLSTIRNADQIAVL------SDGKIVEQGSYNEL 671
Cdd:TIGR00630 867 DIKKLLEVLQRLVdKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
462-644 |
2.45e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.96 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 462 VLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLY--DPQGGTVHLDGIDLRTVNPQ----WLRNNIGAVSQepVLFSC 535
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREASLidaiGRKGDFKDAVE--LLNAV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 536 SIRENILYGANPGEtpsperlqqviedanvsqftdqlpdgldtlvgqrgmmLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:COG2401 123 GLSDAVLWLRRFKE-------------------------------------LSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|.
gi 23397593 616 ALDAVSENLVQNALDNLIQ--GRTVLTIAHR 644
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARraGITLVVATHH 196
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
449-671 |
2.67e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.27 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 449 NVFFTFPTRPESAVlTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQG---GTVHLDGIDLRTVNPQWLR----N 521
Cdd:PRK09473 19 RVTFSTPDGDVTAV-NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKELNklraE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 522 NIGAVSQEPvlfscsireniLYGANPGETPSpERLQQVI---EDANVSQFTDQLPDGLDTL----VGQRGMM----LSGG 590
Cdd:PRK09473 98 QISMIFQDP-----------MTSLNPYMRVG-EQLMEVLmlhKGMSKAEAFEESVRMLDAVkmpeARKRMKMypheFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 591 QKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGS 667
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
....
gi 23397593 668 YNEL 671
Cdd:PRK09473 246 ARDV 249
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
459-676 |
2.90e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.18 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTI-ALLMLRL-YDPQGGTVHLDGIDLRTVNPQ-WLRNNIGAVSQEPVLFSC 535
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGTVEFKGKDLLELSPEdRAGEGIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 536 SirENILYGANPGETPSPERLQQVIEDANVSQFTD------QLPDGLDTLVGQRGmmLSGGQKQRVAIARALIKNPAILI 609
Cdd:PRK09580 93 V--SNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEekiallKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 610 LDEATSALDAVSENLVQNALDNLIQG-RTVLTIAH--RLSTIRNADQIAVLSDGKIVEQGSYNELMGIQE 676
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEE 238
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
126-419 |
3.18e-08 |
|
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: 55.57 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 126 GIGCLVVSSAITMSVPLFLGKVIDVVfnkSGMDSAAMAKLGEYSVLLFGIFVLGGFANfarvHLFGNAALRI---VRS-L 201
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYL---SSYPDEPLSEGYLLALALFLVSLLQSLLL----HQYFFLSFRLgmrVRSaL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 202 RSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGtSLSQNVSDGLRSVAMIGVGTGMMIYtspQL--AAVSALVVpaM 279
Cdd:cd18579 75 SSLIYRKALRLSSSARQETSTGEIVNLMSVDVQRIE-DFFLFLHYLWSAPLQIIVALYLLYR---LLgwAALAGLGV--L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 280 AGMAIVYGRYVRRITKVeldkYAEIMKFAEER-------FGNVKTVKTFCREQqevaAFDGKLDEA----LQIGYKETRA 348
Cdd:cd18579 149 LLLIPLQAFLAKLISKL----RKKLMKATDERvkltneiLSGIKVIKLYAWEK----PFLKRIEELrkkeLKALRKFGYL 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 349 RAIFFGLTGFCGNFIIISVLyygGTLVL-QDSLTIGalTAFMLYA--GYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18579 221 RALNSFLFFSTPVLVSLATF---ATYVLlGNPLTAA--KVFTALSlfNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
568-666 |
4.02e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.48 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 568 FTDQLPD----GLDTL-VGQRGMMLSGGQKQRVAIARALIKNP--AILILDEATSALDAVSENLVQNALDNLI-QGRTVL 639
Cdd:cd03238 64 FIDQLQFlidvGLGYLtLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVI 143
|
90 100 110
....*....|....*....|....*....|...
gi 23397593 640 TIAHRLSTIRNADQI------AVLSDGKIVEQG 666
Cdd:cd03238 144 LIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
575-667 |
7.55e-08 |
|
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: 54.16 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 575 GLDTL-VGQRGMMLSGGQKQRVAIARALIK---NPAILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIR 649
Cdd:cd03271 157 GLGYIkLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIK 236
|
90 100
....*....|....*....|....
gi 23397593 650 NADQIAVLS------DGKIVEQGS 667
Cdd:cd03271 237 CADWIIDLGpeggdgGGQVVASGT 260
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
465-648 |
8.06e-08 |
|
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: 55.56 E-value: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 465 DFSLNLMPGT-----TTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDgIDLrTVNPQWLRNNIgavsQEPVlfscsirE 539
Cdd:COG1245 353 GFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKI-SYKPQYISPDY----DGTV-------E 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 540 NILYGANPGETPSPERLQQVIEdanvsqftdqlPDGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDa 619
Cdd:COG1245 420 EFLRSANTDDFGSSYYKTEIIK-----------PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD- 487
|
170 180 190
....*....|....*....|....*....|..
gi 23397593 620 VSENL-VQNALDNLI--QGRTVLTIAHRLSTI 648
Cdd:COG1245 488 VEQRLaVAKAIRRFAenRGKTAMVVDHDIYLI 519
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
480-620 |
1.09e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 480 GRSGSGKTTiALLMLR-LYDPQGGTVHLDGidlRTVNPQWL--RNNIGAVSQEpvlFSC----SIRENI-----LYGANP 547
Cdd:NF033858 299 GSNGCGKST-TMKMLTgLLPASEGEAWLFG---QPVDAGDIatRRRVGYMSQA---FSLygelTVRQNLelharLFHLPA 371
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23397593 548 GETPspERLQQVIEDANVSQFTDQLPDGLdtlvgqrgmmlSGGQKQRVAIARALIKNPAILILDEATSALDAV 620
Cdd:NF033858 372 AEIA--ARVAEMLERFDLADVADALPDSL-----------PLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
458-643 |
1.91e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 458 PESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHldgidlrtvnpqwlrnnigavsqepvlfsCSI 537
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-----------------------------CGT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 538 RENILYGANPGETPSPERlqQVIedanvsqftDQLPDGLDTLV--GQ----------------RGMM----LSGGQKQRV 595
Cdd:PRK11147 381 KLEVAYFDQHRAELDPEK--TVM---------DNLAEGKQEVMvnGRprhvlgylqdflfhpkRAMTpvkaLSGGERNRL 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 23397593 596 AIARALIKNPAILILDEATSALDAVSENLVQNALDNLiQGrTVLTIAH 643
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY-QG-TVLLVSH 495
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
165-293 |
1.97e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) 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: 350048 [Multi-domain] Cd Length: 297 Bit Score: 53.24 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 165 LGEYSVLLFGIFVLGGFANFarvhLFGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNV 244
Cdd:cd18604 46 LGIYALISLLSVLLGTLRYL----LFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSL 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 23397593 245 SDGLRSVAMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAIVY---GRYVRRI 293
Cdd:cd18604 122 SSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYlraSRELKRL 173
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
472-645 |
2.06e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 472 PGTTTAVVGRSGSGKTTIA-----LLMLRLYDPQG------------GTV---HLDGI---DLRTV-NPQWlrnnigaVS 527
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVkilsgELIPNLGDYEEepswdevlkrfrGTElqnYFKKLyngEIKVVhKPQY-------VD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 528 QEPVLFSCSIREnILYGANpgetpspER--LQQVIEdanvsqftdQLpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNP 605
Cdd:PRK13409 171 LIPKVFKGKVRE-LLKKVD-------ERgkLDEVVE---------RL--GLENILDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 23397593 606 AILILDEATSALDaVSENL-VQNALDNLIQGRTVLTIAHRL 645
Cdd:PRK13409 232 DFYFFDEPTSYLD-IRQRLnVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
456-640 |
3.41e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 456 TRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQwlrNNIGAVSQEPVLFS- 534
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLKAd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENI-----LYGANPGETPSpERLQQViedanvsqftdQLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILI 609
Cdd:PRK13543 97 LSTLENLhflcgLHGRRAKQMPG-SALAIV-----------GLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWL 160
|
170 180 190
....*....|....*....|....*....|...
gi 23397593 610 LDEATSALDAVSENLVQNALDNLI--QGRTVLT 640
Cdd:PRK13543 161 LDEPYANLDLEGITLVNRMISAHLrgGGAALVT 193
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
463-671 |
5.44e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.97 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNPQWLRNNIGAVsqepvlfscsirENI- 541
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI------------ENIe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 542 LYGANPGETPSP--ERLQQVIEDANVSQFtdqlpdgldtlVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDA 619
Cdd:PRK13545 108 LKGLMMGLTKEKikEIIPEIIEFADIGKF-----------IYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23397593 620 VSENLVQNALDNLI-QGRTVLTIAHRLSTIRNADQIAV-LSDGKIVEQGSYNEL 671
Cdd:PRK13545 177 TFTKKCLDKMNEFKeQGKTIFFISHSLSQVKSFCTKALwLHYGQVKEYGDIKEV 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
441-662 |
5.67e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 441 PVGEVGFQ--NVFFTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYdpQG---GTVHLDGIDLRTVN 515
Cdd:PRK13549 254 TIGEVILEvrNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY--PGrweGEIFIDGKPVKIRN 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 516 P-QWLRNNIGAVSQE-------PVLfscSIRENILYgANPGETPSPERLQQVIEDANVSQFTDQL------PDgldtlvg 581
Cdd:PRK13549 332 PqQAIAQGIAMVPEDrkrdgivPVM---GVGKNITL-AALDRFTGGSRIDDAAELKTILESIQRLkvktasPE------- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 582 QRGMMLSGGQKQRVAIARALIKNPAILILDEATSALD--AVSE--NLVqNALDNliQGRTVLTIAHRLSTIRN-ADQIAV 656
Cdd:PRK13549 401 LAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgAKYEiyKLI-NQLVQ--QGVAIIVISSELPEVLGlSDRVLV 477
|
....*.
gi 23397593 657 LSDGKI 662
Cdd:PRK13549 478 MHEGKL 483
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
576-671 |
5.85e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 576 LDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLSTIRN-ADQ 653
Cdd:NF000106 134 LTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQlAHE 213
|
90
....*....|....*...
gi 23397593 654 IAVLSDGKIVEQGSYNEL 671
Cdd:NF000106 214 LTVIDRGRVIADGKVDEL 231
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
448-670 |
9.48e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 9.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 448 QNVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVhldgidlrtvnpQWLRN-NIGAV 526
Cdd:PRK15064 323 ENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSENaNIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 527 SQEPVlfscsirenilyganpgetpsperlQQVIEDANV----SQFTDqlPDGLDTLVgqRGMM---------------- 586
Cdd:PRK15064 388 AQDHA-------------------------YDFENDLTLfdwmSQWRQ--EGDDEQAV--RGTLgrllfsqddikksvkv 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 587 LSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLiQGrTVLTIAH-R--LSTIrnADQIAVLSDGKIV 663
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdRefVSSL--ATRIIEITPDGVV 514
|
....*...
gi 23397593 664 E-QGSYNE 670
Cdd:PRK15064 515 DfSGTYEE 522
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
449-652 |
1.03e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.95 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 449 NVFFTFPTRPesaVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGidlrtvnpQWLRNNIGAVSQ 528
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER--------QSIKKDLCTYQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 529 E-----------PVLfscSIRENILYGANPGETPSpeRLQQVIEDANVSQFTDqLPDGLdtlvgqrgmmLSGGQKQRVAI 597
Cdd:PRK13540 75 QlcfvghrsginPYL---TLRENCLYDIHFSPGAV--GITELCRLFSLEHLID-YPCGL----------LSSGQKRQVAL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 598 ARALIKNPAILILDEATSALDAVS-ENLVQNALDNLIQGRTVLTIAHRLSTIRNAD 652
Cdd:PRK13540 139 LRLWMSKAKLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
463-666 |
1.16e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 50.65 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRtvnpQWLRNNIGAV---SQE-----PVLfs 534
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLVAYvpqSEEvdwsfPVL-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 csIRENILYG--ANPGETPSPERLQQVIEDANVSQFtdqlpDGLDTLVGQRGMmLSGGQKQRVAIARALIKNPAILILDE 612
Cdd:PRK15056 97 --VEDVVMMGryGHMGWLRRAKKRDRQIVTAALARV-----DMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23397593 613 ATSALDAVSENLVQNALDNL-IQGRTVLTIAHRLSTIRNADQIAVLSDGKIVEQG 666
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
459-667 |
1.26e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLML--RLYDPQGGTVHLDGIDLRTVNPQwLRNNIGA--VSQEPVLFS 534
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEPE-ERAHLGIflAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 535 CSIRENIL---YGANpgetpspeRLQQVIEDANVSQFTDQLPDGLDtLVGQRGMML--------SGGQKQRVAIARALIK 603
Cdd:CHL00131 98 GVSNADFLrlaYNSK--------RKFQGLPELDPLEFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 604 NPAILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAH--RLSTIRNADQIAVLSDGKIVEQGS 667
Cdd:CHL00131 169 DSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
463-648 |
1.66e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGT-----TTAVVGRSGSGKTTIALLMLRLYDPQGGTVhldGIDLR-TVNPQWLRNNI-GAVSQepvlFSC 535
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKiSYKPQYIKPDYdGTVED----LLR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 536 SIRENilYGANPGETPSPERLQqviedanvsqftdqLPDGLDTLVGQrgmmLSGGQKQRVAIARALIKNPAILILDEATS 615
Cdd:PRK13409 423 SITDD--LGSSYYKSEIIKPLQ--------------LERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170 180 190
....*....|....*....|....*....|....*.
gi 23397593 616 ALDaVSENL-VQNALDNLIQGR--TVLTIAHRLSTI 648
Cdd:PRK13409 483 HLD-VEQRLaVAKAIRRIAEEReaTALVVDHDIYMI 517
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
135-388 |
1.99e-06 |
|
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: 50.24 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 135 AITMSVPLFLGKVIDVVFNKSGMDsaAMaklgeySVLLFGIFVLGGF---ANFARVHLFGNAALRIVRSLRSRLYRSMLM 211
Cdd:cd18779 16 LLGLALPLLTGVLVDRVIPRGDRD--LL------GVLGLGLAALVLTqllAGLLRSHLLLRLRTRLDTQLTLGFLEHLLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 212 QEVGWFDTKGTGELINRL-SNDTL--MVGTSLSQNVSDGlrsvAMIGVGTGMMIYTSPQLAAVSALVVPAMAGMAIVYGR 288
Cdd:cd18779 88 LPYRFFQQRSTGDLLMRLsSNATIreLLTSQTLSALLDG----TLVLGYLALLFAQSPLLGLVVLGLAALQVALLLATRR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 289 YVRRITKVELDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGLTGFCGNFIIISVL 368
Cdd:cd18779 164 RVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLL 243
|
250 260
....*....|....*....|
gi 23397593 369 YYGGTLVLQDSLTIGALTAF 388
Cdd:cd18779 244 WVGAWQVLDGQLSLGTMLAL 263
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
472-657 |
2.90e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 472 PGTTTAVVGRSGSGKTTIallmLRLydpqggtvhLDGIdlrtvnpqwLRNNIGAVSQEP----VL--FSCSIRENILYGA 545
Cdd:COG1245 98 KGKVTGILGPNGIGKSTA----LKI---------LSGE---------LKPNLGDYDEEPswdeVLkrFRGTELQDYFKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 546 NPGEtpsperlqqvIEDANVSQFTDQLPDGLDTLVGQ-------RGMM-------------------LSGGQKQRVAIAR 599
Cdd:COG1245 156 ANGE----------IKVAHKPQYVDLIPKVFKGTVREllekvdeRGKLdelaeklglenildrdiseLSGGELQRVAIAA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23397593 600 ALIKNPAILILDEATSALDaVSENL-VQNALDNLIQ-GRTVLTIAHRLSTIRN-ADQIAVL 657
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLD-IYQRLnVARLIRELAEeGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
455-662 |
2.92e-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: 50.21 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 455 PTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQ-GGTVHLDGIDLRTVNP-QWLRNNIGAVSQE--- 529
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPaQAIRAGIAMVPEDrkr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 530 ----PVLfscSIRENILYG-----ANPGETPSPERLQQV---IEDANVSQFTDQLPDGldtlvgqrgmMLSGGQKQRVAI 597
Cdd:TIGR02633 348 hgivPIL---GVGKNITLSvlksfCFKMRIDAAAELQIIgsaIQRLKVKTASPFLPIG----------RLSGGNQQKAVL 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 598 ARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ-GRTVLTIAHRLSTIRN-ADQIAVLSDGKI 662
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQeGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
440-664 |
6.39e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.40 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 440 KPVGEVgfQNVfftfpTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTialLMLRLY--DP-QGGTVHLDGIDLRTVNP 516
Cdd:PRK09700 263 ETVFEV--RNV-----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTE---LMNCLFgvDKrAGGEIRLNGKDISPRSP 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 517 -QWLRNNIGAVSQ---EPVLFS-CSIRENILYgANPGETPSPERLQQVIEDANVSQFTDQLPDGLD---TLVGQRGMMLS 588
Cdd:PRK09700 333 lDAVKKGMAYITEsrrDNGFFPnFSIAQNMAI-SRSLKDGGYKGAMGLFHEVDEQRTAENQRELLAlkcHSVNQNITELS 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23397593 589 GGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIRNA-DQIAVLSDGKIVE 664
Cdd:PRK09700 412 GGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
168-292 |
7.78e-06 |
|
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: 48.24 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 168 YSVLLFGIFVLGG-FANFARVHLFGNAALRIVRSlrsrlyrsmlmqEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSD 246
Cdd:cd18606 48 QAIFLFLFGLLLAyLGIRASKRLHNKALKRVLRA------------PMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRM 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 23397593 247 GLRSVAMIgVGT-GMMIYTSPQLaavsALVVPAMAGMAIVYGRYVRR 292
Cdd:cd18606 116 FLYTLSSI-IGTfILIIIYLPWF----AIALPPLLVLYYFIANYYRA 157
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
168-419 |
1.11e-05 |
|
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: 47.91 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 168 YSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDTLMVGTSLSQNVSDG 247
Cdd:cd18605 44 FLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNIL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 248 LRSVA-MIGVGTGMMIytspQLAAVSALVVPAMAGMAIVYGRY------VRRITKVELDK-YAEImkfaEERFGNVKTVK 319
Cdd:cd18605 124 LAQLFgLLGYLVVICY----QLPWLLLLLLPLAFIYYRIQRYYratsreLKRLNSVNLSPlYTHF----SETLKGLVTIR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 320 TFCREQQEVAAFDGKLDEALQIGYKETRA------RAIFFG--LTGFCGNFIIISVLYYGGTlvlqDSLTIG-ALTafml 390
Cdd:cd18605 196 AFRKQERFLKEYLEKLENNQRAQLASQAAsqwlsiRLQLLGvlIVTFVALTAVVQHFFGLSI----DAGLIGlALS---- 267
|
250 260
....*....|....*....|....*....
gi 23397593 391 YAGYVAISMNGLSNFYSQLNKGIGASERI 419
Cdd:cd18605 268 YALPITGLLSGLLNSFTETEKEMVSVERV 296
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
483-663 |
1.19e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 483 GSGKTTIALLMLRLYDPQGGTVHLDGIDLRtvnpqwLRNNIGAVSQEPVLfsC-------------SIRENILYGANPGE 549
Cdd:PRK11288 289 GAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIRAGIML--CpedrkaegiipvhSVADNINISARRHH 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 550 TPSPERLQQVIEDANVSQFTDQL----PDGlDTLVgqrgMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLV 625
Cdd:PRK11288 361 LRAGCLINNRWEAENADRFIRSLniktPSR-EQLI----MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEI 435
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 23397593 626 QNALDNLI-QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIV 663
Cdd:PRK11288 436 YNVIYELAaQGVAVLFVSSDLPEVLGvADRIVVMREGRIA 475
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
587-682 |
1.36e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 587 LSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQ--GRTVLTIAHRLSTIRNADQIAVLSDGKIVE 664
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEGEPGV 151
|
90
....*....|....*...
gi 23397593 665 QGSYNELMGIQEGVFREL 682
Cdd:cd03222 152 YGIASQPKGTREGINRFL 169
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
459-662 |
1.42e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 459 ESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHL-DGIDLrtvnpqwlrnniGAVSQEPVLFscsI 537
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKL------------GYFAQHQLEF---L 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 538 RENilyganpgETPsperLQQVIEDANvSQFTDQLPDGLDTL------VGQRGMMLSGGQKQRVAIARALIKNPAILILD 611
Cdd:PRK10636 389 RAD--------ESP----LQHLARLAP-QELEQKLRDYLGGFgfqgdkVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 612 EATSALD-----AVSENLVQnaldnlIQGRTVLtIAHRLSTIRN-ADQIAVLSDGKI 662
Cdd:PRK10636 456 EPTNHLDldmrqALTEALID------FEGALVV-VSHDRHLLRStTDDLYLVHDGKV 505
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
439-663 |
2.95e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 439 EKPVGEVGFQ----NVFFtfPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIAL-LMLRLYDPQ-GGTVHLDG--ID 510
Cdd:NF040905 250 TPKIGEVVFEvknwTVYH--PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMsVFGRSYGRNiSGTVFKDGkeVD 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 511 LRTVnPQWLRNNIGAVSQEP-----VLFScSIRENILyGANPGETPSPERLQQVIEDANVSQFTDQL----PDgldtlVG 581
Cdd:NF040905 328 VSTV-SDAIDAGLAYVTEDRkgyglNLID-DIKRNIT-LANLGKVSRRGVIDENEEIKVAEEYRKKMniktPS-----VF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 582 QRGMMLSGGQKQRVAIARALIKNPAILILDEATSALD--AVSE-NLVQNALDNliQGRTVLTIAHRL-STIRNADQIAVL 657
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgAKYEiYTIINELAA--EGKGVIVISSELpELLGMCDRIYVM 477
|
....*.
gi 23397593 658 SDGKIV 663
Cdd:NF040905 478 NEGRIT 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
463-672 |
3.24e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNP-QWLRNNIGAVSQE----------PV 531
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAnEAINHGFALVTEErrstgiyaylDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 532 LFScSIRENILYGANPGETPSPERL----QQVIEDANVSQFTDQlpdgldTLVGQrgmmLSGGQKQRVAIARALIKNPAI 607
Cdd:PRK10982 344 GFN-SLISNIRNYKNKVGLLDNSRMksdtQWVIDSMRVKTPGHR------TQIGS----LSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23397593 608 LILDEATSALDAVSE-NLVQNALDNLIQGRTVLTIAHRLSTIRN-ADQIAVLSDGK---IVE--QGSYNELM 672
Cdd:PRK10982 413 LMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLvagIVDtkTTTQNEIL 484
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
131-409 |
3.87e-05 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. 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: 350006 [Multi-domain] Cd Length: 289 Bit Score: 46.08 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 131 VVSSAITMSVPLFLGKVIDVVfnkSGMDSAAmaklgeysvLLFGIFVLGGFANFARVHLFGNAALRIvrSLRSRL----- 205
Cdd:cd18562 9 VALAGVQFAEPVLFGRVVDAL---SSGGDAF---------PLLALWAALGLFSILAGVLVALLADRL--AHRRRLavmas 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 206 -YRSMLMQEVGWFDTKGTGELINR-LSNDTLMVGTSLSQnVSDGLRSVAMIGVGTGMMIYTSPQLAAVsalvvpaMAGMA 283
Cdd:cd18562 75 yFEHVITLPLSFHSQRGSGRLLRImLRGTDALFGLWLGF-FREHLAALVSLIVLLPVALWMNWRLALL-------LVVLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 284 IVY---GRYVRRITK-----VElDKYAEIMKFAEERFGNVKTVKTFCREQQEVAAFDGKLDEALQIGYKETRARAIFFGL 355
Cdd:cd18562 147 AVYaalNRLVMRRTKagqaaVE-EHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITRRLLAAQYPVLNWWALASVL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 23397593 356 TGFCGNFIIISVLYYGGTLVLQDSLTIGALTAFMLYAGYVAISMNGLSNFYSQL 409
Cdd:cd18562 226 TRAASTLTMVAIFALGAWLVQRGELTVGEIVSFVGFATLLIGRLDQLSGFINRL 279
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
442-666 |
3.88e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 442 VGEVGFQNVFFTFPTRPESAVLTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQ---GGTVHLDGIDLRTVNPQ- 517
Cdd:PLN03140 160 IAESALGMLGINLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRk 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 518 ---WLRNN---IGAVS-QEPVLFS--CS---IRENILYG-----ANPGETPSPE----RLQQVIEDANVSQFTDQLPD-- 574
Cdd:PLN03140 240 tsaYISQNdvhVGVMTvKETLDFSarCQgvgTRYDLLSElarreKDAGIFPEAEvdlfMKATAMEGVKSSLITDYTLKil 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 575 GLD----TLVG---QRGmmLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLIQgRTVLTIAHRL-- 645
Cdd:PLN03140 320 GLDickdTIVGdemIRG--ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVH-LTEATVLMSLlq 396
|
250 260
....*....|....*....|....
gi 23397593 646 ---STIRNADQIAVLSDGKIVEQG 666
Cdd:PLN03140 397 papETFDLFDDIILLSEGQIVYQG 420
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
587-655 |
4.38e-05 |
|
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: 44.27 E-value: 4.38e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23397593 587 LSGGQKQRVAIARALI---KNPAIL-ILDEATSALDAVSENLVQNAL-DNLIQGRTVLTIAHRLSTIRNADQIA 655
Cdd:cd03227 78 LSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAIlEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
472-645 |
6.09e-05 |
|
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: 46.55 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 472 PGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTvNPQWLRNNIGAVSQ-EPVLFSCSIRENILYGANPGET 550
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQfDAIDDLLTGREHLYLYARLRGV 2042
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 551 PSpERLQQV----IEDANVSQFTDQLPDgldtlvgqrgmMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQ 626
Cdd:TIGR01257 2043 PA-EEIEKVanwsIQSLGLSLYADRLAG-----------TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
|
170 180
....*....|....*....|
gi 23397593 627 NALDNLI-QGRTVLTIAHRL 645
Cdd:TIGR01257 2111 NTIVSIIrEGRAVVLTSHSM 2130
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
463-672 |
6.23e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTIALLMLRLYDPQGGTVHLDG-IDLRTVNPQwLRNNIGAVsqEPVLFSCsirenI 541
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAISAG-LSGQLTGI--ENIEFKM-----L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 542 LYGANPGETPspERLQQVIEDANVSQFtdqlpdgldtlVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDavs 621
Cdd:PRK13546 112 CMGFKRKEIK--AMTPKIIEFSELGEF-----------IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD--- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 622 ENLVQNALDNLI----QGRTVLTIAHRLSTIRN-ADQIAVLSDGKIVEQGSYNELM 672
Cdd:PRK13546 176 QTFAQKCLDKIYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVL 231
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
168-421 |
8.62e-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: 44.90 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 168 YSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDtlmvgtslSQNVSDG 247
Cdd:cd18559 40 YLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKD--------LDRVDSM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 248 LRSVAMIGVGTGMMI---YTSPQLAAVSALVVPAMAGMAI----VYGRYVRRITKVELDKYAEIMKFAEERFGNVKTVKT 320
Cdd:cd18559 112 APQVIKMWMGPLQNViglYLLILLAGPMAAVGIPLGLLYVpvnrVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 321 FCREQQEVAAFDGKLDEALQIgYKETRARAIFFGLTGFCGNFIIISVLYYggTLVLQDSLTI-GALTAFmlYAGYVAISM 399
Cdd:cd18559 192 FEWEEAFIRQVDAKRDNELAY-LPSIVYLRALAVRLWCVGPCIVLFASFF--AYVSRHSLAGlVALKVF--YSLALTTYL 266
|
250 260
....*....|....*....|..
gi 23397593 400 NGLSNFYSQLNKGIGASERIWE 421
Cdd:cd18559 267 NWPLNMSPEVITNIVAAEVSLE 288
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
575-654 |
8.62e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 575 GLD--TLvGQRGMMLSGGQKQRVAIARALIK---NPAILILDEATSAL---DavsenlVQ---NALDNLI-QGRTVLTIA 642
Cdd:COG0178 814 GLGyiKL-GQPATTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLhfhD------IRkllEVLHRLVdKGNTVVVIE 886
|
90
....*....|..
gi 23397593 643 HRLSTIRNADQI 654
Cdd:COG0178 887 HNLDVIKTADWI 898
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
576-654 |
1.03e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.83 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 576 LDTLV---------GQRGMMLSGGQKQRVAIARALIKNP---AILILDEATSAL--DAVSeNLVqNALDNLI-QGRTVLT 640
Cdd:PRK00349 811 LQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfEDIR-KLL-EVLHRLVdKGNTVVV 888
|
90
....*....|....
gi 23397593 641 IAHRLSTIRNADQI 654
Cdd:PRK00349 889 IEHNLDVIKTADWI 902
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
554-646 |
1.04e-04 |
|
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: 44.66 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 554 ERLQQVIEDANVSQFTDQLpdGLDTLVGQRGMMLSGGQKQRVAIARALIKNPAILILDEATSALDAVSENLVQNALDNLI 633
Cdd:cd03236 109 ELLKKKDERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELA 186
|
90
....*....|....
gi 23397593 634 Q-GRTVLTIAHRLS 646
Cdd:cd03236 187 EdDNYVLVVEHDLA 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
463-621 |
1.48e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 463 LTDFSLNLMPGTTTAVVGRSGSGKTTiaLLML-----RLydpQGGTVHLDGIDL------RTVN------PQWLRNNIga 525
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSS--LLSLiagarKI---QQGRVEVLGGDMadarhrRAVCpriaymPQGLGKNL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 526 vsqEPVLfscSIRENI-----LYGANPGEtpSPERLQQVIEDANVSQFTDQlPDGldtlvgqrgmMLSGGQKQRVAIARA 600
Cdd:NF033858 90 ---YPTL---SVFENLdffgrLFGQDAAE--RRRRIDELLRATGLAPFADR-PAG----------KLSGGMKQKLGLCCA 150
|
170 180
....*....|....*....|.
gi 23397593 601 LIKNPAILILDEATSALDAVS 621
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLS 171
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
559-634 |
2.29e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 559 VIEDANVSQFTDQLPDGLDTLvgqrgmmlSGGQKQ------RVAIARALIKNPAILILDEATSALDAVSenlvQNALDNL 632
Cdd:PRK01156 782 VDQDFNITVSRGGMVEGIDSL--------SGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDR----RTNLKDI 849
|
..
gi 23397593 633 IQ 634
Cdd:PRK01156 850 IE 851
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
478-516 |
2.93e-04 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 42.35 E-value: 2.93e-04
10 20 30
....*....|....*....|....*....|....*....
gi 23397593 478 VVGRSGSGKTTIALLMLRLYDPQGGTVHLDGIDLRTVNP 516
Cdd:pfam06414 16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELHP 54
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
575-654 |
3.20e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 575 GLDTL-VGQRGMMLSGGQKQRVAIARALI---KNPAILILDEATSALDAVSENLVQNALDNLI-QGRTVLTIAHRLSTIR 649
Cdd:PRK00635 797 GLDYLpLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVK 876
|
....*
gi 23397593 650 NADQI 654
Cdd:PRK00635 877 VADYV 881
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
575-666 |
4.58e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.24 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 575 GLDTL-VGQRGMMLSGGQKQRVAIARALIKN--PAILILDEATSALDAVSENLVQNALDNL-IQGRTVLTIAHRLSTIRN 650
Cdd:cd03270 125 GLGYLtLSRSAPTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVEHDEDTIRA 204
|
90 100
....*....|....*....|..
gi 23397593 651 ADQI------AVLSDGKIVEQG 666
Cdd:cd03270 205 ADHVidigpgAGVHGGEIVAQG 226
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
165-233 |
6.00e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), 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: 350045 [Multi-domain] Cd Length: 314 Bit Score: 42.31 E-value: 6.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23397593 165 LGEYSVLLFGIFVLGgfanFARVHLFGNAALRIVRSLRSRLYRSMLMQEVGWFDTKGTGELINRLSNDT 233
Cdd:cd18601 62 LGIYAGLTAATFVFG----FLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDI 126
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
127-229 |
6.53e-04 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 42.40 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 127 IGCLVVSSAITMSVPLFLGKVIDVVFnksgMDSAAMAKLGEYSVLLFGIFVLGGFANFARVHLFGNAALRIVRSLRSRLY 206
Cdd:cd18584 2 VLLGLLAALLIIAQAWLLARIIAGVF----LEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLL 77
|
90 100
....*....|....*....|...
gi 23397593 207 RSMLMQEVGWFDTKGTGELINRL 229
Cdd:cd18584 78 ARLLALGPALLRRQSSGELATLL 100
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
149-293 |
1.06e-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: 41.70 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 149 DVVFNKSGMDSAAMAKLGEYSvlLFGIFVlgGFANFARVHLFGNAALRIVRSLRSRLYRSML---MQevgWFDTKGTGEL 225
Cdd:cd18603 28 DPALNGTQDTEQRDYRLGVYG--ALGLGQ--AIFVFLGSLALALGCVRASRNLHNKLLHNILrapMS---FFDTTPLGRI 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23397593 226 INRLSNDTLMVGTSLSQNVSDGLRSVAMIgVGTGMMI-YTSPQLAAVsalVVPamagMAIVYGrYVRRI 293
Cdd:cd18603 101 LNRFSKDIDTVDNTLPQNIRSFLNCLFQV-ISTLVVIsISTPIFLVV---IIP----LAILYF-FIQRF 160
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
582-654 |
1.37e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 1.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23397593 582 QRGMMLSGGQKQRVAIarALI-----KNPA-ILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQI 654
Cdd:pfam02463 1073 KNLDLLSGGEKTLVAL--ALIfaiqkYKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKL 1149
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
556-667 |
2.02e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23397593 556 LQQVIED-ANVSQFTDQLPDGLDTLV---------GQRGMMLSGGQKQRVAIARALI---KNPAILILDEATSALDAVSE 622
Cdd:PRK00635 1659 LQTPIEEvAETFPFLKKIQKPLQALIdnglgylplGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQK 1738
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 23397593 623 NLVQNALDNLI-QGRTVLTIAHRLSTIRNADQIAVL------SDGKIVEQGS 667
Cdd:PRK00635 1739 SALLVQLRTLVsLGHSVIYIDHDPALLKQADYLIEMgpgsgkTGGKILFSGP 1790
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
587-636 |
3.33e-03 |
|
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: 39.51 E-value: 3.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 23397593 587 LSGGQKQ------RVAIARALIKNPAILILDEATSALDavSENlVQNALDNLIQGR 636
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD--EEN-IEESLAEIIEER 168
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
588-618 |
3.93e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 3.93e-03
10 20 30
....*....|....*....|....*....|.
gi 23397593 588 SGGQKQRVAIARALIKNPAILILDEATSALD 618
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
582-654 |
8.65e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 38.21 E-value: 8.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23397593 582 QRGMMLSGGQKQRVAIAR--ALIK-NPA-ILILDEATSALDAVSENLVQNALDNLIQGRTVLTIAHRLSTIRNADQI 654
Cdd:cd03278 109 QRLSLLSGGEKALTALALlfAIFRvRPSpFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRL 185
|
|
| |
