|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-616 |
1.34e-122 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 374.89 E-value: 1.34e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 21 KSFRYWPSLFKLLWEtHRGYFFCVLVLNFLNGLLPASLILAIKYLVNMVqnlyIQGYKDNYFYDILPFFIFFSVVTLLTS 100
Cdd:COG1132 4 SPRKLLRRLLRYLRP-YRGLLILALLLLLLSALLELLLPLLLGRIIDAL----LAGGDLSALLLLLLLLLGLALLRALLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 101 ATGSILeTHKQLYRnlLSNKINVKLIEKAKRLPYASFENPEVYNKLQRARQDSTYKPFAIFEELMGIVKGAITLISISII 180
Cdd:COG1132 79 YLQRYL-LARLAQR--VVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 181 LMVWNWEFTLILILLPLISAWSIVNVGKEIflvsHKRAEETRKQF--YYYYLMTTDITVKEVKIFGLGSLLLRNYSDLFS 258
Cdd:COG1132 156 LFVIDWRLALIVLLVLPLLLLVLRLFGRRL----RKLFRRVQEALaeLNGRLQESLSGIRVVKAFGREERELERFREANE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 259 KFYNQDRHLLLKKMRIDLSFQLISVIFVIFVQFMIVKDTIQGLIAIGSLIAYFQAVNTTQKTSNELMYMVFNMHQNNLYM 338
Cdd:COG1132 232 ELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 339 TQLFSFLNVPestdkPNVSEEKTLENVSSTEEGIQFLNVSFKYPGqENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKL 418
Cdd:COG1132 312 ERIFELLDEP-----PEIPDPPGAVPLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 419 LTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDFVRYELDVKENIGYGDYKRSNHlvAIQAAAKRSGALTMIDSLP 498
Cdd:COG1132 386 LLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDE--EVEEAAKAAQAHEFIEALP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 499 DKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKY 578
Cdd:COG1132 464 DGYDTVVGE---RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRN 540
|
570 580 590
....*....|....*....|....*....|....*...
gi 502825101 579 ADRIIVLDKGEVAEYGTHVELLDTNGIYARLFNLQAKS 616
Cdd:COG1132 541 ADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-614 |
1.16e-91 |
|
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: 298.29 E-value: 1.16e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 15 SFVSILKSFRYWPSLFKLLWEtHRGYFFCVLVLNFLNGLLPASLILAIKYLVNMVQNlyiqgykDNYFYDILPFFIFFSV 94
Cdd:COG2274 133 EFDKRGEKPFGLRWFLRLLRR-YRRLLLQVLLASLLINLLALATPLFTQVVIDRVLP-------NQDLSTLWVLAIGLLL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 95 VTLLTSATGSIlethKQLYRNLLSNKINVKL----IEKAKRLPYASFEN---PEVYNKLQ---RARQ-----------DS 153
Cdd:COG2274 205 ALLFEGLLRLL----RSYLLLRLGQRIDLRLssrfFRHLLRLPLSFFESrsvGDLASRFRdveSIREfltgslltallDL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 154 tykPFAIFeelMGIVkgaitlisisiilMVW-NWEFTLILIllplisAWSIVNVGkEIFLVSHKRAEETRKQFYYYYLMT 232
Cdd:COG2274 281 ---LFVLI---FLIV-------------LFFySPPLALVVL------LLIPLYVL-LGLLFQPRLRRLSREESEASAKRQ 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 233 TDIT-----VKEVKIFGLGSLLLRNYSDLFSKFYNQDRHLLLKKMRIDLSFQLISVIFVIFVQFMIVKDTIQGLIAIGSL 307
Cdd:COG2274 335 SLLVetlrgIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 308 IAyFQAV--NTTQKTSNeLMYMVFNMHQNNLYMTQLFSFLNVPestdkPNVSEEKTLENVSSTEEGIQFLNVSFKYPGQE 385
Cdd:COG2274 415 IA-FNILsgRFLAPVAQ-LIGLLQRFQDAKIALERLDDILDLP-----PEREEGRSKLSLPRLKGDIELENVSFRYPGDS 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 386 NYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDFVRYELDVKE 465
Cdd:COG2274 488 PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRE 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 466 NIGYGDYKRSnhLVAIQAAAKRSGALTMIDSLPDKMDTQLGktfANGIQLSGGQWQRIAIARAYMRRASLYILDEPTAAL 545
Cdd:COG2274 568 NITLGDPDAT--DEEIIEAARLAGLHDFIEALPMGYDTVVG---EGGSNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 546 DPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYARLFNLQA 614
Cdd:COG2274 643 DAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
29-613 |
5.30e-76 |
|
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: 253.10 E-value: 5.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 29 LFKLLWETHRGY---FFCVLVLNFLNGLLPASLILAIKYLVNmvqNLYIQGYKdNYFYDILPFFIFFSVVTLLTSATGSI 105
Cdd:TIGR02203 1 TFRRLWSYVRPYkagLVLAGVAMILVAATESTLAALLKPLLD---DGFGGRDR-SVLWWVPLVVIGLAVLRGICSFVSTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 106 LEThkQLYRNLLSNkINVKLIEKAKRLPYASFENPEVYNKLQRARQDSTYKPFAIFEELMGIVKGAITLISISIILMVWN 185
Cdd:TIGR02203 77 LLS--WVSNKVVRD-IRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 186 WEFTLILILLPLISAWSIVNVGKEIFLVSHKR----------AEETRKQFyyyylmttditvKEVKIFGLGSLLLRNYSD 255
Cdd:TIGR02203 154 WQLTLIVVVMLPVLSILMRRVSKRLRRISKEIqnsmgqvttvAEETLQGY------------RVVKLFGGQAYETRRFDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 256 LfskfynqDRHLLLKKMRI-------DLSFQLISVIFVIFVQFMIVKDTIQGLIAIGSLIAYFQAVNTTQKTSNELMYmV 328
Cdd:TIGR02203 222 V-------SNRNRRLAMKMtsagsisSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTN-V 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 329 FNMHQNNLYMTQ-LFSFLNVPESTDKPNVSEEKTlenvssteEG-IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVG 406
Cdd:TIGR02203 294 NAPMQRGLAAAEsLFTLLDSPPEKDTGTRAIERA--------RGdVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 407 SNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDFVRYELDVKENIGYG---DYKRSNhlvaIQA 483
Cdd:TIGR02203 366 RSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGrteQADRAE----IER 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 484 AAKRSGALTMIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQK 563
Cdd:TIGR02203 442 ALAAAYAQDFVDKLPLGLDTPIGE---NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQG 518
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 502825101 564 SMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYARLFNLQ 613
Cdd:TIGR02203 519 RTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
372-613 |
6.85e-75 |
|
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: 239.36 E-value: 6.85e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQ-ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRIS 450
Cdd:cd03249 1 IEFKNVSFRYPSRpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 451 AIFQDFVRYELDVKENIGYGDYKRsnHLVAIQAAAKRSGALTMIDSLPDKMDTQLGktfANGIQLSGGQWQRIAIARAYM 530
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVG---ERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYARLF 610
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
...
gi 502825101 611 NLQ 613
Cdd:cd03249 236 KAQ 238
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
340-604 |
5.43e-74 |
|
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: 247.36 E-value: 5.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 340 QLFSFLNVPESTDKPNVSEEKTLENVSsteegIQFLNVSFKYPGQENyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLL 419
Cdd:COG4988 310 KIFALLDAPEPAAPAGTAPLPAAGPPS-----IELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 420 TRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDFVRYELDVKENIGYGDYKRSNHlvAIQAAAKRSGALTMIDSLPD 499
Cdd:COG4988 384 LGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDE--ELEAALEAAGLDEFVAALPD 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 500 KMDTQLGktfANGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYA 579
Cdd:COG4988 462 GLDTPLG---EGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA 538
|
250 260
....*....|....*....|....*
gi 502825101 580 DRIIVLDKGEVAEYGTHVELLDTNG 604
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
372-589 |
3.64e-72 |
|
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: 229.58 E-value: 3.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIgygdykrsnhlvaiqaaakrsgaltmidslpdkmdtqlgktfangiqLSGGQWQRIAIARAYMR 531
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGE 589
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
372-610 |
1.22e-71 |
|
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: 230.58 E-value: 1.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIGYGdyKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMR 531
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYG--RPGATREEVEEAARAANAHEFIMELPEGYDTVIGE---RGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYARLF 610
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
372-613 |
9.95e-68 |
|
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: 220.56 E-value: 9.95e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:cd03253 1 IEFENVTFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIGYGDYKRSNhlVAIQAAAKRSGALTMIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMR 531
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATD--EEVIEAAKAAQIHDKIMRFPDGYDTIVGE---RGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYARLFN 611
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
..
gi 502825101 612 LQ 613
Cdd:cd03253 235 AQ 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
352-612 |
2.31e-67 |
|
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: 230.04 E-value: 2.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 352 DKPNVSEEKTlENVSSTEEGIQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIIL 431
Cdd:COG4987 315 APPAVTEPAE-PAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 432 LNGKRIEDYQPQDWQDRISAIFQD---F---VRyeldvkENIgygdykrsnhLVA--------IQAAAKRSGALTMIDSL 497
Cdd:COG4987 394 LGGVDLRDLDEDDLRRRIAVVPQRphlFdttLR------ENL----------RLArpdatdeeLWAALERVGLGDWLAAL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 498 PDKMDTQLGktfANGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVK 577
Cdd:COG4987 458 PDGLDTWLG---EGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE 534
|
250 260 270
....*....|....*....|....*....|....*
gi 502825101 578 YADRIIVLDKGEVAEYGTHVELLDTNGIYARLFNL 612
Cdd:COG4987 535 RMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
372-613 |
4.73e-66 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 226.82 E-value: 4.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIGY---GDYKRSNhlvaIQAAAKRSGALTMIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARA 528
Cdd:PRK11176 422 VSQNVHLFNDTIANNIAYartEQYSREQ----IEEAARMAYAMDFINKMDNGLDTVIGE---NGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 529 YMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYAR 608
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
....*
gi 502825101 609 LFNLQ 613
Cdd:PRK11176 575 LHKMQ 579
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
338-613 |
5.66e-65 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 223.81 E-value: 5.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 338 MTQLFSFLNVpestdKPNVSEEKTLENVSSTEEG-IQFLNVSFKYPGQENY-TLKNVNFHIKPGETLALVGSNGSGKSTI 415
Cdd:TIGR02204 308 AERLIELLQA-----EPDIKAPAHPKTLPVPLRGeIEFEQVNFAYPARPDQpALDGLNLTVRPGETVALVGPSGAGKSTL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 416 VKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDFVRYELDVKENIGYGDYKRSNHlvAIQAAAKRSGALTMID 495
Cdd:TIGR02204 383 FQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDE--EVEAAARAAHAHEFIS 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 496 SLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYST 575
Cdd:TIGR02204 461 ALPEGYDTYLGE---RGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLAT 537
|
250 260 270
....*....|....*....|....*....|....*...
gi 502825101 576 VKYADRIIVLDKGEVAEYGTHVELLDTNGIYARLFNLQ 613
Cdd:TIGR02204 538 VLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
372-604 |
1.89e-64 |
|
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: 211.70 E-value: 1.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYpGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:cd03254 3 IEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIGYGDYKRSNHLVAIqaAAKRSGALTMIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMR 531
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATDEEVIE--AAKEAGAHDFIMKLPNGYDTVLGE---NGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNG 604
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
335-625 |
2.80e-64 |
|
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: 222.39 E-value: 2.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 335 NLYMTQLF---SFLNV----------------------PESTDKPNVSEEKTlenvssTEEGIQFLNVSFKY-PGQEnyT 388
Cdd:COG5265 302 NAYLIQLYiplNFLGFvyreirqaladmermfdlldqpPEVADAPDAPPLVV------GGGEVRFENVSFGYdPERP--I 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQ-----------PQDwqdriSAIFQDFV 457
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTqaslraaigivPQD-----TVLFNDTI 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 458 RYeldvkeNIGYGDYKRSNHlvAIQAAAKRSGALTMIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMRRASLYI 537
Cdd:COG5265 449 AY------NIAYGRPDASEE--EVEAAARAAQIHDFIESLPDGYDTRVGE---RGLKLSGGEKQRVAIARTLLKNPPILI 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 538 LDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYARLFNLQAKSY 617
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEE 597
|
....*...
gi 502825101 618 IEASATQA 625
Cdd:COG5265 598 EAEEALAA 605
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
372-613 |
1.61e-63 |
|
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: 209.65 E-value: 1.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIGYGDYKRSNHlvAIQAAAKRSGALTMIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMR 531
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSME--RVIEAAKLAGAHDFISELPEGYDTIVGE---QGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYARLFN 611
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
..
gi 502825101 612 LQ 613
Cdd:cd03252 236 LQ 237
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
372-590 |
3.59e-56 |
|
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: 189.34 E-value: 3.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIGYGDYKRSNhlVAIQAAAKRSGALTMIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMR 531
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADD--ERILRAAELAGVTDFVNKHPNGLDLQIGE---RGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQE-IAQKSMgLFISHRYSTVKYADRIIVLDKGEV 590
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQlLGDKTL-IIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
298-609 |
4.51e-56 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 202.26 E-value: 4.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 298 IQGLIAIGSLIAYFqaVNTTQKTSN--ELMYMVFNMHQNNLYMTQLFSFLNvpestDKPNVSEEKTLenVSSTEEG-IQF 374
Cdd:TIGR00958 411 LTGKVSSGNLVSFL--LYQEQLGEAvrVLSYVYSGMMQAVGASEKVFEYLD-----RKPNIPLTGTL--APLNLEGlIEF 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 375 LNVSFKYPGQ-ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIF 453
Cdd:TIGR00958 482 QDVSFSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVG 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 454 QDFVRYELDVKENIGYGdyKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTQLGKTfanGIQLSGGQWQRIAIARAYMRRA 533
Cdd:TIGR00958 562 QEPVLFSGSVRENIAYG--LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEK---GSQLSGGQKQRIAIARALVRKP 636
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 534 SLYILDEPTAALDpAAEEEVFQDFQEIAQKSMgLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYARL 609
Cdd:TIGR00958 637 RVLILDEATSALD-AECEQLLQESRSRASRTV-LLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
281-627 |
4.60e-55 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 197.11 E-value: 4.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 281 ISVIFVI---FVQfmivkdtiQGLIAIGSLIAYfqaVNTTQKTSNELMYMV-F--NMHQNNLYMTQLFSFLN-VPESTDK 353
Cdd:PRK13657 254 MLAILVLgaaLVQ--------KGQLRVGEVVAF---VGFATLLIGRLDQVVaFinQVFMAAPKLEEFFEVEDaVPDVRDP 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 354 PNVSEektLENVSSTeegIQFLNVSFKYPGQENyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLN 433
Cdd:PRK13657 323 PGAID---LGRVKGA---VEFDDVSFSYDNSRQ-GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILID 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 434 GKRIEDYQPQDWQDRISAIFQDFVRYELDVKENIGYGdyKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTQLGKtfaNGI 513
Cdd:PRK13657 396 GTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVG--RPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGE---RGR 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 514 QLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEY 593
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVES 550
|
330 340 350
....*....|....*....|....*....|....*...
gi 502825101 594 GTHVELLDTNGIYARL----FNLQAKSYIEASATQASS 627
Cdd:PRK13657 551 GSFDELVARGGRFAALlraqGMLQEDERRKQPAAEGAN 588
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
372-590 |
6.94e-54 |
|
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: 183.44 E-value: 6.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENY-TLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRIS 450
Cdd:cd03248 12 VKFQNVTFAYPTRPDTlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 451 AIFQDFVRYELDVKENIGYGdyKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYM 530
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYG--LQSCSFECVKEAAQKAHAHSFISELASGYDTEVGE---KGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEV 590
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
279-601 |
2.00e-51 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 188.54 E-value: 2.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 279 QLISVIFVIFVQFMIvkdtIQGLIAIGSLIAyfqavnTTQKTSNELMYMV-FNM-----HQNNLYMTQLFSFLNVPesTD 352
Cdd:TIGR03375 380 QLVSVAIVVVGVYLI----SDGELTMGGLIA------CVMLSGRALAPLGqLAGlltryQQAKTALQSLDELMQLP--VE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 353 KPnvsEEKTLENVSSTEEGIQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILL 432
Cdd:TIGR03375 448 RP---EGTRFLHRPRLQGEIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLL 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 433 NGKRIEDYQPQDWQDRISAIFQDFVRYELDVKENIGYGDYKRSNHlvAIQAAAKRSGALTMIDSLPDKMDTQLGKtfaNG 512
Cdd:TIGR03375 525 DGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYADDE--EILRAAELAGVTEFVRRHPDGLDMQIGE---RG 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 513 IQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAE 592
Cdd:TIGR03375 600 RSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVA 679
|
....*....
gi 502825101 593 YGTHVELLD 601
Cdd:TIGR03375 680 DGPKDQVLE 688
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
279-613 |
2.09e-51 |
|
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: 188.80 E-value: 2.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 279 QLISVIFVIFVQFMIVKDTIQGLIAIGSLIAyfqavnttqktsnelmymvFNM-----HQNNLYMTQLF--------SFL 345
Cdd:TIGR01846 369 ELIQKLTFAILLWFGAHLVIGGALSPGQLVA-------------------FNMlagrvTQPVLRLAQLWqdfqqtgiALE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 346 NVPESTDKPNVSEEKTLENVSSTEEGIQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTD 425
Cdd:TIGR01846 430 RLGDILNSPTEPRSAGLAALPELRGAITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTP 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 426 YEGIILLNGKRIEDYQPQDWQDRISAIFQDFVRYELDVKENIGYGDYKRSNHLVAiqAAAKRSGALTMIDSLPDKMDTQL 505
Cdd:TIGR01846 510 QHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVI--HAAKLAGAHDFISELPQGYNTEV 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 506 GKtfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVL 585
Cdd:TIGR01846 588 GE---KGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVL 664
|
330 340
....*....|....*....|....*...
gi 502825101 586 DKGEVAEYGTHVELLDTNGIYARLFNLQ 613
Cdd:TIGR01846 665 EKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
372-585 |
3.85e-50 |
|
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: 182.10 E-value: 3.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIGYGDYKRSNHlvAIQAAAKRSGALTMIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMR 531
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARPDASDA--EIREALERAGLDEFVAALPQGLDTPIGE---GGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVL 585
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
372-595 |
1.71e-48 |
|
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: 168.83 E-value: 1.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIG----YGDykrsnhlVAIQAAAKRSGALTMIDSLPDKMDTQLGktfANGIQLSGGQWQRIAIAR 527
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDpfgeYSD-------EELWQALERVGLKEFVESLPGGLDTVVE---EGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 528 AYMRRASLYILDEPTAALDPAAEEEVFQDFQE-IAQKSMgLFISHRYSTVKYADRIIVLDKGEVAEYGT 595
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREaFKDCTV-LTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
373-589 |
1.22e-45 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 160.71 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 373 QFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAI 452
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 453 FQD----FVryELDVKENIGYGdyKRSNHLVAIQAAAKRSGALTMIDsLPDKMDTQLgktfangIQLSGGQWQRIAIARA 528
Cdd:cd03225 81 FQNpddqFF--GPTVEEEVAFG--LENLGLPEEEIEERVEEALELVG-LEGLRDRSP-------FTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 529 YMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMG-LFISHRYSTVK-YADRIIVLDKGE 589
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTiIIVTHDLDLLLeLADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
372-600 |
7.47e-45 |
|
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: 159.42 E-value: 7.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGqENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQD----FVryELDVKENIGYG----DYKRSNHLVAIQAAAKRSGALTMIDSLPDkmdtqlgktfangiQLSGGQWQRI 523
Cdd:COG1122 80 VFQNpddqLF--APTVEEDVAFGpenlGLPREEIRERVEEALELVGLEHLADRPPH--------------ELSGGQKQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 524 AIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMG-LFISHRYSTV-KYADRIIVLDKGEVAEYGTHVELL 600
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTvIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVF 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
363-609 |
3.97e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 166.15 E-value: 3.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 363 ENVSSTEEGIQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQP 442
Cdd:PRK11160 330 STAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 443 QDWQDRISAIFQdfvRYELdvkenigYGDYKRSNHLVAIQAA--AKRSGALTMI--DSL---PDKMDTQLGKtfaNGIQL 515
Cdd:PRK11160 410 AALRQAISVVSQ---RVHL-------FSATLRDNLLLAAPNAsdEALIEVLQQVglEKLledDKGLNAWLGE---GGRQL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 516 SGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQ-KSMgLFISHRYSTVKYADRIIVLDKGEVAEYG 594
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQnKTV-LMITHRLTGLEQFDRICVMDNGQIIEQG 555
|
250
....*....|....*
gi 502825101 595 THVELLDTNGIYARL 609
Cdd:PRK11160 556 THQELLAQQGRYYQL 570
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
372-601 |
1.50e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.99 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENytLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDyQPQDWQDRISA 451
Cdd:COG1131 1 IEVRGLTKRYGDKTA--LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYE-LDVKENIGYgdYKRSNHLVAIQAAAKRSGALTMIDsLPDKMDTQLGKtfangiqLSGGQWQRIAIARAYM 530
Cdd:COG1131 78 VPQEPALYPdLTVRENLRF--FARLYGLPRKEARERIDELLELFG-LTDAADRKVGT-------LSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS-HRYSTV-KYADRIIVLDKGEVAEYGTHVELLD 601
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
372-627 |
2.55e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 162.77 E-value: 2.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLY---TDYEGIILLNGKRIEDYQPQDWQDR 448
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 ISAIFQDF------VRYELDVKENIGYGDYKRSNHLVAIQAAAKRSGALTMIDSLPDkmdtqlgktfangiQLSGGQWQR 522
Cdd:COG1123 85 IGMVFQDPmtqlnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPH--------------QLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 523 IAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKS-MG-LFISHRYSTV-KYADRIIVLDKGEVAEYGTHVEL 599
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgTTvLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260
....*....|....*....|....*...
gi 502825101 600 LDTNGIYARLFNLQAKSYIEASATQASS 627
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAE 258
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
389-543 |
5.48e-43 |
|
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: 151.26 E-value: 5.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQD-FVRYELDVKENI 467
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDpQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502825101 468 GYGDYkrsnhLVAIQAAAKRSGALTMID--SLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPTA 543
Cdd:pfam00005 81 RLGLL-----LKGLSKREKDARAEEALEklGLGDLADRPVGE---RPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
376-595 |
1.30e-42 |
|
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: 161.84 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDwqdrisaiFQD 455
Cdd:COG4618 335 NLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE--------LGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 456 FVRY-----EL---DVKENIG-YGDYKRSnhlvAIQAAAKRSGALTMIDSLPDKMDTQLGktfANGIQLSGGQWQRIAIA 526
Cdd:COG4618 407 HIGYlpqdvELfdgTIAENIArFGDADPE----KVVAAAKLAGVHEMILRLPDGYDTRIG---EGGARLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502825101 527 RAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaqKSMG---LFISHRYSTVKYADRIIVLDKGEVAEYGT 595
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL--KARGatvVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
376-601 |
1.30e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 160.84 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYP---GQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQD---RI 449
Cdd:COG1123 265 NLSKRYPvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRElrrRV 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 450 SAIFQD-----FVRyeLDVKENIGYGdyKRSNHLVAIQAAAKRsgALTMIDSLpdkmdtQLGKTFAN--GIQLSGGQWQR 522
Cdd:COG1123 345 QMVFQDpysslNPR--MTVGDIIAEP--LRLHGLLSRAERRER--VAELLERV------GLPPDLADryPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 523 IAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMG---LFISHRYSTVKY-ADRIIVLDKGEVAEYGTHVE 598
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDL-QRELGltyLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEE 491
|
...
gi 502825101 599 LLD 601
Cdd:COG1123 492 VFA 494
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
376-589 |
1.03e-41 |
|
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: 148.16 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQENytLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQd 455
Cdd:cd00267 4 NLSFRYGGRTA--LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 456 fvryeldvkenigygdykrsnhlvaiqaaakrsgaltmidslpdkmdtqlgktfangiqLSGGQWQRIAIARAYMRRASL 535
Cdd:cd00267 81 -----------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 536 YILDEPTAALDPAAEEEVFQDFQEIAQK-SMGLFISHRYSTV-KYADRIIVLDKGE 589
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
376-600 |
1.33e-41 |
|
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: 158.67 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQD 455
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 456 FVRYELDVKENIG-YGDYKRSNhlvAIQAAAKRSGALTMIDSLPDKMDTQLGktfANGIQLSGGQWQRIAIARAYMRRAS 534
Cdd:TIGR01842 401 VELFPGTVAENIArFGENADPE---KIIEAAKLAGVHELILRLPDGYDTVIG---PGGATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 535 LYILDEPTAALDPAAEEEVFQDFQEI-AQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELL 600
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
375-594 |
1.77e-41 |
|
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: 149.96 E-value: 1.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 375 LNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDR---ISA 451
Cdd:cd03257 7 LSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRrkeIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYeLD----VKENIG-----YGDYKRSNHLVAIQAAAKRSGAL--TMIDSLPDkmdtqlgktfangiQLSGGQW 520
Cdd:cd03257 87 VFQDPMSS-LNprmtIGEQIAeplriHGKLSKKEARKEAVLLLLVGVGLpeEVLNRYPH--------------ELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502825101 521 QRIAIARAYMRRASLYILDEPTAALDPAAEEEV---FQDFQEIAQKSMgLFISHRYSTVKY-ADRIIVLDKGEVAEYG 594
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQIldlLKKLQEELGLTL-LFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
372-601 |
4.65e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.47 E-value: 4.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIED------YQPQ-- 443
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRarrrigYVPQra 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 444 --DWQDRISAifQDFVRYELDVKenIGYGDYKRSNHLVAIQAAAKRSGALtmidslpDKMDTQLGktfangiQLSGGQWQ 521
Cdd:COG1121 85 evDWDFPITV--RDVVLMGRYGR--RGLFRRPSRADREAVDEALERVGLE-------DLADRPIG-------ELSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 522 RIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMG-LFISHRYSTV-KYADRIIVLDKGEVAE------- 592
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTiLVVTHDLGAVrEYFDRVLLLNRGLVAHgppeevl 226
|
250
....*....|....*..
gi 502825101 593 --------YGTHVELLD 601
Cdd:COG1121 227 tpenlsraYGGPVALLA 243
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
341-609 |
6.16e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 157.31 E-value: 6.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 341 LFSFLNVPESTDKpnvSEEKTLENVSSTEEGIQFLNVsFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLt 420
Cdd:PRK11174 324 LVTFLETPLAHPQ---QGEKELASNDPVTIEAEDLEI-LSPDGKT--LAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 421 rL-YTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDFVRYELDVKENIGYGDYKRSNHlvAIQAAAKRSGALTMIDSLPD 499
Cdd:PRK11174 397 -LgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDE--QLQQALENAWVSEFLPLLPQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 500 KMDTQLGKtfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYA 579
Cdd:PRK11174 474 GLDTPIGD---QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW 550
|
250 260 270
....*....|....*....|....*....|
gi 502825101 580 DRIIVLDKGEVAEYGTHVELLDTNGIYARL 609
Cdd:PRK11174 551 DQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
372-605 |
1.72e-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: 148.73 E-value: 1.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQpQDWQ--DRI 449
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEE-NLWEirKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 450 SAIFQD----FVR--YELDVK---ENIGygdYKRSNHLVAIQAAAKRSGALTMIDSLPdkmdtqlgktfangIQLSGGQW 520
Cdd:TIGR04520 80 GMVFQNpdnqFVGatVEDDVAfglENLG---VPREEMRKRVDEALKLVGMEDFRDREP--------------HLLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 521 QRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGL---FISHRYSTVKYADRIIVLDKGEVAEYGT-- 595
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKL-NKEEGItviSITHDMEEAVLADRVIVMNKGKIVAEGTpr 221
|
250
....*....|....
gi 502825101 596 ----HVELLDTNGI 605
Cdd:TIGR04520 222 eifsQVELLKEIGL 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
376-614 |
4.10e-40 |
|
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: 147.11 E-value: 4.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQD 455
Cdd:COG1120 6 NLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 456 F-VRYELDVKENIGYGdykRSNHLVAIQ-------AAAKRSGALTMIDSLPDK-MDTqlgktfangiqLSGGQWQRIAIA 526
Cdd:COG1120 84 PpAPFGLTVRELVALG---RYPHLGLFGrpsaedrEAVEEALERTGLEHLADRpVDE-----------LSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 527 RAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSmG---LFISH------RystvkYADRIIVLDKGEVAEYGTHV 597
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARER-GrtvVMVLHdlnlaaR-----YADRLVLLKDGRIVAQGPPE 223
|
250
....*....|....*..
gi 502825101 598 ELLdTNGIYARLFNLQA 614
Cdd:COG1120 224 EVL-TPELLEEVYGVEA 239
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
376-591 |
7.66e-40 |
|
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: 144.98 E-value: 7.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIED------YQPQ----DW 445
Cdd:cd03235 4 DLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKerkrigYVPQrrsiDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 446 QDRISaifqdfvryeldVKENIGYGDYKRSNHLVAIQAAAKRSG--ALTMIDsLPDKMDTQLGktfangiQLSGGQWQRI 523
Cdd:cd03235 82 DFPIS------------VRDVVLMGLYGHKGLFRRLSKADKAKVdeALERVG-LSELADRQIG-------ELSGGQQQRV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 524 AIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMG-LFISHRYSTV-KYADRIIVLDKGEVA 591
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTiLVVTHDLGLVlEYFDRVLLLNRTVVA 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
372-590 |
8.54e-39 |
|
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: 142.24 E-value: 8.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYT--LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDW---- 445
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 446 QDRISAIFQDF--VRYeLDVKENI-----GYGDYKRSNHLVAIQAaakrsgaLTMIDsLPDKMDTqlgktFANgiQLSGG 518
Cdd:cd03255 81 RRHIGFVFQSFnlLPD-LTALENVelpllLAGVPKKERRERAEEL-------LERVG-LGDRLNH-----YPS--ELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 519 QWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKsMG---LFISHRYSTVKYADRIIVLDKGEV 590
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKE-AGttiVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
372-590 |
1.82e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 142.50 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQP---QDWQDR 448
Cdd:COG3638 3 LELRNLSKRYPGGTP-ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 ISAIFQDF--VRyELDVKENI-----GYGDYKRSnhLVAIQAAAKRSGALTMIDS--LPDKMDTQLGktfangiQLSGGQ 519
Cdd:COG3638 82 IGMIFQQFnlVP-RLSVLTNVlagrlGRTSTWRS--LLGLFPPEDRERALEALERvgLADKAYQRAD-------QLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 520 WQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQkSMGLfishrysTV-----------KYADRIIVLDKG 588
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAR-EDGI-------TVvvnlhqvdlarRYADRIIGLRDG 223
|
..
gi 502825101 589 EV 590
Cdd:COG3638 224 RV 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
372-594 |
2.41e-38 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 139.76 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQpqdwqdrisa 451
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 ifqdfvryeldvkenigygdykrsnhlvaiqaaAKRSGALTMIDSLPDKMDTQLGKTFanGIQLSGGQWQRIAIARAYMR 531
Cdd:cd03247 71 ---------------------------------KALSSLISVLNQRPYLFDTTLRNNL--GRRFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYG 594
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
372-594 |
2.73e-38 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 140.73 E-value: 2.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQenYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQdwQDRISA 451
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRY-ELDVKENIGYGDYKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTQLgktfangiqlSGGQWQRIAIARAYM 530
Cdd:cd03259 77 VFQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHEL----------SGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMG---LFISH-RYSTVKYADRIIVLDKGEVAEYG 594
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKEL-QRELGittIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
372-601 |
4.07e-38 |
|
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: 141.17 E-value: 4.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQP---QDWQDR 448
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 ISAIFQDF-VRYELDVKENIGYGdykRSNHLVAIQAAAkrsgaltmidSLPDKMDTQ-----------LGKTFANGIQLS 516
Cdd:cd03256 80 IGMIFQQFnLIERLSVLENVLSG---RLGRRSTWRSLF----------GLFPKEEKQralaalervglLDKAYQRADQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 517 GGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQ-KSMGLFIS-HRYSTVK-YADRIIVLDKGEVAEY 593
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReEGITVIVSlHQVDLAReYADRIVGLKDGRIVFD 226
|
....*...
gi 502825101 594 GTHVELLD 601
Cdd:cd03256 227 GPPAELTD 234
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
372-590 |
5.17e-38 |
|
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: 138.50 E-value: 5.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIgygdykrsnhlvaiqaaakrsgaltmidslpdkmdtqlgktfangiqLSGGQWQRIAIARAYMR 531
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQEI-AQKSMGLFISHRYSTVKYADRIIVLDKGEV 590
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
368-595 |
6.05e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.08 E-value: 6.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 368 TEEGIQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQD 447
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 448 RISAIFQD----FV--RYELDVK---ENIGygdYKRSNHLVAIQAAAKRSGALTMIDSLPDKmdtqlgktfangiqLSGG 518
Cdd:PRK13635 82 QVGMVFQNpdnqFVgaTVQDDVAfglENIG---VPREEMVERVDQALRQVGMEDFLNREPHR--------------LSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 519 QWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMG--LFISHRYSTVKYADRIIVLDKGEVAEYGT 595
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGItvLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
375-621 |
3.72e-37 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 138.78 E-value: 3.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 375 LNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQ 454
Cdd:COG1124 7 LSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 455 DFV-----RYELD--VKE--NIgygdYKRSNHLVAIQAAAKRSGaltmidslpdkmdtqLGKTFAN--GIQLSGGQWQRI 523
Cdd:COG1124 87 DPYaslhpRHTVDriLAEplRI----HGLPDREERIAELLEQVG---------------LPPSFLDryPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 524 AIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEI-AQKSMG-LFISHRYSTVKY-ADRIIVLDKGEVaeygthVELL 600
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTyLFVSHDLAVVAHlCDRVAVMQNGRI------VEEL 221
|
250 260
....*....|....*....|.
gi 502825101 601 DTNGIYARLFNLQAKSYIEAS 621
Cdd:COG1124 222 TVADLLAGPKHPYTRELLAAS 242
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
372-592 |
3.73e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 137.87 E-value: 3.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYT--LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDW---- 445
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 446 QDRISAIFQDFvrY---ELDVKENIGYG-DYKRSNHLVAIQAAAKrsgALTMIDsLPDKMDTqlgktFANgiQLSGGQWQ 521
Cdd:COG1136 85 RRHIGFVFQFF--NllpELTALENVALPlLLAGVSRKERRERARE---LLERVG-LGDRLDH-----RPS--QLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502825101 522 RIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAqKSMG---LFISHRYSTVKYADRIIVLDKGEVAE 592
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELN-RELGttiVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
372-590 |
4.89e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 137.25 E-value: 4.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQenYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:COG4619 1 LELEGLSFRVGGK--PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIGYGDYKRsnHLVAIQAAAKRsgALTMIDsLPDKMdtqLGKTFANgiqLSGGQWQRIAIARAYMR 531
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQLR--ERKFDRERALE--LLERLG-LPPDI---LDKPVER---LSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQE-IAQKSMG-LFISH------RystvkYADRIIVLDKGEV 590
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAvLWVSHdpeqieR-----VADRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
372-601 |
6.75e-37 |
|
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: 137.68 E-value: 6.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYpgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEdYQPQDWQDRISA 451
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYE-LDVKENIGYgdYKRSNHLVAIQAAAKRSGALTMIDsLPDKMDTQLGKtfangiqLSGGQWQRIAIARAYM 530
Cdd:COG4555 79 LPDERGLYDrLTVRENIRY--FAELYGLFDEELKKRIEELIELLG-LEEFLDRRVGE-------LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIA-QKSMGLFISHRYSTV-KYADRIIVLDKGEVAEYGTHVELLD 601
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
378-613 |
1.28e-36 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 144.47 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 378 SFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDFV 457
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 458 RYELDVKENIGYG--DYKRSNhlvaIQAAAKRSGALTMIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMRRASL 535
Cdd:PRK10789 400 LFSDTVANNIALGrpDATQQE----IEHVARLASVHDDILRLPQGYDTEVGE---RGVMLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502825101 536 YILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYARLFNLQ 613
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
372-589 |
2.85e-36 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 133.85 E-value: 2.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQenYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDY--QPQDWQDRI 449
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 450 SAIFQDFVRY-ELDVKENIGYGdykrsnhlvaiqaaakrsgaltmidslpdkmdtqlgktfangiqLSGGQWQRIAIARA 528
Cdd:cd03229 79 GMVFQDFALFpHLTVLENIALG--------------------------------------------LSGGQQQRVALARA 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 529 YMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMG---LFISHRYSTV-KYADRIIVLDKGE 589
Cdd:cd03229 115 LAMDPDVLLLDEPTSALDPITRREVRALLKSL-QAQLGitvVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
372-592 |
1.19e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 133.64 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGqENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQD---WQDR 448
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 ISAIFQDFvR--YELDVKENIGYGdykrsnhLVAI----QAAAKR-SGALTMIDsLPDKMDtqlgktfANGIQLSGGQWQ 521
Cdd:COG2884 81 IGVVFQDF-RllPDRTVYENVALP-------LRVTgksrKEIRRRvREVLDLVG-LSDKAK-------ALPHELSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 522 RIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQksMG---LFISHRYSTV-KYADRIIVLDKGEVAE 592
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINR--RGttvLIATHDLELVdRMPKRVLELEDGRLVR 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
389-585 |
1.58e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.15 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDR-ISAIFQDF--VRyELDVKE 465
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELnlVP-NLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 466 NIGYGDYKRSNHLV---AIQAAAKRsgALTMIDsLPDKMDTQLGktfangiQLSGGQWQRIAIARAYMRRASLYILDEPT 542
Cdd:COG1129 99 NIFLGREPRRGGLIdwrAMRRRARE--LLARLG-LDIDPDTPVG-------DLSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502825101 543 AALDpaaEEEVFQDFQEIAQ-KSMG---LFISHRYSTVKY-ADRIIVL 585
Cdd:COG1129 169 ASLT---EREVERLFRIIRRlKAQGvaiIYISHRLDEVFEiADRVTVL 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
372-591 |
1.87e-35 |
|
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: 131.01 E-value: 1.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQD-WQDRIS 450
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 451 AIFQdfvryeldvkenigygdykrsnhlvaiqaaakrsgaltmidslpdkmdtqlgktfangiqLSGGQWQRIAIARAYM 530
Cdd:cd03216 79 MVYQ------------------------------------------------------------LSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMG-LFISHRYSTV-KYADRIIVLDKGEVA 591
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAvIFISHRLDEVfEIADRVTVLRDGRVV 161
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
376-594 |
5.96e-35 |
|
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: 130.25 E-value: 5.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQd 455
Cdd:cd03214 4 NLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 456 fvryeldvkenigygdykrsnhlvaiqaAAKRSGALTMIDslpdkmdtqlgKTFAngiQLSGGQWQRIAIARAYMRRASL 535
Cdd:cd03214 81 ----------------------------ALELLGLAHLAD-----------RPFN---ELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 536 YILDEPTAALDPAAEEEVFQDFQEIAqKSMG---LFISHRYS-TVKYADRIIVLDKGEVAEYG 594
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLA-RERGktvVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
271-611 |
1.12e-34 |
|
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: 139.87 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 271 KMRIDLSFQLISVIFVIFV---QFMIVKDTIQGLIAIGSLIAYF-----QAVNTTQKTSNElmyMVFNMHQNNLYMtqlf 342
Cdd:TIGR01193 381 QQAIKAVTKLILNVVILWTgayLVMRGKLTLGQLITFNALLSYFltpleNIINLQPKLQAA---RVANNRLNEVYL---- 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 343 sflnVPESTDKPNVSEEKTLENVSsteegIQFLNVSFKYpGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRL 422
Cdd:TIGR01193 454 ----VDSEFINKKKRTELNNLNGD-----IVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 423 YTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDFVRYELDVKENIGYGDyKRSNHLVAIQAAAKRSGALTMIDSLPDKMD 502
Cdd:TIGR01193 524 FQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGA-KENVSQDEIWAACEIAEIKDDIENMPLGYQ 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 503 TQLGKtfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMgLFISHRYSTVKYADRI 582
Cdd:TIGR01193 603 TELSE---EGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTI-IFVAHRLSVAKQSDKI 678
|
330 340
....*....|....*....|....*....
gi 502825101 583 IVLDKGEVAEYGTHVELLDTNGIYARLFN 611
Cdd:TIGR01193 679 IVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
372-601 |
1.40e-34 |
|
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: 131.27 E-value: 1.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQD---WQDR 448
Cdd:TIGR02315 2 LEVENLSKVYPNGKQ-ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrkLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 ISAIFQDFVRYE-LDVKENI-------------GYGDYKRSNHLVAIQAAaKRSGALTMIDSLPDkmdtqlgktfangiQ 514
Cdd:TIGR02315 81 IGMIFQHYNLIErLTVLENVlhgrlgykptwrsLLGRFSEEDKERALSAL-ERVGLADKAYQRAD--------------Q 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 515 LSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKsMGLFIS---HRYSTVK-YADRIIVLDKGEV 590
Cdd:TIGR02315 146 LSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKE-DGITVIinlHQVDLAKkYADRIVGLKAGEI 224
|
250
....*....|.
gi 502825101 591 AEYGTHVELLD 601
Cdd:TIGR02315 225 VFDGAPSELDD 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
372-590 |
2.15e-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: 2.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDyQPQDWQDRISA 451
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYE-LDVKENIgygdykrsnhlvaiqaaakrsgaltmidslpdkmdtqlgktfangiQLSGGQWQRIAIARAYM 530
Cdd:cd03230 78 LPEEPSLYEnLTVRENL----------------------------------------------KLSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMG-LFISHRYSTV-KYADRIIVLDKGEV 590
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGKTiLLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
372-600 |
4.84e-34 |
|
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: 129.62 E-value: 4.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYT--LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQP---QDWQ 446
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 447 DRISAIFQDF-VRYELDVKENIGY----------GDYKRSNHLvaiqaaakrsgaLTMIDsLPDKMDtqlgktfANGIQL 515
Cdd:cd03258 82 RRIGMIFQHFnLLSSRTVFENVALpleiagvpkaEIEERVLEL------------LELVG-LEDKAD-------AYPAQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 516 SGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGL---FISHRYSTVK-YADRIIVLDKGEVA 591
Cdd:cd03258 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDI-NRELGLtivLITHEMEVVKrICDRVAVMEKGEVV 220
|
....*....
gi 502825101 592 EYGTHVELL 600
Cdd:cd03258 221 EEGTVEEVF 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
389-601 |
6.63e-34 |
|
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: 128.71 E-value: 6.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDW---------QDRisAIFQdfvry 459
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaragigyvpEGR--RIFP----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 460 ELDVKENIGYGDYKRSNHlvaiQAAAKRSGALTMIDSLPDKMDtQLGKTfangiqLSGGQWQRIAIARAYMRRASLYILD 539
Cdd:cd03224 89 ELTVEENLLLGAYARRRA----KRKARLERVYELFPRLKERRK-QLAGT------LSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502825101 540 EPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTV--KYADRIIVLDKGEVAEYGTHVELLD 601
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFalEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
372-594 |
2.37e-33 |
|
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: 127.30 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYpgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDY-----EGIILLNGKRI--EDYQPQD 444
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIydLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 445 WQDRISAIFQDFVRYELDVKENIGYG----DYKRSNHLVAIQAAAKRSGALTmiDSLPDKmdtqlgktfANGIQLSGGQW 520
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrlhGIKLKEELDERVEEALRKAALW--DEVKDR---------LHALGLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 521 QRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVK-YADRIIVLDKGEVAEYG 594
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFG 222
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
372-627 |
2.86e-33 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 134.85 E-value: 2.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYpGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:PRK10790 341 IDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIGYGDYKRSNH----LVAIQAAakrsgalTMIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIAR 527
Cdd:PRK10790 420 VQQDPVVLADTFLANVTLGRDISEEQvwqaLETVQLA-------ELARSLPDGLYTPLGE---QGNNLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 528 AYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYA 607
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYW 569
|
250 260
....*....|....*....|.
gi 502825101 608 RLFNLQ-AKSYIEASATQASS 627
Cdd:PRK10790 570 QMYQLQlAGEELAASVREEES 590
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
372-600 |
4.92e-33 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 127.03 E-value: 4.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:cd03295 1 IEFENVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRY-ELDVKENIGygdykrsnhLV---------AIQAAAKRsgALTMIDsLPDkmdtqlgKTFANGI--QLSGGQ 519
Cdd:cd03295 80 VIQQIGLFpHMTVEENIA---------LVpkllkwpkeKIRERADE--LLALVG-LDP-------AEFADRYphELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 520 WQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMG---LFISHRY-STVKYADRIIVLDKGEVAEYGT 595
Cdd:cd03295 141 QQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRL-QQELGktiVFVTHDIdEAFRLADRIAIMKNGEIVQVGT 219
|
....*
gi 502825101 596 HVELL 600
Cdd:cd03295 220 PDEIL 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
372-600 |
1.21e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 126.64 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQD----FVryELDVKENIGYGdykRSNHLVaiqaaaKRSGALTMIDSLPDK--MDTQLGKTFANgiqLSGGQWQRIAI 525
Cdd:PRK13632 88 IFQNpdnqFI--GATVEDDIAFG---LENKKV------PPKKMKDIIDDLAKKvgMEDYLDKEPQN---LSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 526 ARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS--HRYSTVKYADRIIVLDKGEVAEYGTHVELL 600
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
363-572 |
2.14e-32 |
|
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: 131.71 E-value: 2.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 363 ENVSSTEEGIQFLNVSFKYPGQeNYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQP 442
Cdd:TIGR02868 326 GAVGLGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 443 QDWQDRISAIFQDFVRYELDVKEN--IGYGDYKRSnhlvAIQAAAKRSGALTMIDSLPDKMDTQLGKTfanGIQLSGGQW 520
Cdd:TIGR02868 405 DEVRRRVSVCAQDAHLFDTTVRENlrLARPDATDE----ELWAALERVGLADWLRALPDGLDTVLGEG---GARLSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502825101 521 QRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHR 572
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
372-605 |
4.68e-32 |
|
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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 125.26 E-value: 4.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKY-PGQ--ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQD- 447
Cdd:TIGR04521 1 IKLKNVSYIYqPGTpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 448 --RISAIFQdFVRYEL---DVKENIGYGDykrSNHLVAIQAAAKRSGALTMIDSLPDKMDTQlgKTFangiQLSGGQWQR 522
Cdd:TIGR04521 81 rkKVGLVFQ-FPEHQLfeeTVYKDIAFGP---KNLGLSEEEAEERVKEALELVGLDEEYLER--SPF----ELSGGQMRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 523 IAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGL---FISHRYSTV-KYADRIIVLDKGEVAEYGT--- 595
Cdd:TIGR04521 151 VAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRL-HKEKGLtviLVTHSMEDVaEYADRVIVMHKGKIVLDGTpre 229
|
250
....*....|...
gi 502825101 596 ---HVELLDTNGI 605
Cdd:TIGR04521 230 vfsDVDELEKIGL 242
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
375-601 |
5.43e-32 |
|
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: 126.32 E-value: 5.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 375 LNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDY---EGIILLNGKRIEDYQPQDWQD---- 447
Cdd:COG0444 7 LKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKirgr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 448 RISAIFQD-------------FVRYELDVKENIGYGD-YKRSNHL---VAIQAAAKRsgaltmIDSLPdkmdtqlgktfa 510
Cdd:COG0444 87 EIQMIFQDpmtslnpvmtvgdQIAEPLRIHGGLSKAEaRERAIELlerVGLPDPERR------LDRYP------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 511 ngIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMG---LFISHRYSTVKY-ADRIIVLD 586
Cdd:COG0444 149 --HELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDL-QRELGlaiLFITHDLGVVAEiADRVAVMY 225
|
250
....*....|....*
gi 502825101 587 KGEVAEYGTHVELLD 601
Cdd:COG0444 226 AGRIVEEGPVEELFE 240
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
372-599 |
2.04e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 123.69 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKY-PGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRIS 450
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 451 AIFQD----FV--RYELDVK---ENIG--YGDYK-RSNH---LVAIQAAAKRSGAltmidslpdkmdtqlgktfangiQL 515
Cdd:PRK13650 85 MVFQNpdnqFVgaTVEDDVAfglENKGipHEEMKeRVNEaleLVGMQDFKEREPA-----------------------RL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 516 SGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS--HRYSTVKYADRIIVLDKGEVAEY 593
Cdd:PRK13650 142 SGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISitHDLDEVALSDRVLVMKNGQVEST 221
|
....*.
gi 502825101 594 GTHVEL 599
Cdd:PRK13650 222 STPREL 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
372-603 |
2.97e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 121.79 E-value: 2.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQenytLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDwqdR-IS 450
Cdd:COG3840 2 LRLDDLTYRYGDF----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RpVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 451 AIFQD---FVryELDVKENIGYG---DYKRS-NHLVAIQAAAKRSGALTMIDSLPDkmdtqlgktfangiQLSGGQWQRI 523
Cdd:COG3840 75 MLFQEnnlFP--HLTVAQNIGLGlrpGLKLTaEQRAQVEQALERVGLAGLLDRLPG--------------QLSGGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 524 AIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIA--QKSMGLFISHRYSTVK-YADRIIVLDKGEVAEYGTHVELL 600
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCreRGLTVLMVTHDPEDAArIADRVLLVADGRIAADGPTAALL 218
|
...
gi 502825101 601 DTN 603
Cdd:COG3840 219 DGE 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
389-595 |
3.09e-31 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 121.78 E-value: 3.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQD---------WQdrISAIFQdfvry 459
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEiarlgigrtFQ--IPRLFP----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 460 ELDVKENI----------GYGDYKRSNHLVAIQAAAKRsgALTMIDsLPDKMDTQLGktfangiQLSGGQWQRIAIARAY 529
Cdd:cd03219 89 ELTVLENVmvaaqartgsGLLLARARREEREARERAEE--LLERVG-LADLADRPAG-------ELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 530 MRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMG-LFISHRYSTV-KYADRIIVLDKGEV-AEyGT 595
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITvLLVEHDMDVVmSLADRVTVLDQGRViAE-GT 226
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
375-600 |
5.71e-31 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 121.87 E-value: 5.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 375 LNVSFKYPG-----QENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEdyqPQDWQDR- 448
Cdd:COG4167 10 LSKTFKYRTglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLE---YGDYKYRc 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 --ISAIFQDfVRYELDVKENIGY---GDYKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTqlgktfanGIQ-LSGGQWQR 522
Cdd:COG4167 87 khIRMIFQD-PNTSLNPRLNIGQileEPLRLNTDLTAEEREERIFATLRLVGLLPEHANF--------YPHmLSSGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 523 IAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGL---FISHRYSTVKY-ADRIIVLDKGEVAEYGTHVE 598
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLEL-QEKLGIsyiYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAE 236
|
..
gi 502825101 599 LL 600
Cdd:COG4167 237 VF 238
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
372-590 |
9.79e-31 |
|
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: 119.56 E-value: 9.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDyQPQDW---QDR 448
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNInelRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 ISAIFQDFVRYE-LDVKENIGYGDYKRsNHLVAIQAAAKRSGALTMIdSLPDKMDtqlgktfANGIQLSGGQWQRIAIAR 527
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPIKV-KGMSKAEAEERALELLEKV-GLADKAD-------AYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 528 AYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFI-SHRYSTV-KYADRIIVLDKGEV 590
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVvTHEMGFArEVADRVIFMDDGRI 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
391-608 |
1.38e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 122.53 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 391 NVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQD---RISAIFQDfvRYE-LD---- 462
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQD--PYAsLNprmt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 463 VKENIGYGdykrsnhlVAIQAAAKRSGALTMIDSLPDKMDtqLGKTFANGI--QLSGGQWQRIAIARAYMRRASLYILDE 540
Cdd:COG4608 114 VGDIIAEP--------LRIHGLASKAERRERVAELLELVG--LRPEHADRYphEFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502825101 541 PTAALDPAAEEEVFQDFQEIaQKSMGL---FISHRYSTVKY-ADRIIVLDKGEVaeygthVELLDTNGIYAR 608
Cdd:COG4608 184 PVSALDVSIQAQVLNLLEDL-QDELGLtylFISHDLSVVRHiSDRVAVMYLGKI------VEIAPRDELYAR 248
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
372-601 |
1.64e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 120.63 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQD----FVRYEldVKENIGYGdykRSNHLVAIQAAAKR-SGALTMIDSLpDKMDTQLGktfangiQLSGGQWQRIAIA 526
Cdd:PRK13648 88 VFQNpdnqFVGSI--VKYDVAFG---LENHAVPYDEMHRRvSEALKQVDML-ERADYEPN-------ALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 527 RAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS--HRYSTVKYADRIIVLDKGEVAEYGTHVELLD 601
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
366-592 |
1.90e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.19 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 366 SSTEEGIQFLNVSFKYPGQENYT--LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPq 443
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 444 dwqdRISAIFQDFVRYE-LDVKENIGYGDykRSNHLVAIQAAAKRSGALTMI------DSLPDkmdtqlgktfangiQLS 516
Cdd:COG1116 81 ----DRGVVFQEPALLPwLTVLDNVALGL--ELRGVPKAERRERARELLELVglagfeDAYPH--------------QLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 517 GGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQ---KSMgLFISHryST---VKYADRIIVLDK--G 588
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetgKTV-LFVTH--DVdeaVFLADRVVVLSArpG 217
|
....
gi 502825101 589 EVAE 592
Cdd:COG1116 218 RIVE 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
372-589 |
2.66e-30 |
|
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: 117.96 E-value: 2.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQE---NYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGkRIEdYQPQD-Wqd 447
Cdd:cd03250 1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIA-YVSQEpW-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 448 risaIFQDFVRyeldvkENIGYGD------YKRsnhlvAIQAAAKRSGaltmIDSLPDKMDTQLGKtfaNGIQLSGGQWQ 521
Cdd:cd03250 77 ----IQNGTIR------ENILFGKpfdeerYEK-----VIKACALEPD----LEILPDGDLTEIGE---KGINLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 522 RIAIARAYMRRASLYILDEPTAALDPAAEEEVFQD--FQEIAQKSMGLFISHRYSTVKYADRIIVLDKGE 589
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
372-585 |
8.89e-30 |
|
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: 117.19 E-value: 8.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYT--LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPqdwqdRI 449
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 450 SAIFQDFVRYE-LDVKENIGYGDykrsnHLVAIQAAAKRSGALTMIDslpdkmdtQLG-KTFANG--IQLSGGQWQRIAI 525
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGL-----ELQGVPKAEARERAEELLE--------LVGlSGFENAypHQLSGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 526 ARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKS--MGLFISHRYS-TVKYADRIIVL 585
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVL 205
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
372-590 |
1.44e-29 |
|
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: 116.35 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGqeNYT-LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQD---WQD 447
Cdd:cd03292 1 IEFINVTKTYPN--GTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 448 RISAIFQDF-VRYELDVKENIGYGdykrsnhLVAIQA----AAKRSGALTMIDSLPDKMDTqlgktFANgiQLSGGQWQR 522
Cdd:cd03292 79 KIGVVFQDFrLLPDRNVYENVAFA-------LEVTGVppreIRKRVPAALELVGLSHKHRA-----LPA--ELSGGEQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 523 IAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS-HRYSTV-KYADRIIVLDKGEV 590
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAtHAKELVdTTRHRVIALERGKL 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
372-595 |
1.52e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 119.82 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQenYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQdwQDRISA 451
Cdd:COG3842 6 LELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDfvrYEL----DVKENIGYG----DYKRSnhlvAIQAAAKRsgALTMIDsLPDkmdtqLGKTFANgiQLSGGQWQRI 523
Cdd:COG3842 82 VFQD---YALfphlTVAENVAFGlrmrGVPKA----EIRARVAE--LLELVG-LEG-----LADRYPH--QLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 524 AIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMG---LFISHR----YStvkYADRIIVLDKGEVAEYGT 595
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRL-QRELGitfIYVTHDqeeaLA---LADRIAVMNDGRIEQVGT 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
337-589 |
1.60e-29 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 125.14 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 337 YMTQLFSFLNVPESTD-KP---NVSEEKTLENVSSteegIQFLNVSFKYPGQENYTL-KNVNFHIKPGETLALVGSNGSG 411
Cdd:PTZ00265 348 YMKSLEATNSLYEIINrKPlveNNDDGKKLKDIKK----IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCG 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 412 KSTIVKLLTRLYTDYEGIILLN-GKRIEDYQPQDWQDRISAIFQDFVRYELDVKENIGYGDYK----------------- 473
Cdd:PTZ00265 424 KSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSlkdlealsnyynedgnd 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 474 -RSNHLVAIQAAAKRSGALTMI-------------------------------------DSLPDKMDTQLGktfANGIQL 515
Cdd:PTZ00265 504 sQENKNKRNSCRAKCAGDLNDMsnttdsneliemrknyqtikdsevvdvskkvlihdfvSALPDKYETLVG---SNASKL 580
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 516 SGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIA--QKSMGLFISHRYSTVKYADRIIVLDKGE 589
Cdd:PTZ00265 581 SGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
372-606 |
1.61e-29 |
|
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: 125.06 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIG-YGDYKRSNHLVAIQAAAKRsgalTMIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYM 530
Cdd:TIGR00957 1365 IPQDPVLFSGSLRMNLDpFSQYSDEEVWWALELAHLK----TFVSALPDKLDHECAE---GGENLSVGQRQLVCLARALL 1437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIY 606
Cdd:TIGR00957 1438 RKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
372-595 |
3.33e-29 |
|
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: 115.20 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIG-YGDYKRsnhlVAIQAAAKRSGAltmidslpdkmdtqlgktfanGIQLSGGQWQRIAIARAYM 530
Cdd:cd03369 87 IPQDPTLFSGTIRSNLDpFDEYSD----EEIYGALRVSEG---------------------GLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGT 595
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
372-602 |
4.59e-29 |
|
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: 115.68 E-value: 4.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQD---R 448
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 ISAIFQD---FVryELDVKENIGYGDYKRSN---HLVAIQAAAK--RSGALTMIDSLPDkmdtqlgktfangiQLSGGQW 520
Cdd:cd03261 79 MGMLFQSgalFD--SLTVFENVAFPLREHTRlseEEIREIVLEKleAVGLRGAEDLYPA--------------ELSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 521 QRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGL---FISHRYSTVKY-ADRIIVLDKGEVAEYGTH 596
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSL-KKELGLtsiMVTHDLDTAFAiADRIAVLYDGKIVAEGTP 221
|
....*.
gi 502825101 597 VELLDT 602
Cdd:cd03261 222 EELRAS 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
386-600 |
5.03e-29 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 115.51 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 386 NYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQdwQDRISAIFQDFVRY-ELDVK 464
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 465 ENIGYGDYKRSNHLVAIQAAAKRSGALTMIDSLPDKmdtqlgktfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPTAA 544
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNR----------KPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 545 LDPAAEEEVFQDFQEIaQKSMG---LFISHRYSTVKY-ADRIIVLDKGEVAEYGTHVELL 600
Cdd:cd03299 160 LDVRTKEKLREELKKI-RKEFGvtvLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
372-602 |
5.08e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 115.58 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSfKYPGQeNYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:PRK09493 2 IEFKNVS-KHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 --IFQDFVRY-ELDVKENIGYGdykrSNHLVAIQAAAKRSGALTMIDS--LPDKMDTQLGktfangiQLSGGQWQRIAIA 526
Cdd:PRK09493 80 gmVFQQFYLFpHLTALENVMFG----PLRVRGASKEEAEKQARELLAKvgLAERAHHYPS-------ELSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502825101 527 RAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFI-SHRYSTV-KYADRIIVLDKGEVAEYGTHVELLDT 602
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIvTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
362-612 |
6.78e-29 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 123.22 E-value: 6.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 362 LENVSSTEEGIQFLNVSFKYPGQENYTL-KNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLY----------------- 423
Cdd:PTZ00265 1156 IKNKNDIKGKIEIMDVNFRYISRPNVPIyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtnd 1235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 424 ----TDYE---------------------------------GIILLNGKRIEDYQPQDWQDRISAIFQDFVRYELDVKEN 466
Cdd:PTZ00265 1236 mtneQDYQgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYEN 1315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 467 IGYGdyKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTQLGKTfanGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALD 546
Cdd:PTZ00265 1316 IKFG--KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPY---GKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 547 PAAE---EEVFQDFQEIAQKSMgLFISHRYSTVKYADRIIVLDKGE-----VAEYGTHVELLDT-NGIYARLFNL 612
Cdd:PTZ00265 1391 SNSEkliEKTIVDIKDKADKTI-ITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVqDGVYKKYVKL 1464
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
372-601 |
7.24e-29 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 115.03 E-value: 7.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQdwQDRISA 451
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRY-ELDVKENIGYGDYKRSNHLVAIQAAAKRsgALTMIdslpdKMDTQLGKTFAngiQLSGGQWQRIAIARAYM 530
Cdd:cd03300 77 VFQNYALFpHLTVFENIAFGLRLKKLPKAEIKERVAE--ALDLV-----QLEGYANRKPS---QLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMG---LFISHRYS-TVKYADRIIVLDKGEVAEYGTHVELLD 601
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRL-QKELGitfVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
376-590 |
7.69e-29 |
|
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: 113.89 E-value: 7.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQENyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDyqpqdwQDRISAIF-- 453
Cdd:cd03226 4 NISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRKSIGyv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 454 -QDfVRYEL---DVKENIGYGDYKRSNHLVAIQAAAKRSGALTMIDSLPdkMDtqlgktfangiqLSGGQWQRIAIARAY 529
Cdd:cd03226 77 mQD-VDYQLftdSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHP--LS------------LSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 530 MRRASLYILDEPTAALDPAAEEEVFQDFQEIA-QKSMGLFISHRYSTV-KYADRIIVLDKGEV 590
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLaKVCDRVLLLANGAI 204
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
389-601 |
1.06e-28 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 114.71 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDyQPQDWQD---RISAIFQDFvryEL---- 461
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKlrrKVGMVFQQF---NLfphl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 462 DVKENIGYGD---YKRSNhlvaiQAAAKRsgALTMIDS--LPDKMDtqlgktfANGIQLSGGQWQRIAIARAYMRRASLY 536
Cdd:COG1126 93 TVLENVTLAPikvKKMSK-----AEAEER--AMELLERvgLADKAD-------AYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502825101 537 ILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFI-SH-----RystvKYADRIIVLDKGEVAEYGTHVELLD 601
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVvTHemgfaR----EVADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
371-602 |
1.21e-28 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 114.36 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 371 GIQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQdrIS 450
Cdd:cd03296 2 SIEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN--VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 451 AIFQDFVRYE-LDVKENIGYGdykrsnhlVAIQAAAKRSGALTM---IDSLPDKMD-TQLGKTFANgiQLSGGQWQRIAI 525
Cdd:cd03296 78 FVFQHYALFRhMTVFDNVAFG--------LRVKPRSERPPEAEIrakVHELLKLVQlDWLADRYPA--QLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 526 ARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKsMG---LFISHRYS-TVKYADRIIVLDKGEVAEYGTHVELLD 601
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDE-LHvttVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
.
gi 502825101 602 T 602
Cdd:cd03296 227 H 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
372-595 |
1.35e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 117.10 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYpgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPqdwQDR-IS 450
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP---KDRnIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 451 AIFQDFVRYE-LDVKENIGYG---------DYKRsnhlvAIQAAAKRSGaLT-MIDSLPDkmdtqlgktfangiQLSGGQ 519
Cdd:COG3839 79 MVFQSYALYPhMTVYENIAFPlklrkvpkaEIDR-----RVREAAELLG-LEdLLDRKPK--------------QLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 520 WQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGlfishrySTVKY-----------ADRIIVLDKG 588
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRL-HRRLG-------TTTIYvthdqveamtlADRIAVMNDG 210
|
....*..
gi 502825101 589 EVAEYGT 595
Cdd:COG3839 211 RIQQVGT 217
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
370-599 |
2.20e-28 |
|
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: 119.52 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 370 EGIQFLNVSFKYP---GQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQ 446
Cdd:COG4615 326 QTLELRGVTYRYPgedGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 447 DRISAIFQDFVRYEldvkenigygdykrsnHLVAIQAAAKRSGALTMIDSLpdKMDTQLgkTFANG----IQLSGGQWQR 522
Cdd:COG4615 406 QLFSAVFSDFHLFD----------------RLLGLDGEADPARARELLERL--ELDHKV--SVEDGrfstTDLSQGQRKR 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 523 IAIARAYMRRASLYILDEPTAALDPAaeeevFQDF--QEI--AQKSMG---LFISH--RYSTVkyADRIIVLDKGEVAEY 593
Cdd:COG4615 466 LALLVALLEDRPILVFDEWAADQDPE-----FRRVfyTELlpELKARGktvIAISHddRYFDL--ADRVLKMDYGKLVEL 538
|
....*.
gi 502825101 594 GTHVEL 599
Cdd:COG4615 539 TGPAAL 544
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
372-594 |
4.15e-28 |
|
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: 111.96 E-value: 4.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQenYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPqdwQDR-IS 450
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP---KDRdIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 451 AIFQDFVRY-ELDVKENIGYGDYKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTqlgktfangiQLSGGQWQRIAIARAY 529
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPK----------QLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 530 MRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMG---LFISHRYS-TVKYADRIIVLDKGEVAEYG 594
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRL-QQRLGtttIYVTHDQVeAMTMADRIAVMNDGQIQQIG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
389-571 |
5.10e-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: 111.80 E-value: 5.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDyQPQDWQDRISAIF-QDFVRYELDVKENI 467
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGhADGLKPELTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 GY--GDYKRSNHLVAIQAAAKRSGaltmidsLPDKMDTQLGktfangiQLSGGQWQRIAIARAYMRRASLYILDEPTAAL 545
Cdd:COG4133 97 RFwaALYGLRADREAIDEALEAVG-------LAGLADLPVR-------QLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180
....*....|....*....|....*..
gi 502825101 546 DPAAEEEVFQDFQE-IAQKSMGLFISH 571
Cdd:COG4133 163 DAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
389-601 |
5.49e-28 |
|
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: 112.38 E-value: 5.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIED------------YQPQDWQdrisaIFQDf 456
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpphriarlgigYVPEGRR-----IFPS- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 457 vryeLDVKENIGYGDYKRSnhlvaiqAAAKRSGALTMIDSL-PD--KMDTQLGKTfangiqLSGGQWQRIAIARAYMRRA 533
Cdd:COG0410 93 ----LTVEENLLLGAYARR-------DRAEVRADLERVYELfPRlkERRRQRAGT------LSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 534 SLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTV--KYADRIIVLDKGEVAEYGTHVELLD 601
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFalEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
389-601 |
8.66e-28 |
|
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: 117.86 E-value: 8.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLyTDYEGIILLNGKRIEDYQPQDWQD---RISAIFQD-FV----Rye 460
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALRPlrrRMQVVFQDpFGslspR-- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 461 LDVKENIGYG------DYKRSNHLVAIQAAAKRSGaLT--MIDSLPDkmdtqlgktfangiQLSGGQWQRIAIARAYMRR 532
Cdd:COG4172 379 MTVGQIIAEGlrvhgpGLSAAERRARVAEALEEVG-LDpaARHRYPH--------------EFSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 533 ASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGL---FISHRYSTVKY-ADRIIVLDKGEVAEYGTHVELLD 601
Cdd:COG4172 444 PKLLVLDEPTSALDVSVQAQILDLLRDL-QREHGLaylFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
372-603 |
2.27e-27 |
|
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: 110.84 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQD---R 448
Cdd:COG1127 6 IEVRNLTKSFGDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYElrrR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 ISAIFQ-----DFvryeLDVKENIG-----YGDYKRSnhLVAIQAAAK--RSGALTMIDSLPDkmdtqlgktfangiQLS 516
Cdd:COG1127 84 IGMLFQggalfDS----LTVFENVAfplreHTDLSEA--EIRELVLEKleLVGLPGAADKMPS--------------ELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 517 GGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGL---FISHRYSTV-KYADRIIVLDKGEVAE 592
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIREL-RDELGLtsvVVTHDLDSAfAIADRVAVLADGKIIA 222
|
250
....*....|.
gi 502825101 593 YGTHVELLDTN 603
Cdd:COG1127 223 EGTPEELLASD 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
389-590 |
2.36e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 115.89 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDR-ISAIFQDFVRYE-LDVKEN 466
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgIGMVHQHFMLVPnLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 467 IGYGDYKRSNHLVAIQAAAKRsgaltmIDSLPDKM------DTQLGktfangiQLSGGQWQRIAIARAYMRRASLYILDE 540
Cdd:COG3845 101 IVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVE-------DLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502825101 541 PTAALDPAAEEEVFQDFQEIAQ--KSMgLFISHRYSTVK-YADRIIVLDKGEV 590
Cdd:COG3845 168 PTAVLTPQEADELFEILRRLAAegKSI-IFITHKLREVMaIADRVTVLRRGKV 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
369-595 |
7.00e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.56 E-value: 7.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 369 EEGIQFLNVSFKY----PGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDyQPQD 444
Cdd:PRK13633 2 NEMIKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD-EENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 445 WQDRISA--IFQ--DFVRYELDVKENIGYGDykrSNHLVAIQAAAKRsgaltmIDSLPDKMDTQLGKTFANGIqLSGGQW 520
Cdd:PRK13633 81 WDIRNKAgmVFQnpDNQIVATIVEEDVAFGP---ENLGIPPEEIRER------VDESLKKVGMYEYRRHAPHL-LSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 521 QRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKS--MGLFISHRYSTVKYADRIIVLDKGEVAEYGT 595
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
375-601 |
8.84e-27 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 111.34 E-value: 8.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 375 LNVSFK------YPGQENYTLK---NVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDW 445
Cdd:PRK15079 14 LKVHFDikdgkqWFWQPPKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 446 QDR---ISAIFQDFVRyELDVKENIG----------YGDYKRSNHLVAIQAAAKRSGAL-TMIDSLPDkmdtqlgktfan 511
Cdd:PRK15079 94 RAVrsdIQMIFQDPLA-SLNPRMTIGeiiaeplrtyHPKLSRQEVKDRVKAMMLKVGLLpNLINRYPH------------ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 512 giQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGL---FISHRYSTVKY-ADRIIVLDK 587
Cdd:PRK15079 161 --EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL-QREMGLsliFIAHDLAVVKHiSDRVLVMYL 237
|
250
....*....|....
gi 502825101 588 GEVAEYGTHVELLD 601
Cdd:PRK15079 238 GHAVELGTYDEVYH 251
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
375-594 |
1.27e-26 |
|
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: 107.77 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 375 LNVSFKYPgQENYTLKnVNFHIkPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQ------PQdwQDR 448
Cdd:cd03297 2 LCVDIEKR-LPDFTLK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinlpPQ--QRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 ISAIFQDFVRY-ELDVKENIGYGDYKRSNHLVAIQAAAkrsgaltMIDSLpdkmdtQLGK-TFANGIQLSGGQWQRIAIA 526
Cdd:cd03297 77 IGLVFQQYALFpHLNVRENLAFGLKRKRNREDRISVDE-------LLDLL------GLDHlLNRYPAQLSGGEKQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502825101 527 RAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMG--LFISHRYSTVKY-ADRIIVLDKGEVAEYG 594
Cdd:cd03297 144 RALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIpvIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
372-595 |
1.44e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 114.01 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKS----TIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQ- 446
Cdd:COG4172 9 VEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 447 ---DRISAIFQdfvryE----LD----VKENIG-----YGDYKRSN---------HLVAIQAAAKRsgaltmIDSLPDkm 501
Cdd:COG4172 89 irgNRIAMIFQ-----EpmtsLNplhtIGKQIAevlrlHRGLSGAAararalellERVGIPDPERR------LDAYPH-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 502 dtqlgktfangiQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMG---LFISHRYSTV-K 577
Cdd:COG4172 156 ------------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDL-QRELGmalLLITHDLGVVrR 222
|
250
....*....|....*...
gi 502825101 578 YADRIIVLDKGEVAEYGT 595
Cdd:COG4172 223 FADRVAVMRQGEIVEQGP 240
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
375-594 |
1.82e-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: 107.58 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 375 LNVSFKYPGQENYTLknvNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGkriEDYQPQDWQDR-ISAIF 453
Cdd:cd03298 3 LDKIRFSYGEQPMHF---DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING---VDVTAAPPADRpVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 454 QDF-VRYELDVKENIGYGdykRSNHL-------VAIQAAAKRSGALTMIDSLPDkmdtqlgktfangiQLSGGQWQRIAI 525
Cdd:cd03298 77 QENnLFAHLTVEQNVGLG---LSPGLkltaedrQAIEVALARVGLAGLEKRLPG--------------ELSGGERQRVAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502825101 526 ARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEI-AQKSMG-LFISHRYSTVKY-ADRIIVLDKGEVAEYG 594
Cdd:cd03298 140 ARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTvLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
372-599 |
4.05e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.35 E-value: 4.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLY---TDYEGIILLNGKRIEDYQPQDWQDR 448
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 ISAIFQD----FVryELDVKENIGYG----DYKRSNHLVAIQAAAKRSGALTMIDSLPdkmdtqlgktfANgiqLSGGQW 520
Cdd:PRK13640 86 VGIVFQNpdnqFV--GATVGDDVAFGlenrAVPRPEMIKIVRDVLADVGMLDYIDSEP-----------AN---LSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 521 QRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGLF---ISHRYSTVKYADRIIVLDKGEVAEYGTHV 597
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKL-KKKNNLTvisITHDIDEANMADQVLVLDDGKLLAQGSPV 228
|
..
gi 502825101 598 EL 599
Cdd:PRK13640 229 EI 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
372-600 |
6.05e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 109.01 E-value: 6.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVS--FKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRL--YTdyEGIILLNGKRIEDYQPQDWQD 447
Cdd:COG1135 2 IELENLSktFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLerPT--SGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 448 ---RISAIFQDFvryEL----DVKENIGY-----GdYKRSnhlvAIQA-----------AAKRsgaltmiDSLPDkmdtq 504
Cdd:COG1135 80 arrKIGMIFQHF---NLlssrTVAENVALpleiaG-VPKA----EIRKrvaellelvglSDKA-------DAYPS----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 505 lgktfangiQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKsMGL---FISHRYSTVKY-AD 580
Cdd:COG1135 140 ---------QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRE-LGLtivLITHEMDVVRRiCD 209
|
250 260
....*....|....*....|
gi 502825101 581 RIIVLDKGEVAEYGTHVELL 600
Cdd:COG1135 210 RVAVLENGRIVEQGPVLDVF 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
372-598 |
6.57e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.83 E-value: 6.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKY-PGQ--ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQP--QDWQ 446
Cdd:PRK13637 3 IKIENLTHIYmEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 447 DRISAIFQ--DFVRYELDVKENIGYGDYKRSNHLVAIQAAAKRSGALTMID--SLPDKmdtqlgktfaNGIQLSGGQWQR 522
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDK----------SPFELSGGQKRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 523 IAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQK-SMG-LFISHRYSTV-KYADRIIVLDKGEVAEYGTHVE 598
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTiILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
371-601 |
9.78e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 108.70 E-value: 9.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 371 GIQFLNVSFKYPgqeNYT-LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGkriedyqpQDW---- 445
Cdd:COG1118 2 SIEVRNISKRFG---SFTlLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--------RDLftnl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 446 --QDR-ISAIFQDfvrYEL----DVKENIGYG--DYKRSNHlvaiQAAAKRSGALTMIDsLPDkmdtqLGKTFANgiQLS 516
Cdd:COG1118 71 ppRERrVGFVFQH---YALfphmTVAENIAFGlrVRPPSKA----EIRARVEELLELVQ-LEG-----LADRYPS--QLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 517 GGQWQRIAIARAYMRRASLYILDEPTAALDPAA----EEEVFQDFQEIAQKSmgLFISH------RystvkYADRIIVLD 586
Cdd:COG1118 136 GGQRQRVALARALAVEPEVLLLDEPFGALDAKVrkelRRWLRRLHDELGGTT--VFVTHdqeealE-----LADRVVVMN 208
|
250
....*....|....*
gi 502825101 587 KGEVAEYGTHVELLD 601
Cdd:COG1118 209 QGRIEQVGTPDEVYD 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
389-595 |
3.71e-25 |
|
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: 104.74 E-value: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQD---------WQdrISAIFQdfvry 459
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRiarlgiartFQ--NPRLFP----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 460 ELDVKEN--IGYGDYKRSNHLVAI--------QAAAKRSGALTMID--SLPDKMDTQLGktfangiQLSGGQWQRIAIAR 527
Cdd:COG0411 93 ELTVLENvlVAAHARLGRGLLAALlrlprarrEEREARERAEELLErvGLADRADEPAG-------NLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 528 AYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKsMG---LFISHRYSTV-KYADRIIVLDKGEV-AEyGT 595
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDE-RGitiLLIEHDMDLVmGLADRIVVLDFGRViAE-GT 236
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
389-600 |
4.17e-25 |
|
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: 105.03 E-value: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQD----RISAIFQDFVRY-ELDV 463
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 464 KENIGY-----GDYKRSNHLVAIQaAAKRSGALTMIDSLPDkmdtqlgktfangiQLSGGQWQRIAIARAYMRRASLYIL 538
Cdd:cd03294 120 LENVAFglevqGVPRAEREERAAE-ALELVGLEGWEHKYPD--------------ELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 539 DEPTAALDP---AAEEEVFQDFQEIAQKSMgLFISHRYS-TVKYADRIIVLDKGEVAEYGTHVELL 600
Cdd:cd03294 185 DEAFSALDPlirREMQDELLRLQAELQKTI-VFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
372-599 |
5.39e-25 |
|
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: 103.35 E-value: 5.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIeDYQPQDWQDRISA 451
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRY-ELDVKENIGYgdYKRSNHLVAIQAAAKRSGALTMIDsLPDKMDTQLGktfangiQLSGGQWQRIAIARAYM 530
Cdd:cd03263 80 CPQFDALFdELTVREHLRF--YARLKGLPKSEIKEEVELLLRVLG-LTDKANKRAR-------TLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKY-ADRIIVLDKGEVAEYGTHVEL 599
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
372-609 |
9.56e-25 |
|
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: 103.84 E-value: 9.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIgygDYKRSNHLVAIQAAAKRSGALTMIDSLP---DKMDTQLGKTFangiqlSGGQWQRIAIARA 528
Cdd:cd03288 100 ILQDPILFSGSIRFNL---DPECKCTDDRLWEALEIAQLKNMVKSLPgglDAVVTEGGENF------SVGQRQLFCLARA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 529 YMRRASLYILDEPTAALDPAAEeevfqdfqEIAQK-SMGLF-------ISHRYSTVKYADRIIVLDKGEVAEYGTHVELL 600
Cdd:cd03288 171 FVRKSSILIMDEATASIDMATE--------NILQKvVMTAFadrtvvtIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
250
....*....|
gi 502825101 601 -DTNGIYARL 609
Cdd:cd03288 243 aQEDGVFASL 252
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
356-599 |
3.20e-24 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 103.01 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 356 VSEEKTLENVSSTEEGIQFLNvsfkYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGk 435
Cdd:cd03291 24 AKQENNDRKHSSDDNNLFFSN----LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 436 RIEdYQPQdwqdrISAIFQDfvryelDVKENIGYG-DYKRSNHLVAIQAAAKRSGaltmIDSLPDKMDTQLGKtfaNGIQ 514
Cdd:cd03291 99 RIS-FSSQ-----FSWIMPG------TIKENIIFGvSYDEYRYKSVVKACQLEED----ITKFPEKDNTVLGE---GGIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 515 LSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQD--FQEIAQKSMgLFISHRYSTVKYADRIIVLDKGEVAE 592
Cdd:cd03291 160 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEScvCKLMANKTR-ILVTSKMEHLKKADKILILHEGSSYF 238
|
....*..
gi 502825101 593 YGTHVEL 599
Cdd:cd03291 239 YGTFSEL 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
385-594 |
3.63e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.71 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 385 ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDyEGIILLNGKRIEDYQPQD---WQDRISAIFQD---FVR 458
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDpnsSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 459 YELDVKENIGYGDYKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTQLGktfangiQLSGGQWQRIAIARAYMRRASLYIL 538
Cdd:PRK15134 377 PRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPA-------EFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 539 DEPTAALDPAAEEEVFQDFQEIAQKSM--GLFISHRYSTVK-YADRIIVLDKGEVAEYG 594
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQlaYLFISHDLHVVRaLCHQVIVLRQGEVVEQG 508
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
350-594 |
5.29e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 106.86 E-value: 5.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 350 STDKPNVSEEKTLEN-VSSTEEGIQFLNVSFKYP---------GQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLL 419
Cdd:PRK10261 291 SLEHPAKQEPPIEQDtVVDGEPILQVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRAL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 420 TRLYTDYEGIILLNGKRIE---DYQPQDWQDRISAIFQDfVRYELDVKENIGYGDYK--RSNHLVAIQAAAKR-SGALTM 493
Cdd:PRK10261 371 LRLVESQGGEIIFNGQRIDtlsPGKLQALRRDIQFIFQD-PYASLDPRQTVGDSIMEplRVHGLLPGKAAAARvAWLLER 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 494 IDSLPDkmdtqlgKTFANGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMG---LFIS 570
Cdd:PRK10261 450 VGLLPE-------HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL-QRDFGiayLFIS 521
|
250 260
....*....|....*....|....*
gi 502825101 571 HRYSTV-KYADRIIVLDKGEVAEYG 594
Cdd:PRK10261 522 HDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
389-594 |
9.89e-24 |
|
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: 99.16 E-value: 9.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLT--RLYTDYEGIILLNGKRIEdyqPQDWQDRISAIFQDFVRYE-LDVKE 465
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD---KRSFRKIIGYVPQDDILHPtLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 466 NIGYgdykrsnhlvaiqaAAKRSGaltmidslpdkmdtqlgktfangiqLSGGQWQRIAIARAYMRRASLYILDEPTAAL 545
Cdd:cd03213 102 TLMF--------------AAKLRG-------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502825101 546 DPAAEEEVFQDFQEIAQKSMGLFIS-H--RYSTVKYADRIIVLDKGEVAEYG 594
Cdd:cd03213 143 DSSSALQVMSLLRRLADTGRTIICSiHqpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
376-603 |
1.02e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 101.32 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQENYT-LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQ 454
Cdd:PRK13642 9 NLVFKYEKESDVNqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 455 D----FVryELDVKENIGYGdykRSNHLVAIQAAAKR-SGALTMIDSLPDKMDTQlgktfangIQLSGGQWQRIAIARAY 529
Cdd:PRK13642 89 NpdnqFV--GATVEDDVAFG---MENQGIPREEMIKRvDEALLAVNMLDFKTREP--------ARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 530 MRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKS--MGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTN 603
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
389-592 |
1.50e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.53 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDY---QPQDWQDRISAIFQD---FVRYELD 462
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDsisAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 463 VKENIGygdyKRSNHLVAIQAAAKRSGALTMIDS--LPDKMDTQLGKtfangiQLSGGQWQRIAIARAYMRRASLYILDE 540
Cdd:PRK10419 108 VREIIR----EPLRHLLSLDKAERLARASEMLRAvdLDDSVLDKRPP------QLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 541 PTAALDPAAEEEVFQDFQEIAQKSmG---LFISHRYSTV-KYADRIIVLDKGEVAE 592
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQF-GtacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
393-609 |
2.26e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.27 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 393 NFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQdwQDRISAIFQD---FVryELDVKENIGY 469
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQEnnlFS--HLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 470 G--------DYKRSnhlvAIQAAAKRSGALTMIDSLPDkmdtqlgktfangiQLSGGQWQRIAIARAYMRRASLYILDEP 541
Cdd:PRK10771 95 GlnpglklnAAQRE----KLHAIARQMGIEDLLARLPG--------------QLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502825101 542 TAALDPAAEEEVFQDFQEI-AQKSMGLF-ISHRYS-TVKYADRIIVLDKGEVAEYGTHVELLDTNGIYARL 609
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVcQERQLTLLmVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
389-595 |
3.86e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.08 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDF-VRYELDVKENI 467
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSsLSFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 GYGDYKRSNHLVAIQAAAKRSGALTMIDSLPDKmDTQlgktfangiQLSGGQWQRIAIARA------YMRRASLYILDEP 541
Cdd:PRK13548 98 AMGRAPHGLSRAEDDALVAAALAQVDLAHLAGR-DYP---------QLSGGEQQRVQLARVlaqlwePDGPPRWLLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 542 TAALDPAAEEEVFQDFQEIAQKSMG--LFISHRYS-TVKYADRIIVLDKGEVAEYGT 595
Cdd:PRK13548 168 TSALDLAHQHHVLRLARQLAHERGLavIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
372-602 |
4.75e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 103.25 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKS----TIVKLLTRLYTDY-EGIILLNGKRIEDYQPQDWQ 446
Cdd:PRK15134 8 IENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYpSGDIRFHGESLLHASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 447 ----DRISAIFQdfvryELDVKENIGYGDYKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTQLGKTFANGI--QLSGGQW 520
Cdd:PRK15134 88 gvrgNKIAMIFQ-----EPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYphQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 521 QRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQK-SMG-LFISHRYSTV-KYADRIIVLDKGEVAEYGTHV 597
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGlLFITHNLSIVrKLADRVAVMQNGRCVEQNRAA 242
|
....*
gi 502825101 598 ELLDT 602
Cdd:PRK15134 243 TLFSA 247
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
371-601 |
5.81e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 5.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 371 GIQFLNVSFKYPGQ---ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRI----EDYQPQ 443
Cdd:PRK13649 2 GINLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 444 DWQDRISAIFQ--DFVRYELDVKENIGYGDykrSNHLVAIQAA---AKRSGALTMID-SLPDKmdtqlgktfaNGIQLSG 517
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGP---QNFGVSQEEAealAREKLALVGISeSLFEK----------NPFELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 518 GQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGL-FISHRYSTV-KYADRIIVLDKGEVAEYGT 595
Cdd:PRK13649 149 GQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIvLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
250
....*....|..
gi 502825101 596 ------HVELLD 601
Cdd:PRK13649 229 pkdifqDVDFLE 240
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
389-592 |
7.63e-23 |
|
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: 98.34 E-value: 7.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGK---RIEDYQPQDWQDRISAIFQD---FVRYELD 462
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyQLDRKQRRAFRRDVQLVFQDspsAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 463 VKENIGygdyKRSNHLVAIQAAAKRSGALTMID--SLPDKMDTQLGKtfangiQLSGGQWQRIAIARAYMRRASLYILDE 540
Cdd:TIGR02769 107 VRQIIG----EPLRHLTSLDESEQKARIAELLDmvGLRSEDADKLPR------QLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 541 PTAALDPAAEEEVFQDFQEIAQKS--MGLFISHRYSTV-KYADRIIVLDKGEVAE 592
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLQQAFgtAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
371-596 |
1.78e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 371 GIQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIIllngkRIEDYQpQDWQDRIS 450
Cdd:COG4161 2 SIQLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL-----NIAGHQ-FDFSQKPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 451 AifqdfvRYELDVKENIG--YGDYKRSNHLVAIQ---AAAKRSGALTMIDSL--PDKMDTQLGKT-FANG--IQLSGGQW 520
Cdd:COG4161 74 E------KAIRLLRQKVGmvFQQYNLWPHLTVMEnliEAPCKVLGLSKEQARekAMKLLARLRLTdKADRfpLHLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502825101 521 QRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFI-SHRYSTV-KYADRIIVLDKGEVAEYGTH 596
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIvTHEVEFArKVASQVVYMEKGRIIEQGDA 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
372-594 |
1.94e-22 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 95.90 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDyQPQDWQDRISA 451
Cdd:cd03266 4 ADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYE-LDVKENIGYgdYKRSNHLvaiqaaaKRSGALTMIDSLPDKMDTqlgKTFAN--GIQLSGGQWQRIAIARA 528
Cdd:cd03266 83 VSDSTGLYDrLTARENLEY--FAGLYGL-------KGDELTARLEELADRLGM---EELLDrrVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 529 YMRRASLYILDEPTAALDPAAEEEVFQDFQEiaQKSMG---LFISHRYSTV-KYADRIIVLDKGEVAEYG 594
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQ--LRALGkciLFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
389-608 |
2.11e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 98.50 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDR---ISAIFQDfvRY-ELDVK 464
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqkIQIVFQN--PYgSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 465 ENIGY--GDYKRSNhlVAIQAAAKRSGALTMI----------DSLPdKMdtqlgktfangiqLSGGQWQRIAIARAYMRR 532
Cdd:PRK11308 109 KKVGQilEEPLLIN--TSLSAAERREKALAMMakvglrpehyDRYP-HM-------------FSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 533 ASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGL---FISHRYSTVKY-ADRIIVLDKGEVAEYGthvellDTNGIYAR 608
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVLNLMMDL-QQELGLsyvFISHDLSVVEHiADEVMVMYLGRCVEKG------TKEQIFNN 245
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
372-588 |
2.15e-22 |
|
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: 95.75 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPqDWQdRISA 451
Cdd:cd03268 1 LKTNDLTKTYGKKR--VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-ALR-RIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRY-ELDVKENIGYG------DYKRSNHL---VAIQAAAKRsgaltmidslpdKMdtqlgKTFangiqlSGGQWQ 521
Cdd:cd03268 77 LIEAPGFYpNLTARENLRLLarllgiRKKRIDEVldvVGLKDSAKK------------KV-----KGF------SLGMKQ 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 522 RIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFI-SHRYSTV-KYADRIIVLDKG 588
Cdd:cd03268 134 RLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLIsSHLLSEIqKVADRIGIINKG 202
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
389-614 |
2.70e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 96.62 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDFVRYE-LDVKENI 467
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEgITVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 GYGdykRSNHL-------VAIQAAAKRSGALTMIDSLPDKMDTqlgktfangiQLSGGQWQRIAIARAYMRRASLYILDE 540
Cdd:PRK11231 98 AYG---RSPWLslwgrlsAEDNARVNQAMEQTRINHLADRRLT----------DLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 541 PTAALDPAAEEEVFQDFQEIAQKSmglfishrySTV-----------KYADRIIVLDKGEVAEYGTHVELLdTNGIYARL 609
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQG---------KTVvtvlhdlnqasRYCDHLVVLANGHVMAQGTPEEVM-TPGLLRTV 234
|
....*
gi 502825101 610 FNLQA 614
Cdd:PRK11231 235 FDVEA 239
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
389-613 |
3.12e-22 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 97.46 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDyQPQDWQDRISAIFQDFVRYE-LDVKENI 467
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR-EPRKVRRSIGIVPQYASVDEdLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 ----GYGDYKRSnhlvaiqAAAKRSGALTMIDSLPDKMDTQLGktfangiQLSGGQWQRIAIARAYMRRASLYILDEPTA 543
Cdd:TIGR01188 88 emmgRLYGLPKD-------EAEERAEELLELFELGEAADRPVG-------TYSGGMRRRLDIAASLIHQPDVLFLDEPTT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 544 ALDPAAEEEVFQDFQEIAQKSMGLFISHRY--STVKYADRIIVLDKGEVAEYGTHVEL---LDTNGIYARLFNLQ 613
Cdd:TIGR01188 154 GLDPRTRRAIWDYIRALKEEGVTILLTTHYmeEADKLCDRIAIIDHGRIIAEGTPEELkrrLGKDTLESRPRDIQ 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
372-604 |
3.58e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 101.98 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:PLN03232 1235 IKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYELDVKENIgygDYKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTQLgktFANGIQLSGGQWQRIAIARAYMR 531
Cdd:PLN03232 1315 IPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEV---SEGGENFSVGQRQLLSLARALLR 1388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNG 604
Cdd:PLN03232 1389 RSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
372-612 |
3.63e-22 |
|
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: 95.92 E-value: 3.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYpgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTR-LYTDYEGIILLNGKRIEDYQPQDWQDRI- 449
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWELRKRIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 450 --SAIFQDFVRYELDVKE--------NIGygdykRSNHLVAIQAAAkrsgALTMIDSLpdKMDTQLGKTFAngiQLSGGQ 519
Cdd:COG1119 82 lvSPALQLRFPRDETVLDvvlsgffdSIG-----LYREPTDEQRER----ARELLELL--GLAHLADRPFG---TLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 520 WQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQ---KSMgLFISHRY----STVkyaDRIIVLDKGEVAE 592
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegaPTL-VLVTHHVeeipPGI---THVLLLKDGRVVA 223
|
250 260
....*....|....*....|
gi 502825101 593 YGTHVELLdTNGIYARLFNL 612
Cdd:COG1119 224 AGPKEEVL-TSENLSEAFGL 242
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
372-594 |
3.76e-22 |
|
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: 94.95 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGeTLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNG----------KRIEDYQ 441
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 442 PQD--WQDRISAIfqDFVRYeLDVKENIGYGDYKRsnhlvAIQAAAKRSGaltMIDSLPDKMDtqlgktfangiQLSGGQ 519
Cdd:cd03264 78 PQEfgVYPNFTVR--EFLDY-IAWLKGIPSKEVKA-----RVDEVLELVN---LGDRAKKKIG-----------SLSGGM 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 520 WQRIAIARAYMRRASLYILDEPTAALDPaAEEEVFQD-FQEIAQKSMGLFISHRYSTVKY-ADRIIVLDKGEVAEYG 594
Cdd:cd03264 136 RRRVGIAQALVGDPSILIVDEPTAGLDP-EERIRFRNlLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
372-607 |
4.64e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 100.13 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQP-QDWQDRIS 450
Cdd:PRK15439 12 LCARSISKQYSGVE--VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPaKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 451 AIFQDFVRY-ELDVKENIGYGdykrsnhLVAIQAAAKRSGALTMIDSLPDKMDTQLGktfangiQLSGGQWQRIAIARAY 529
Cdd:PRK15439 90 LVPQEPLLFpNLSVKENILFG-------LPKRQASMQKMKQLLAALGCQLDLDSSAG-------SLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 530 MRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGL-FISHRYSTV-KYADRIIVLDKGEVAEYGTHVELLDTNGIYA 607
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIvFISHKLPEIrQLADRISVMRDGTIALSGKTADLSTDDIIQA 235
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
393-594 |
5.20e-22 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 94.54 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 393 NFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPqdWQDRISAIFQDFVRY-ELDVKENIGYGd 471
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP--YQRPVSMLFQENNLFaHLTVRQNIGLG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 472 YKRSNHLVAIQ-----AAAKRSGALTMIDSLPDkmdtqlgktfangiQLSGGQWQRIAIARAYMRRASLYILDEPTAALD 546
Cdd:TIGR01277 95 LHPGLKLNAEQqekvvDAAQQVGIADYLDRLPE--------------QLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502825101 547 PAAEEEVFQDFQEIA--QKSMGLFISHRYS-TVKYADRIIVLDKGEVAEYG 594
Cdd:TIGR01277 161 PLLREEMLALVKQLCseRQRTLLMVTHHLSdARAIASQIAVVSQGKIKVVS 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
322-607 |
7.06e-22 |
|
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: 101.18 E-value: 7.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 322 NELMYMVFNMHQNNLYMTQLFSFLNVPEStdKPNVSEEKTLEnvSSTEEGIQFLNVSFKYPGQENYTLKNVNFHIKPGET 401
Cdd:TIGR00957 591 NILPMVISSIVQASVSLKRLRIFLSHEEL--EPDSIERRTIK--PGEGNSITVHNATFTWARDLPPTLNGITFSIPEGAL 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 402 LALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIedYQPQD-WqdrisaIFQDFVRyeldvkENIGYGDYKRSNHLVA 480
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA--YVPQQaW------IQNDSLR------ENILFGKALNEKYYQQ 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 481 -IQAAAkrsgALTMIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDF-- 557
Cdd:TIGR00957 733 vLEACA----LLPDLEILPSGDRTEIGE---KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVig 805
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 502825101 558 -QEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYA 607
Cdd:TIGR00957 806 pEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFA 856
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
372-599 |
7.77e-22 |
|
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: 94.36 E-value: 7.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDyQPQDWQDRISA 451
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDF-VRYELDVKENigygdykrsnhlVAIQAA---AKRSGALTMIDSLPDKMD-----TQLGKTFangiqlSGGQWQR 522
Cdd:cd03265 78 VFQDLsVDDELTGWEN------------LYIHARlygVPGAERRERIDELLDFVGlleaaDRLVKTY------SGGMRRR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 523 IAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEI-AQKSMGLFISHRY--STVKYADRIIVLDKGEVAEYGTHVEL 599
Cdd:cd03265 140 LEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYmeEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
341-609 |
1.02e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 100.58 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 341 LFSFLNVPESTDKPNVSEeKTLENVSSTEEGIQFLNVSFKyPGQ----------------ENYTLKNVNFHIKPGETLAL 404
Cdd:PLN03130 571 LFMLPNLITQAVNANVSL-KRLEELLLAEERVLLPNPPLE-PGLpaisikngyfswdskaERPTLSNINLDVPVGSLVAI 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 405 VGSNGSGK-STIVKLLTRLYTDYEGIILLNGKRIedYQPQdwqdrISAIFQDFVRyeldvkENIGYG-DYKRSNHLVAIQ 482
Cdd:PLN03130 649 VGSTGEGKtSLISAMLGELPPRSDASVVIRGTVA--YVPQ-----VSWIFNATVR------DNILFGsPFDPERYERAID 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 483 AAAKRSGaltmIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDF--QEI 560
Cdd:PLN03130 716 VTALQHD----LDLLPGGDLTEIGE---RGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCikDEL 788
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 502825101 561 AQKSMGLfISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYARL 609
Cdd:PLN03130 789 RGKTRVL-VTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
372-589 |
1.02e-21 |
|
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: 91.74 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQenYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIIllngkriedyqpqdwqdrisa 451
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 ifqdfvryELDVKENIGYgdykrsnhlvaiqaaakrsgaltmidslpdkmdtqlgktFAngiQLSGGQWQRIAIARAYMR 531
Cdd:cd03221 58 --------TWGSTVKIGY---------------------------------------FE---QLSGGEKMRLALAKLLLE 87
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 532 RASLYILDEPTAALDP---AAEEEVFQDFQeiaqksmG--LFISH-RY--STVkyADRIIVLDKGE 589
Cdd:cd03221 88 NPNLLLLDEPTNHLDLesiEALEEALKEYP-------GtvILVSHdRYflDQV--ATKIIELEDGK 144
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
389-589 |
1.36e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.46 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYT--DYEGIILLNGKRIEDYQPQDWQDR-ISAIFQDF--VRyELDV 463
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTERAgIAIIHQELalVK-ELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 464 KENIGYGDYKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTQLGktfangiQLSGGQWQRIAIARAYMRRASLYILDEPTA 543
Cdd:PRK13549 100 LENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVG-------NLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502825101 544 ALDpAAEEEVFQDF-QEIAQKSMG-LFISHRYSTVK-YADRIIVLDKGE 589
Cdd:PRK13549 173 SLT-ESETAVLLDIiRDLKAHGIAcIYISHKLNEVKaISDTICVIRDGR 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
389-551 |
2.29e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPqdwqdrISAI----FQDFVRYELDVK 464
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV------AEAChylgHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 465 ENIGYGDYKRSNHLVAIQAAAKRSGaLTMIDSLPDKMdtqlgktfangiqLSGGQWQRIAIARAYMRRASLYILDEPTAA 544
Cdd:PRK13539 92 ENLEFWAAFLGGEELDIAAALEAVG-LAPLAHLPFGY-------------LSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
....*..
gi 502825101 545 LDPAAEE 551
Cdd:PRK13539 158 LDAAAVA 164
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
372-590 |
2.56e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.00 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFkYPGQ--ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIeDYQPqDWQ--D 447
Cdd:COG1101 4 LKNLSKTF-NPGTvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLP-EYKraK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 448 RISAIFQDFVR---YELDVKENIgygdykrsnhlvAIqaAAKR------SGALT--MID-----------SLPDKMDTQL 505
Cdd:COG1101 81 YIGRVFQDPMMgtaPSMTIEENL------------AL--AYRRgkrrglRRGLTkkRRElfrellatlglGLENRLDTKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 506 GktfangiQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKS--MGLFISH--RYStVKYADR 581
Cdd:COG1101 147 G-------LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHnmEQA-LDYGNR 218
|
....*....
gi 502825101 582 IIVLDKGEV 590
Cdd:COG1101 219 LIMMHEGRI 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
372-592 |
2.58e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 98.12 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQeNYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:PRK10522 323 LELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYEldvkENIGYGDYKRSNHLVAIQAAakrsgALTMIDSLpdkmdTQLGKTFANgIQLSGGQWQRIAIARAYMR 531
Cdd:PRK10522 402 VFTDFHLFD----QLLGPEGKPANPALVEKWLE-----RLKMAHKL-----ELEDGRISN-LKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQEIAQKsMG---LFISHRYSTVKYADRIIVLDKGEVAE 592
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLLQE-MGktiFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
372-595 |
2.75e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 95.64 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVS--FKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQD-- 447
Cdd:PRK11153 2 IELKNISkvFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 448 -RISAIFQDFvrYELD---VKENIGYgdykrsnhlvAIQAA-------AKRSGALTMIDSLPDKMDtqlgktfANGIQLS 516
Cdd:PRK11153 82 rQIGMIFQHF--NLLSsrtVFDNVAL----------PLELAgtpkaeiKARVTELLELVGLSDKAD-------RYPAQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 517 GGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGL---FISHRYSTVK-YADRIIVLDKGEVAE 592
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDI-NRELGLtivLITHEMDVVKrICDRVAVIDAGRLVE 221
|
...
gi 502825101 593 YGT 595
Cdd:PRK11153 222 QGT 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
372-600 |
3.55e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.28 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDR--- 448
Cdd:PRK11264 4 IEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGlir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 -----ISAIFQDFVRY-ELDVKENIGYGDykrsnhlvAIQAAAKRSGALTMIDSLPDKMDTQlGKTFANGIQLSGGQWQR 522
Cdd:PRK11264 82 qlrqhVGFVFQNFNLFpHRTVLENIIEGP--------VIVKGEPKEEATARARELLAKVGLA-GKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 523 IAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFI-SHRYSTVK-YADRIIVLDKGEVAEYGTHVELL 600
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIvTHEMSFARdVADRAIFMDQGRIVEQGPAKALF 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
359-618 |
3.59e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.78 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 359 EKTLENVSSTEEGIQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIE 438
Cdd:PRK09452 2 KKLNKQPSSLSPLVELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 439 DYQPQdwQDRISAIFQDFVRY-ELDVKENIGYGdyKRSNHLVAIQAAAKRSGALTMIdslpdkmdtQLgKTFANG--IQL 515
Cdd:PRK09452 80 HVPAE--NRHVNTVFQSYALFpHMTVFENVAFG--LRMQKTPAAEITPRVMEALRMV---------QL-EEFAQRkpHQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 516 SGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGL---FISH-RYSTVKYADRIIVLDKGEVA 591
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKAL-QRKLGItfvFVTHdQEEALTMSDRIVVMRDGRIE 224
|
250 260
....*....|....*....|....*..
gi 502825101 592 EYGTHVElldtngIYARLFNLQAKSYI 618
Cdd:PRK09452 225 QDGTPRE------IYEEPKNLFVARFI 245
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
389-604 |
4.67e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.02 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDyqpqdwqdrisaifqdfvryelDVKENIG 468
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----------------------EDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 469 Y-----GDYKR---SNHLVAI-------QAAAKRSgALTMID--SLPDKMDTQLGKtfangiqLSGGQWQRIAIARAYMR 531
Cdd:COG4152 75 YlpeerGLYPKmkvGEQLVYLarlkglsKAEAKRR-ADEWLErlGLGDRANKKVEE-------LSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQEIAQKsmG---LFISHRYSTV-KYADRIIVLDKGEVAEYGTHVELLDTNG 604
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAK--GttvIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
372-594 |
7.17e-21 |
|
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: 91.19 E-value: 7.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSfKYPGQENyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDyqpqdwqdrisa 451
Cdd:cd03269 1 LEVENVT-KRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 ifqdfvryelDVKENIGY-----GDYKRS------NHLvAIQAAAKRSGALTMIDSLPDKMDtqLGKTFANGI-QLSGGQ 519
Cdd:cd03269 67 ----------AARNRIGYlpeerGLYPKMkvidqlVYL-AQLKGLKKEEARRRIDEWLERLE--LSEYANKRVeELSKGN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 520 WQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQK-SMGLFISHRYSTV-KYADRIIVLDKGEVAEYG 594
Cdd:cd03269 134 QQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
356-609 |
7.89e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 97.74 E-value: 7.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 356 VSEEKTLENVSSTEEG---IQFLNVSFKYPGQ-ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVK-LLTRLYTDYEGII 430
Cdd:PLN03232 596 LSEERILAQNPPLQPGapaISIKNGYFSWDSKtSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSV 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 431 LLNGKRIedYQPQdwqdrISAIFQDFVRyeldvkENIGYG-DYKRSNHLVAIQAAAKRSGaltmIDSLPDKMDTQLGKtf 509
Cdd:PLN03232 676 VIRGSVA--YVPQ-----VSWIFNATVR------ENILFGsDFESERYWRAIDVTALQHD----LDLLPGRDLTEIGE-- 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 510 aNGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQD-FQEIAQKSMGLFISHRYSTVKYADRIIVLDKG 588
Cdd:PLN03232 737 -RGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEG 815
|
250 260
....*....|....*....|.
gi 502825101 589 EVAEYGTHVELLDTNGIYARL 609
Cdd:PLN03232 816 MIKEEGTFAELSKSGSLFKKL 836
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
373-591 |
9.36e-21 |
|
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: 91.18 E-value: 9.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 373 QFLNVSFKYPGQENYT--LKNVNFHIKPGETLALVGSNGSGKSTIVKLLT-RLYTDY--EGIILLNGKRIEdyqPQDWQD 447
Cdd:cd03234 5 PWWDVGLKAKNWNKYAriLNDVSLHVESGQVMAILGSSGSGKTTLLDAISgRVEGGGttSGQILFNGQPRK---PDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 448 RISAIFQD--FVRYeLDVKENIGYGDYKRsnhLVAIQAAAKRSgALTMIDSLPDKMDTQLGKTFANGIqlSGGQWQRIAI 525
Cdd:cd03234 82 CVAYVRQDdiLLPG-LTVRETLTYTAILR---LPRKSSDAIRK-KRVEDVLLRDLALTRIGGNLVKGI--SGGERRRVSI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 526 ARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS-H--RYSTVKYADRIIVLDKGEVA 591
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTiHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
389-551 |
1.10e-20 |
|
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: 90.50 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQdWQDRISAI-FQDFVRYELDVKENI 467
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-PHENILYLgHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 GYgdykrsnhLVAIQAAAKRsgaltMIDSLPDKMD-TQLGKTFANgiQLSGGQWQRIAIARAYMRRASLYILDEPTAALD 546
Cdd:TIGR01189 95 HF--------WAAIHGGAQR-----TIEDALAAVGlTGFEDLPAA--QLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
....*
gi 502825101 547 PAAEE 551
Cdd:TIGR01189 160 KAGVA 164
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
381-570 |
1.17e-20 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 90.17 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 381 YPGqENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIeDYQPQ---DWQDRISAIFQDFV 457
Cdd:TIGR01166 1 YPG-GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKgllERRQRVGLVFQDPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 458 R--YELDVKENIGYGdyKRSNHLVAIQAAAKRSGALTMIDSLP-DKMDTQlgktfangiQLSGGQWQRIAIARAYMRRAS 534
Cdd:TIGR01166 79 DqlFAADVDQDVAFG--PLNLGLSEAEVERRVREALTAVGASGlRERPTH---------CLSGGEKKRVAIAGAVAMRPD 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 502825101 535 LYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS 570
Cdd:TIGR01166 148 VLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVIS 183
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
389-590 |
1.39e-20 |
|
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: 89.41 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQ---------DRIS-AIFQDFvr 458
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragiayvpeDRKReGLVLDL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 459 yelDVKENIgygdykrsnhlvaiqaaakrsgaltmidslpdkmdtqlgktfANGIQLSGGQWQRIAIARAYMRRASLYIL 538
Cdd:cd03215 94 ---SVAENI------------------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502825101 539 DEPTAALDPAAEEEVFQDFQEIAQKSMG-LFISHRYSTVKY-ADRIIVLDKGEV 590
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAvLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
372-594 |
1.39e-20 |
|
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: 90.67 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYP--------------------GQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIIL 431
Cdd:cd03220 1 IELENVSKSYPtykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 432 LNGkriedyqpqdwqdRISAIF--QDFVRYELDVKENIgygdykrsnHLVAIQAAAKRSGALTMIDS------LPDKMDT 503
Cdd:cd03220 81 VRG-------------RVSSLLglGGGFNPELTGRENI---------YLNGRLLGLSRKEIDEKIDEiiefseLGDFIDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 504 QLgKTFANGIQLsggqwqRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQE-IAQKSMGLFISHRYSTVK-YADR 581
Cdd:cd03220 139 PV-KTYSSGMKA------RLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRElLKQGKTVILVSHDPSSIKrLCDR 211
|
250
....*....|...
gi 502825101 582 IIVLDKGEVAEYG 594
Cdd:cd03220 212 ALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
372-600 |
3.93e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.06 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIeDYQPQ---DWQDR 448
Cdd:PRK13636 6 LKVEELNYNYS-DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 ISAIFQ--DFVRYELDVKENIGYGDYKRSNHLVAIQAAAKRSGALTMIDSLPDKmdtqlgKTFAngiqLSGGQWQRIAIA 526
Cdd:PRK13636 84 VGMVFQdpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK------PTHC----LSFGQKKRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502825101 527 RAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGLFI---SHRYSTVK-YADRIIVLDKGEVAEYGTHVELL 600
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEM-QKELGLTIiiaTHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
372-597 |
4.06e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.55 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQD---WQDR 448
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 ISAIFQDF-VRYELDVKENIGY---------GDYKRSnhlvaIQAAAKRSGALTMIDSLPdkmdtqlgktfangIQLSGG 518
Cdd:PRK10908 81 IGMIFQDHhLLMDRTVYDNVAIpliiagasgDDIRRR-----VSAALDKVGLLDKAKNFP--------------IQLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 519 QWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQE---------IAQKSMGLFISHRYstvkyadRIIVLDKGE 589
Cdd:PRK10908 142 EQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEfnrvgvtvlMATHDIGLISRRSY-------RMLTLSDGH 214
|
....*...
gi 502825101 590 VaeYGTHV 597
Cdd:PRK10908 215 L--HGGVG 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
389-591 |
5.81e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.54 E-value: 5.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDW---------QDRIS-AIFQDfvr 458
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAiragiayvpEDRKGeGLVLD--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 459 yeLDVKENIGYGDYKRSNHLVAIQAAAKRSGALTMIDSL---PDKMDTQLGktfangiQLSGGQWQRIAIARAYMRRASL 535
Cdd:COG1129 345 --LSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRLrikTPSPEQPVG-------NLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502825101 536 YILDEPTAALDPAAEEEVFQDFQEIAQKSMG-LFIShryST----VKYADRIIVLDKGEVA 591
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIRELAAEGKAvIVIS---SElpelLGLSDRILVMREGRIV 473
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
271-610 |
5.91e-20 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 94.98 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 271 KMRIDLSFqlisVIFVIFVQFMIVKDTIQGLIAIGSLIAY-------FQ-AVNTTqKTSNELMYMVfnmhqnnlymTQLF 342
Cdd:TIGR01271 1112 QMRIDIIF----VFFFIAVTFIAIGTNQDGEGEVGIILTLamnilstLQwAVNSS-IDVDGLMRSV----------SRVF 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 343 SFLNVPESTDKP-------NVSEEKTLENVSSTEE---GIQFL--NVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGS 410
Cdd:TIGR01271 1177 KFIDLPQEEPRPsggggkyQLSTVLVIENPHAQKCwpsGGQMDvqGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGS 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 411 GKSTIVKLLTRLYTDyEGIILLNGKRIEDYQPQDWQDRISAIFQD-FV-----RYELDVKENigYGDYKrsnhlvaIQAA 484
Cdd:TIGR01271 1257 GKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKvFIfsgtfRKNLDPYEQ--WSDEE-------IWKV 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 485 AKRSGALTMIDSLPDKMDTQLgktFANGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKS 564
Cdd:TIGR01271 1327 AEEVGLKSVIEQFPDKLDFVL---VDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNC 1403
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 502825101 565 MGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYARLF 610
Cdd:TIGR01271 1404 TVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
372-595 |
6.00e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.37 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYP--------------------GQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIIL 431
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 432 LNGkriedyqpqdwqdRISAI------FQDfvryELDVKENIgygdykrsnHLVAIQAAAKRSGALTMIDS------LPD 499
Cdd:COG1134 85 VNG-------------RVSALlelgagFHP----ELTGRENI---------YLNGRLLGLSRKEIDEKFDEivefaeLGD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 500 KMDTQLgKTFANGIQLsggqwqRIAIARAYMRRASLYILDEPTAALDPAaeeevFQD-----FQEIAQKSMG-LFISHRY 573
Cdd:COG1134 139 FIDQPV-KTYSSGMRA------RLAFAVATAVDPDILLVDEVLAVGDAA-----FQKkclarIRELRESGRTvIFVSHSM 206
|
250 260
....*....|....*....|...
gi 502825101 574 STVK-YADRIIVLDKGEVAEYGT 595
Cdd:COG1134 207 GAVRrLCDRAIWLEKGRLVMDGD 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
372-599 |
6.20e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 90.46 E-value: 6.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKY-PGQ--ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILL------NGKRIEDYQP 442
Cdd:PRK13634 3 ITFQKVEHRYqYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 443 qdWQDRISAIFQdFVRYEL---DVKENIGYGDykrSNHLVAIQAAAKRSGALTMIDSLPDKMDTQlgktfaNGIQLSGGQ 519
Cdd:PRK13634 83 --LRKKVGIVFQ-FPEHQLfeeTVEKDICFGP---MNFGVSEEDAKQKAREMIELVGLPEELLAR------SPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 520 WQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMGL---FISHRYSTV-KYADRIIVLDKGEVAEYGT 595
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKL-HKEKGLttvLVTHSMEDAaRYADQIVVMHKGTVFLQGT 229
|
....
gi 502825101 596 HVEL 599
Cdd:PRK13634 230 PREI 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
389-599 |
6.92e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 94.85 E-value: 6.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDFVRYELDVKENI- 467
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVd 1405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 -----GYGDYKRSNHLVAIQ--AAAKRSGaltmIDSlpdkmdtqlgKTFANGIQLSGGQWQRIAIARAYMRRASLYIL-D 539
Cdd:PTZ00243 1406 pfleaSSAEVWAALELVGLRerVASESEG----IDS----------RVLEGGSNYSVGQRQLMCMARALLKKGSGFILmD 1471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 540 EPTAALDPAAEeevfqdfQEIAQKSMGLF-------ISHRYSTVKYADRIIVLDKGEVAEYGTHVEL 599
Cdd:PTZ00243 1472 EATANIDPALD-------RQIQATVMSAFsaytvitIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
372-596 |
7.58e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.30 E-value: 7.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYpgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDrISA 451
Cdd:PRK11124 3 IQLNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKA-IRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQD----FVRYEL----DVKENIgygdykrsnhlvaIQAAAKRSG-----ALTMIDSLPDKMdtQLGKtFANG--IQLS 516
Cdd:PRK11124 80 LRRNvgmvFQQYNLwphlTVQQNL-------------IEAPCRVLGlskdqALARAEKLLERL--RLKP-YADRfpLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 517 GGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFI-SHRYSTV-KYADRIIVLDKGEVAEYG 594
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIvTHEVEVArKTASRVVYMENGHIVEQG 223
|
..
gi 502825101 595 TH 596
Cdd:PRK11124 224 DA 225
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
389-599 |
8.23e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 88.68 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPqdwqDRIsAIFQDFVRYE-LDVKENI 467
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP----DRM-VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 GYG------DYKRSNH---------LVAIQAAAkrsgaltmiDSLPDkmdtqlgktfangiQLSGGQWQRIAIARAYMRR 532
Cdd:TIGR01184 76 ALAvdrvlpDLSKSERraiveehiaLVGLTEAA---------DKRPG--------------QLSGGMKQRVAIARALSIR 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 533 ASLYILDEPTAALDPAAEEEVFQDFQEIAQKS--MGLFISHRY-STVKYADRIIVLDKGEVAEYGTHVEL 599
Cdd:TIGR01184 133 PKVLLLDEPFGALDALTRGNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
385-600 |
8.25e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.26 E-value: 8.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 385 ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQ-------------DRISA 451
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadknqlrllrTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRYE-LDVKENIgygdYKRSNHLVAIQAAAKRSGALTMIDSLpdKMDTQLGKTFAngIQLSGGQWQRIAIARAYM 530
Cdd:PRK10619 97 VFQHFNLWShMTVLENV----MEAPIQVLGLSKQEARERAVKYLAKV--GIDERAQGKYP--VHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIAQ--KSMgLFISHRYSTVKY-ADRIIVLDKGEVAEYGTHVELL 600
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEegKTM-VVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
389-586 |
8.39e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 88.31 E-value: 8.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKST----IVKLLTRLYTdYEGIILLNGKRIEDYQPQdwQDRISAIFQDFVRYE-LDV 463
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTllaaIAGTLSPAFS-ASGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 464 KENIGYG---DYKRSNHLVAIQAAAKRSGALTMIDSLPDkmdtqlgktfangiQLSGGQWQRIAIARAYMRRASLYILDE 540
Cdd:COG4136 94 GENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDPA--------------TLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502825101 541 PTAALDPAAEEEVFQD-FQEIAQKSM-GLFISHRYSTVKYADRIIVLD 586
Cdd:COG4136 160 PFSKLDAALRAQFREFvFEQIRQRGIpALLVTHDEEDAPAAGRVLDLG 207
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
372-595 |
8.94e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 89.66 E-value: 8.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQP-QDWQDRIS 450
Cdd:PRK13644 2 IRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 451 AIFQD----FVRYEldVKENIGYGDYKRSNHLVAIQAAAKRSGAltmidslpdkmDTQLGK-TFANGIQLSGGQWQRIAI 525
Cdd:PRK13644 81 IVFQNpetqFVGRT--VEEDLAFGPENLCLPPIEIRKRVDRALA-----------EIGLEKyRHRSPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502825101 526 ARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGL-FISHRYSTVKYADRIIVLDKGEVAEYGT 595
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIvYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
389-589 |
9.42e-20 |
|
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: 92.97 E-value: 9.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYT--DYEGIILLNGKRIEDYQPQDWQDR-ISAIFQDFVRY-ELDVK 464
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVpELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 465 ENIGYG-DYKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTQlgktfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPTA 543
Cdd:TIGR02633 97 ENIFLGnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTR------PVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502825101 544 ALdPAAEEEVFQDF-QEIAQKSMG-LFISHRYSTVK-YADRIIVLDKGE 589
Cdd:TIGR02633 171 SL-TEKETEILLDIiRDLKAHGVAcVYISHKLNEVKaVCDTICVIRDGQ 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
391-600 |
1.02e-19 |
|
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: 90.93 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 391 NVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGkriedyqpQDWQD------------RISAIFQD--- 455
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG--------EVLQDsargiflpphrrRIGYVFQEarl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 456 FVRyeLDVKENIGYGdYKRSNhlvAIQAAAKRSGALTM--IDSLPDKMDTQLgktfangiqlSGGQWQRIAIARAYMRRA 533
Cdd:COG4148 89 FPH--LSVRGNLLYG-RKRAP---RAERRISFDEVVELlgIGHLLDRRPATL----------SGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502825101 534 SLYILDEPTAALDPAAEEEVFQDFQEIAQKS---MgLFISHRYSTVKY-ADRIIVLDKGEVAEYGTHVELL 600
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELdipI-LYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
389-610 |
1.05e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 91.63 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNG---KRIEDYQPQD-WQDRISAIFQDFVRY-ELDV 463
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREvRRKKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 464 KENIGYGdykrsNHLVAIQAAAKRSGALtmiDSLpdkmdTQLG-KTFANGI--QLSGGQWQRIAIARAYMRRASLYILDE 540
Cdd:PRK10070 124 LDNTAFG-----MELAGINAEERREKAL---DAL-----RQVGlENYAHSYpdELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502825101 541 PTAALDPAAEEEVFQDFQEIAQKSMG--LFISHRY-STVKYADRIIVLDKGEVAEYGTHVELLDTNG-IYARLF 610
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRtiVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAnDYVRTF 264
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
386-602 |
1.56e-19 |
|
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: 90.56 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 386 NYTLKnVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNG-------KRIeDYQPQdwQDRISAIFQDFVR 458
Cdd:TIGR02142 11 DFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGI-FLPPE--KRRIGYVFQEARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 459 Y-ELDVKENIGYGdYKRSNhLVAIQAAAKRSGALTMIDSLPDKMDTQLgktfangiqlSGGQWQRIAIARAYMRRASLYI 537
Cdd:TIGR02142 87 FpHLSVRGNLRYG-MKRAR-PSERRISFERVIELLGIGHLLGRLPGRL----------SGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 538 LDEPTAALDPAAEEEVFQDFQEIAQkSMG---LFISHRYSTV-KYADRIIVLDKGEVAEYGTHVELLDT 602
Cdd:TIGR02142 155 MDEPLAALDDPRKYEILPYLERLHA-EFGipiLYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
376-606 |
1.66e-19 |
|
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: 88.76 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLyTDYEGIILLNGKRIEDYQPQDWQDRISAIFQD 455
Cdd:cd03289 7 DLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKAFGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 456 FVRYELDVKENIG-YGDYKRSNhlvaIQAAAKRSGALTMIDSLPDKMDTQLgktFANGIQLSGGQWQRIAIARAYMRRAS 534
Cdd:cd03289 86 VFIFSGTFRKNLDpYGKWSDEE----IWKVAEEVGLKSVIEQFPGQLDFVL---VDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502825101 535 LYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIY 606
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
389-605 |
1.71e-19 |
|
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: 87.58 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDwqdRISA----------IFQDfvr 458
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE---RARAgiayvpqgreIFPR--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 459 yeLDVKENIgygdykrsnhLVAIQAAAKRSGALtmIDSLPD------KMDTQLGktfanGiQLSGGQWQRIAIARAYMRR 532
Cdd:TIGR03410 90 --LTVEENL----------LTGLAALPRRSRKI--PDEIYElfpvlkEMLGRRG-----G-DLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 533 ASLYILDEPTAALDPAAEEEVFQDFQEIA-QKSMGLFISHRYS--TVKYADRIIVLDKGEVAEYGThVELLDTNGI 605
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLdfARELADRYYVMERGRVVASGA-GDELDEDKV 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
361-600 |
1.86e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.69 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 361 TLENVSSTEEGIQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDY 440
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPGRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 441 QPQDWQDRISAIFQDFVRYE-LDVKENIGYGDYKRSNHLVAIQAA--AKRSGALTMIDSLPdkmdtqlgktFANGI--QL 515
Cdd:PRK10575 79 SSKAFARKVAYLPQQLPAAEgMTVRELVAIGRYPWHGALGRFGAAdrEKVEEAISLVGLKP----------LAHRLvdSL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 516 SGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS--HRYS-TVKYADRIIVLDKGEVAE 592
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIA 228
|
....*...
gi 502825101 593 YGTHVELL 600
Cdd:PRK10575 229 QGTPAELM 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
376-599 |
2.87e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 88.21 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYP-GQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIeDYQPQDW---QDRISA 451
Cdd:PRK13639 6 DLKYSYPdGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQ--DFVRYELDVKENIGYG--DYKRSNHLVA--IQAAAKRSGALTMIDSLPDkmdtqlgktfangiQLSGGQWQRIAI 525
Cdd:PRK13639 83 VFQnpDDQLFAPTVEEDVAFGplNLGLSKEEVEkrVKEALKAVGMEGFENKPPH--------------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 526 ARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS-HRYSTV-KYADRIIVLDKGEVAEYGTHVEL 599
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
389-613 |
2.92e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.59 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTivkLLTRL--YTDYEGIILLNGKRIEDYQPQDwQDRISAIF--QDFVRYELDVK 464
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAE-LARHRAYLsqQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 465 ENIGYGDYKRSNHLVAIQAAAKRSGALtmidSLPDKMDTQLGktfangiQLSGGQWQRIAIARAYMR-------RASLYI 537
Cdd:COG4138 88 QYLALHQPAGASSEAVEQLLAQLAEAL----GLEDKLSRPLT-------QLSGGEWQRVRLAAVLLQvwptinpEGQLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 538 LDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS-----HrysTVKYADRIIVLDKGEVAEYGTHVELLDTNGIyARLFNL 612
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCQQGITVVMSshdlnH---TLRHADRVWLLKQGKLVASGETAEVMTPENL-SEVFGV 232
|
.
gi 502825101 613 Q 613
Cdd:COG4138 233 K 233
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
404-599 |
3.55e-19 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 89.09 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 404 LVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQdwQDRISAIFQDFVRY-ELDVKENIGYGdyKRSNHLVAIQ 482
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFpHMTVEENVAFG--LKMRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 483 AAAKRSGALTMIdslpdkmdtQLGkTFANG--IQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEI 560
Cdd:TIGR01187 77 IKPRVLEALRLV---------QLE-EFADRkpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502825101 561 aQKSMGL---FISHRYS-TVKYADRIIVLDKGEVAEYGTHVEL 599
Cdd:TIGR01187 147 -QEQLGItfvFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
379-594 |
3.68e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.76 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 379 FKYpgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIeDYQPQDW---QDRISAIFQD 455
Cdd:PRK13638 9 FRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLlalRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 456 FVR--YELDVKENIGYgdyKRSNHLVAIQAAAKR-SGALTMIDSlpdkmdtqlgKTFANG-IQ-LSGGQWQRIAIARAYM 530
Cdd:PRK13638 86 PEQqiFYTDIDSDIAF---SLRNLGVPEAEITRRvDEALTLVDA----------QHFRHQpIQcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKY--ADRIIVLDKGEVAEYG 594
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYeiSDAVYVLRQGQILTHG 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
390-599 |
4.62e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 89.32 E-value: 4.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 390 KNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDwqdR-ISAIFQDFVRY-ELDVKENI 467
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---RgVGMVFQSYALYpHLSVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 GYG----------DYKRSNHLVAI-QAAAkrsgaltMIDSLPDkmdtqlgktfangiQLSGGQWQRIAIARAYMRRASLY 536
Cdd:PRK11000 97 SFGlklagakkeeINQRVNQVAEVlQLAH-------LLDRKPK--------------ALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 537 ILDEPTAALDPAAEeevFQDFQEIA--QKSMG---LFISH-RYSTVKYADRIIVLDKGEVAEYGTHVEL 599
Cdd:PRK11000 156 LLDEPLSNLDAALR---VQMRIEISrlHKRLGrtmIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
372-588 |
4.66e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.61 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQD-WQDRIS 450
Cdd:PRK09700 6 ISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 451 AIFQDF-VRYELDVKENIGYGDY--KRSNHLVAIQAAAKRSGALTMIDSLPDKMDtqLGKTFANgiqLSGGQWQRIAIAR 527
Cdd:PRK09700 84 IIYQELsVIDELTVLENLYIGRHltKKVCGVNIIDWREMRVRAAMMLLRVGLKVD--LDEKVAN---LSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 528 AYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGL-FISHRYSTVK-YADRIIVLDKG 588
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIvYISHKLAEIRrICDRYTVMKDG 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
389-599 |
4.76e-19 |
|
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: 91.90 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGkRIEdYQPQdwqdrISAIFQDfvryelDVKENIG 468
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-RIS-FSPQ-----TSWIMPG------TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 469 YG-DYKRSNHLVAIQAAAKRSGaltmIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDP 547
Cdd:TIGR01271 509 FGlSYDEYRYTSVIKACQLEED----IALFPEKDKTVLGE---GGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502825101 548 AAEEEVFQD-FQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVEL 599
Cdd:TIGR01271 582 VTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
372-600 |
5.29e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 86.47 E-value: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:PRK11614 6 LSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRY--ELDVKENIGYGDYkrsnhlvaiqaAAKRSGALTMIDSLPDKMDTQLGKTFANGIQLSGGQWQRIAIARAY 529
Cdd:PRK11614 84 IVPEGRRVfsRMTVEENLAMGGF-----------FAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 530 MRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYS--TVKYADRIIVLDKGEVAEYGTHVELL 600
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
389-600 |
5.68e-19 |
|
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: 86.44 E-value: 5.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIED------------YQPQDwqdriSAIFQDf 456
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmhkrarlgigYLPQE-----ASIFRK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 457 vryeLDVKENIGygdykrsnhLVAIQAAAKRSGALTMIDSLPDkmDTQLGKTFAN-GIQLSGGQWQRIAIARAYMRRASL 535
Cdd:cd03218 90 ----LTVEENIL---------AVLEIRGLSKKEREEKLEELLE--EFHITHLRKSkASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 536 YILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS-HRYS-TVKYADRIIVLDKGEVAEYGTHVELL 600
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
376-599 |
6.36e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.12 E-value: 6.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQenYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPqdWQDRISAIFQD 455
Cdd:PRK11607 24 NLTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 456 FVRY-ELDVKENIGYGdyKRSNHLVAIQAAAKRSGALTMIDSlpdkmdtqlgKTFANGI--QLSGGQWQRIAIARAYMRR 532
Cdd:PRK11607 100 YALFpHMTVEQNIAFG--LKQDKLPKAEIASRVNEMLGLVHM----------QEFAKRKphQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 533 ASLYILDEPTAALDPAAEEEVFQDFQEIAQK--SMGLFISH-RYSTVKYADRIIVLDKGEVAEYGTHVEL 599
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
389-571 |
7.96e-19 |
|
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: 85.24 E-value: 7.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGkRIEDYQPQDWQDRISAI-FQDFVRYELDVKENI 467
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG-GPLDFQRDSIARGLLYLgHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 GYgdYKRSNHLVAIQAAAKRSGaLTMIDSLPdkmdtqlgktFAngiQLSGGQWQRIAIARAYMRRASLYILDEPTAALDP 547
Cdd:cd03231 95 RF--WHADHSDEQVEEALARVG-LNGFEDRP----------VA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|....*
gi 502825101 548 AAEEEVFQDF-QEIAQKSMGLFISH 571
Cdd:cd03231 159 AGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
372-595 |
1.04e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.81 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKY-PGQ--ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIE----DYQPQD 444
Cdd:PRK13641 3 IKFENVDYIYsPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 445 WQDRISAIFQdFVRYEL-------DVK---ENIGYGDYKrsnhlvAIQAAAKRSGALTMIDSLPDKmdtqlgktfaNGIQ 514
Cdd:PRK13641 83 LRKKVSLVFQ-FPEAQLfentvlkDVEfgpKNFGFSEDE------AKEKALKWLKKVGLSEDLISK----------SPFE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 515 LSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaQKS--MGLFISHRYSTV-KYADRIIVLDKGEVA 591
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAghTVILVTHNMDDVaEYADDVLVLEHGKLI 224
|
....
gi 502825101 592 EYGT 595
Cdd:PRK13641 225 KHAS 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
376-593 |
1.06e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLnGKRIE-DYQPQDwqdrisaifQ 454
Cdd:COG0488 320 GLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKiGYFDQH---------Q 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 455 DFVRYELDVKENI-GYGDYKRSNHLVAIqaaakrsgaltmidsL------PDKMDTQLGKtfangiqLSGGQWQRIAIAR 527
Cdd:COG0488 388 EELDPDKTVLDELrDGAPGGTEQEVRGY---------------LgrflfsGDDAFKPVGV-------LSGGEKARLALAK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502825101 528 AYMRRASLYILDEPTAALDPA---AEEEVFQDFQeiaqksmG--LFISH-RY--STVkyADRIIVLDKGEVAEY 593
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIEtleALEEALDDFP-------GtvLLVSHdRYflDRV--ATRILEFEDGGVREY 510
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
396-595 |
1.22e-18 |
|
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: 85.54 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 396 IKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEdYQPQdwqdRISAIFQDFVRYELDVKENIGYGD-YKR 474
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQ----YIKADYEGTVRDLLSSITKDFYTHpYFK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 475 SNHLVAIQaaakrsgaltmIDSLpdkMDTQLgktfangIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDpaAEE--- 551
Cdd:cd03237 97 TEIAKPLQ-----------IEQI---LDREV-------PELSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQrlm 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502825101 552 --EVFQDFQEIAQKSMgLFISHRYSTVKY-ADRIIVLDkGEVAEYGT 595
Cdd:cd03237 154 asKVIRRFAENNEKTA-FVVEHDIIMIDYlADRLIVFE-GEPSVNGV 198
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
389-600 |
1.49e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 86.00 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIE--DYQPQdwQDRISAIFQDfVRYELDVKEN 466
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYR--SQRIRMIFQD-PSTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 467 IG-YGDYK-RSNHLVAIQAAAKR-SGALTMIDSLPDKmdtqlgktfANGI--QLSGGQWQRIAIARAYMRRASLYILDEP 541
Cdd:PRK15112 106 ISqILDFPlRLNTDLEPEQREKQiIETLRQVGLLPDH---------ASYYphMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 542 TAALDPAAEEEVFQDFQEIAQKSMglfISHRYST-----VKY-ADRIIVLDKGEVAEYGTHVELL 600
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQG---ISYIYVTqhlgmMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
372-600 |
1.86e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 90.18 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 I------FQDFVRYELDvkeniGYGDYKRSNhlvaIQAAAKRSGALTMIDSLPDKMDTQLgktFANGIQLSGGQWQRIAI 525
Cdd:PLN03130 1318 IpqapvlFSGTVRFNLD-----PFNEHNDAD----LWESLERAHLKDVIRRNSLGLDAEV---SEAGENFSVGQRQLLSL 1385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 526 ARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELL 600
Cdd:PLN03130 1386 ARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
376-593 |
1.90e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEG-IILLNGKRIEdYQPQD---WQDR--I 449
Cdd:COG0488 3 NLSKSFGGRP--LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGeVSIPKGLRIG-YLPQEpplDDDLtvL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 450 SAIFQDFVRY--------ELDVKENIGYGDYKR----SNHLVAIQAAAKRSGALTMIDSL---PDKMDTQLGktfangiQ 514
Cdd:COG0488 80 DTVLDGDAELraleaeleELEAKLAEPDEDLERlaelQEEFEALGGWEAEARAEEILSGLgfpEEDLDRPVS-------E 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 515 LSGGQWQRIAIARAYMRRASLYILDEPTAALD-PAAE--EEVFQDFqeiaQKSMgLFISH-RY--STVkyADRIIVLDKG 588
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDlESIEwlEEFLKNY----PGTV-LVVSHdRYflDRV--ATRILELDRG 225
|
....*
gi 502825101 589 EVAEY 593
Cdd:COG0488 226 KLTLY 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
389-594 |
2.65e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.96 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDY-----EGIILLNGKRIEDYQPQDWQDRISAIFQ-DFVRYELD 462
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 463 VKENIGYGdyKRSNHLVAIQAA--AKRSGAL---TMIDSLPDKMDTQLGKtfangiqLSGGQWQRIAIARAYMRRASLYI 537
Cdd:PRK14247 99 IFENVALG--LKLNRLVKSKKElqERVRWALekaQLWDEVKDRLDAPAGK-------LSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 538 LDEPTAALDPAAEEEVFQDFQEIaQKSMGLFISHRY--STVKYADRIIVLDKGEVAEYG 594
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFpqQAARISDYVAFLYKGQIVEWG 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
381-585 |
2.69e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.05 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 381 YPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQdwQDRISAIFqdfvryE 460
Cdd:NF040873 2 YGGRP--VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--RSEVPDSL------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 461 LDVKENIGYGDYKRSNHLVAIQAAAKR--SGALTMIDsLPDKMDTQLGktfangiQLSGGQWQRIAIARAYMRRASLYIL 538
Cdd:NF040873 72 LTVRDLVAMGRWARRGLWRRLTRDDRAavDDALERVG-LADLAGRQLG-------ELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502825101 539 DEPTAALDPAAEEEVFQDFQEIAQKSMG-LFISHRYSTVKYADRIIVL 585
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATvVVVTHDLELVRRADPCVLL 191
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
375-595 |
4.46e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.99 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 375 LNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGII-----LL---NGKRIEDYQPQDWQ 446
Cdd:PRK10261 18 LNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLrrrSRQVIELSEQSAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 447 DR------ISAIFQD--------FVRYElDVKENIGYgdYKRSNHLVAIqAAAKRsgaltMIDS--LPDKmDTQLGKtFA 510
Cdd:PRK10261 98 MRhvrgadMAMIFQEpmtslnpvFTVGE-QIAESIRL--HQGASREEAM-VEAKR-----MLDQvrIPEA-QTILSR-YP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 511 NgiQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQK-SMG-LFISHRYSTV-KYADRIIVLDK 587
Cdd:PRK10261 167 H--QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGvIFITHDMGVVaEIADRVLVMYQ 244
|
....*...
gi 502825101 588 GEVAEYGT 595
Cdd:PRK10261 245 GEAVETGS 252
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
368-618 |
8.97e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.29 E-value: 8.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 368 TEEGIQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRL-----YTDYEGIILLNGKRIedYQP 442
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI--YSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 443 Q----DWQDRISAIFQDFVRYELDVKENIGYG-------DYKRSNHLV--AIQAAAkrsgaltMIDSLPDKM-DTQLGkt 508
Cdd:PRK14239 78 RtdtvDLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgikDKQVLDEAVekSLKGAS-------IWDEVKDRLhDSALG-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 509 fangiqLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTV-KYADRIIVLDK 587
Cdd:PRK14239 149 ------LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLD 222
|
250 260 270
....*....|....*....|....*....|.
gi 502825101 588 GEVAEYGthvellDTNGIYARLFNLQAKSYI 618
Cdd:PRK14239 223 GDLIEYN------DTKQMFMNPKHKETEDYI 247
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
373-603 |
9.53e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 9.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 373 QFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGkriedyQPQDWQDRISA- 451
Cdd:PRK11288 6 SFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG------QEMRFASTTAAl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 ------IFQD--FVRyELDVKENIGYGDYKRSNHLVAIQAAAKRsgALTMIDSLPDKMD--TQLGKtfangiqLSGGQWQ 521
Cdd:PRK11288 78 aagvaiIYQElhLVP-EMTVAENLYLGQLPHKGGIVNRRLLNYE--AREQLEHLGVDIDpdTPLKY-------LSIGQRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 522 RIAIARAYMRRASLYILDEPTAALDpAAEEEVFqdFQEIAQ-KSMG---LFISHRYSTVkYA--DRIIVLDKGEVAEygT 595
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLS-AREIEQL--FRVIRElRAEGrviLYVSHRMEEI-FAlcDAITVFKDGRYVA--T 221
|
....*...
gi 502825101 596 HVELLDTN 603
Cdd:PRK11288 222 FDDMAQVD 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
376-600 |
9.89e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.90 E-value: 9.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQ---ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILL-------NGKRIEDYQpqDW 445
Cdd:PRK13645 11 NVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipaNLKKIKEVK--RL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 446 QDRISAIFQdFVRYEL---DVKENIGYGDYkrsnHLVA-IQAAAKRSGALTMIDSLPDKMDTQlgktfaNGIQLSGGQWQ 521
Cdd:PRK13645 89 RKEIGLVFQ-FPEYQLfqeTIEKDIAFGPV----NLGEnKQEAYKKVPELLKLVQLPEDYVKR------SPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 522 RIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEI--AQKSMGLFISHRYSTV-KYADRIIVLDKGEVAEYGTHVE 598
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFE 237
|
..
gi 502825101 599 LL 600
Cdd:PRK13645 238 IF 239
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
392-615 |
1.25e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.67 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 392 VNFHIKPGETLALVGSNGSGKSTivkLLTRL--YTDYEGIILLNGKRIEDYQPQDwQDRISAIF--QDFVRYELDVKENI 467
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAE-LARHRAYLsqQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 gygdykrSNHLVAIQAAAKRSGALTMIDS---LPDKMDTQLGktfangiQLSGGQWQRIAIARAYMR-------RASLYI 537
Cdd:PRK03695 91 -------TLHQPDKTRTEAVASALNEVAEalgLDDKLGRSVN-------QLSGGEWQRVRLAAVVLQvwpdinpAGQLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 538 LDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS-----HrysTVKYADRIIVLDKGEVAEYGTHVELLDTNGIyARLFNL 612
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSshdlnH---TLRHADRVWLLKQGKLLASGRRDEVLTPENL-AQVFGV 232
|
...
gi 502825101 613 QAK 615
Cdd:PRK03695 233 NFR 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
389-595 |
1.26e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 84.75 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDwqDRISAIFQDFVRYE-LDVKENI 467
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRhMTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 GYG-----DYKRSNhlvaiqAAAKRSGALTMIDSLpdkmdtQLGKtFANGI--QLSGGQWQRIAIARAYMRRASLYILDE 540
Cdd:PRK10851 96 AFGltvlpRRERPN------AAAIKAKVTQLLEMV------QLAH-LADRYpaQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502825101 541 PTAALDPAAEEEVFQDFQEIAQ--KSMGLFISH-RYSTVKYADRIIVLDKGEVAEYGT 595
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
383-613 |
1.37e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.11 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 383 GQENYTL-KNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDFVRY-E 460
Cdd:PRK10253 16 GYGKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPgD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 461 LDVKENIGYGDYK--------RSNHLVAIQAAAKRSGaltmIDSLPDK-MDTqlgktfangiqLSGGQWQRIAIARAYMR 531
Cdd:PRK10253 96 ITVQELVARGRYPhqplftrwRKEDEEAVTKAMQATG----ITHLADQsVDT-----------LSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQEIAQK---SMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLdTNGIYAR 608
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREkgyTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV-TAELIER 239
|
....*
gi 502825101 609 LFNLQ 613
Cdd:PRK10253 240 IYGLR 244
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
371-618 |
2.50e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.39 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 371 GIQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLyTDYEGIILLNGkRIEDYQPQDWQDRI- 449
Cdd:PRK14258 7 AIKVNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEG-RVEFFNQNIYERRVn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 450 --------SAIFQDFVRYELDVKENIGYGdykrsNHLVAIQAAAKRSGALTMIDSLPDKMDTQLGKTFANGIQLSGGQWQ 521
Cdd:PRK14258 83 lnrlrrqvSMVHPKPNLFPMSVYDNVAYG-----VKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 522 RIAIARAYMRRASLYILDEPTAALDPAAE---EEVFQDFQEIAQKSMgLFISHRYSTVKYADRIIVLDKGEVAEYGTHVE 598
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLRLRSELTM-VIVSHNLHQVSRLSDFTAFFKGNENRIGQLVE 236
|
250 260
....*....|....*....|
gi 502825101 599 LLDTNGIYARLFNLQAKSYI 618
Cdd:PRK14258 237 FGLTKKIFNSPHDSRTREYV 256
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
365-590 |
2.71e-17 |
|
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: 81.61 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 365 VSSTEEG-IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQ 443
Cdd:cd03267 12 VYSKEPGlIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 444 dWQDRISAIF--QDFVRYELDVKEniGYGDYKRSNHLVAIQAAAKRSGALTMIDsLPDKMDTQLGktfangiQLSGGQWQ 521
Cdd:cd03267 92 -FLRRIGVVFgqKTQLWWDLPVID--SFYLLAAIYDLPPARFKKRLDELSELLD-LEELLDTPVR-------QLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 522 RIAIARAYMRRASLYILDEPTAALDPAAEEEVfQDFQEIAQKSMG---LFISHRYSTV-KYADRIIVLDKGEV 590
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENI-RNFLKEYNRERGttvLLTSHYMKDIeALARRVLVIDKGRL 232
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
389-592 |
3.11e-17 |
|
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: 81.33 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRI----EDYQPQDWQDRISAIFQDFvryeldvk 464
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldEDARARLRARHVGFVFQSF-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 465 enigygdykrsnHL---------VAIQA-------AAKRsgALTMIDS--LPDKMDTQLGktfangiQLSGGQWQRIAIA 526
Cdd:COG4181 100 ------------QLlptltalenVMLPLelagrrdARAR--ARALLERvgLGHRLDHYPA-------QLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 527 RAYMRRASLYILDEPTAALDpAAEEEVFQD--FQEIAQKSMGLFI-SHRYSTVKYADRIIVLDKGEVAE 592
Cdd:COG4181 159 RAFATEPAILFADEPTGNLD-AATGEQIIDllFELNRERGTTLVLvTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
372-601 |
3.14e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.34 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQenYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDyQPQDWQDRISA 451
Cdd:PRK13536 42 IDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQ-DFVRYELDVKEN-IGYGDYKRSnHLVAIQAAAKrsgALTMIDSLPDKMDTQLGktfangiQLSGGQWQRIAIARAY 529
Cdd:PRK13536 119 VPQfDNLDLEFTVRENlLVFGRYFGM-STREIEAVIP---SLLEFARLESKADARVS-------DLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 530 MRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRY--STVKYADRIIVLDKG-EVAEYGTHvELLD 601
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFmeEAERLCDRLCVLEAGrKIAEGRPH-ALID 261
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
372-599 |
3.37e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.52 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENY---TLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRI----EDYQPQD 444
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 445 WQDRISAIFQ--DFVRYELDVKENIGYGDykrSNHLVAIQAAAKRSGALTMidslpdkmdtQLGktFANGI------QLS 516
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGP---KNFKMNLDEVKNYAHRLLM----------DLG--FSRDVmsqspfQMS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 517 GGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEV---FQDFQEIAQKSMgLFISHRYSTV-KYADRIIVLDKGEVAE 592
Cdd:PRK13646 148 GGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVmrlLKSLQTDENKTI-ILVSHDMNEVaRYADEVIVMKEGSIVS 226
|
....*..
gi 502825101 593 YGTHVEL 599
Cdd:PRK13646 227 QTSPKEL 233
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
376-590 |
4.29e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.16 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQENYT--LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDW----QDRI 449
Cdd:PRK10535 9 DIRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 450 SAIFQdfvRYELdvkenigygdykrSNHLVAIQ--------------AAAKRSGALTMIDSLPDKMDTQLGktfangiQL 515
Cdd:PRK10535 89 GFIFQ---RYHL-------------LSHLTAAQnvevpavyaglerkQRLLRAQELLQRLGLEDRVEYQPS-------QL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 516 SGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFI-SHRYSTVKYADRIIVLDKGEV 590
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIvTHDPQVAAQAERVIEIRDGEI 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
372-595 |
4.34e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.09 E-value: 4.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYT---LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEG------IILLNGKRIEDYQP 442
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 443 QdwQDRISAIFQ--DFVRYELDVKENIGYGDykrSNHLVAIQAAAKRSG-ALTMIDslpdkmdtqLGKTF--ANGIQLSG 517
Cdd:PRK13643 82 V--RKKVGVVFQfpESQLFEETVLKDVAFGP---QNFGIPKEKAEKIAAeKLEMVG---------LADEFweKSPFELSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 518 GQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMG-LFISHRYSTV-KYADRIIVLDKGEVAEYGT 595
Cdd:PRK13643 148 GQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTvVLVTHLMDDVaDYADYVYLLEKGHIISCGT 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
371-608 |
5.55e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 82.97 E-value: 5.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 371 GIQFLNVSFKYPGqENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPqdwQDR-I 449
Cdd:PRK11650 3 GLKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---ADRdI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 450 SAIFQDFVRY-ELDVKENIGYGDYKR--SNHLVA--IQAAAKRSGALTMIDSLPDkmdtqlgktfangiQLSGGQWQRIA 524
Cdd:PRK11650 79 AMVFQNYALYpHMSVRENMAYGLKIRgmPKAEIEerVAEAARILELEPLLDRKPR--------------ELSGGQRQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 525 IARAYMRRASLYILDEPTAALDpaAEEEVfQDFQEIA--QKSMG---LFISH-RYSTVKYADRIIVLDKGEVAEYGTHVE 598
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLD--AKLRV-QMRLEIQrlHRRLKttsLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVE 221
|
250
....*....|
gi 502825101 599 lldtngIYAR 608
Cdd:PRK11650 222 ------VYEK 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
341-592 |
1.32e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.32 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 341 LFSFLNVPESTDKPNVSEEKTlenVSSTEEGIQFLNVSFKYPgqeNYT--LKNVNFHIKPGETLALVGSNGSGKSTIVKL 418
Cdd:COG4178 335 LAGFEEALEAADALPEAASRI---ETSEDGALALEDLTLRTP---DGRplLEDLSLSLKPGERLLITGPSGSGKSTLLRA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 419 LTRLYTDYEG-IILLNGKRI-----EDYQPQDwqdrisaifqdfvryelDVKENIGYGDYKRSNHLVAIQAAAKRSGalt 492
Cdd:COG4178 409 IAGLWPYGSGrIARPAGARVlflpqRPYLPLG-----------------TLREALLYPATAEAFSDAELREALEAVG--- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 493 mIDSLPDKMDTQlgktfAN-GIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISH 571
Cdd:COG4178 469 -LGHLAERLDEE-----ADwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
250 260
....*....|....*....|.
gi 502825101 572 RYSTVKYADRIIVLDKGEVAE 592
Cdd:COG4178 543 RSTLAAFHDRVLELTGDGSWQ 563
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
376-549 |
1.34e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.08 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYpgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLY-----TDYEGIILLNGKRIedYQPQdwQD--- 447
Cdd:COG1117 16 NLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDI--YDPD--VDvve 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 448 ---RISAIFQdfvryeldvK---------ENIGYG-----DYKRSN--HLV--AIQAAAkrsgaltmidsLPDKMDTQLG 506
Cdd:COG1117 90 lrrRVGMVFQ---------KpnpfpksiyDNVAYGlrlhgIKSKSEldEIVeeSLRKAA-----------LWDEVKDRLK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502825101 507 KtfaNGIQLSGGQWQRIAIARAymrraslyI--------LDEPTAALDPAA 549
Cdd:COG1117 150 K---SALGLSGGQQQRLCIARA--------LavepevllMDEPTSALDPIS 189
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
372-581 |
1.51e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.47 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYpgQE----NYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQD 447
Cdd:PRK11629 6 LQCDNLCKRY--QEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 448 ----RISAIFQ------DFVRYElDVKENIGYGDYKRSnhlvaiQAAAKrsgALTMIDSLPDKMDTQLGKTfangiQLSG 517
Cdd:PRK11629 84 lrnqKLGFIYQfhhllpDFTALE-NVAMPLLIGKKKPA------EINSR---ALEMLAAVGLEHRANHRPS-----ELSG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 518 GQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEI--AQKSMGLFISHRYSTVKYADR 581
Cdd:PRK11629 149 GERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSR 214
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
375-580 |
1.93e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 78.07 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 375 LNVSFKYpgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEdyqpqdwQDRisAIFQ 454
Cdd:PRK13540 5 IELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-------KDL--CTYQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 455 D---FVRYELDVKENIGYgdykRSNHLVAIQAAAKRSG--ALTMIDSLPDKMDtqlgktFANGIqLSGGQWQRIAIARAY 529
Cdd:PRK13540 74 KqlcFVGHRSGINPYLTL----RENCLYDIHFSPGAVGitELCRLFSLEHLID------YPCGL-LSSGQKRQVALLRLW 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502825101 530 MRRASLYILDEPTAALDPAAEEEVFQDFQE-IAQKSMGLFISHRYSTVKYAD 580
Cdd:PRK13540 143 MSKAKLWLLDEPLVALDELSLLTIITKIQEhRAKGGAVLLTSHQDLPLNKAD 194
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
389-601 |
2.68e-16 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 79.07 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIE-------DYQPQDWQD------RISAIFQD 455
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgELVPADRRQlqrirtRLGMVFQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 456 FVRY-ELDVKENIGYGDYkrsnHLVAIQAAAKRSGALTMID--SLPDKMDtqlgktfANGIQLSGGQWQRIAIARAYMRR 532
Cdd:COG4598 104 FNLWsHMTVLENVIEAPV----HVLGRPKAEAIERAEALLAkvGLADKRD-------AYPAHLSGGQQQRAAIARALAME 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 533 ASLYILDEPTAALDPAAEEEVFQDFQEIAQ--KSMgLFISHRystVKYA----DRIIVLDKGEVAEYGTHVELLD 601
Cdd:COG4598 173 PEVMLFDEPTSALDPELVGEVLKVMRDLAEegRTM-LVVTHE---MGFArdvsSHVVFLHQGRIEEQGPPAEVFG 243
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
372-602 |
3.67e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.46 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYpgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQdRISA 451
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQ-RVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQ-DFVRYELDVKENIGYgdYKRSNHLVAIQAAAKRSGALTMIdSLPDKMDTQLGktfangiQLSGGQWQRIAIARAYM 530
Cdd:PRK13537 85 VPQfDNLDPDFTVRENLLV--FGRYFGLSAAAARALVPPLLEFA-KLENKADAKVG-------ELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRY--STVKYADRIIVLDKG-EVAEYGTHvELLDT 602
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFmeEAERLCDRLCVIEEGrKIAEGAPH-ALIES 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
386-599 |
3.71e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 80.15 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 386 NYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGkriEDYQPQDWQDR-ISAIFQDFVRY-ELDV 463
Cdd:PRK11432 19 NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRdICMVFQSYALFpHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 464 KENIGYGDYKRSNHLVAIQAAAKRSGALTMIDSLPDK-MDtqlgktfangiQLSGGQWQRIAIARAYMRRASLYILDEPT 542
Cdd:PRK11432 96 GENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRyVD-----------QISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502825101 543 AALDPAAEEEVFQDFQEIaQKSMG---LFISHRYS-TVKYADRIIVLDKGEVAEYGTHVEL 599
Cdd:PRK11432 165 SNLDANLRRSMREKIREL-QQQFNitsLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
389-601 |
4.28e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.63 E-value: 4.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLT-RLYTD--YEGIILLNGKRIEDYQpqdwQDRISA-IFQD--FVRyELD 462
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfRSPKGvkGSGSVLLNGMPIDAKE----MRAISAyVQQDdlFIP-TLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 463 VKENIGY-GDYKRSNHLVAIQAAAKRSGALTMIdSLPDKMDTQLGkTFANGIQLSGGQWQRIAIARAYMRRASLYILDEP 541
Cdd:TIGR00955 116 VREHLMFqAHLRMPRRVTKKEKRERVDEVLQAL-GLRKCANTRIG-VPGRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 542 TAALDPAAEEEVFQDFQEIAQKSMGLFIS-HRYSTVKYA--DRIIVLDKGEVAEYGTHVELLD 601
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSELFElfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
389-589 |
4.40e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.20 E-value: 4.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDR-ISAIFQDF-VRYELDVKEN 466
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELnLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 467 IGYGDYKRsNHLVAIQAAAKRSGAltmidslpDKMDTQLGKTFANGI---QLSGGQWQRIAIARAYMRRASLYILDEPTA 543
Cdd:PRK10762 100 IFLGREFV-NRFGRIDWKKMYAEA--------DKLLARLNLRFSSDKlvgELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502825101 544 ALDPAAEEEVFQDFQEIAQKSMGL-FISHRYSTV-KYADRIIVLDKGE 589
Cdd:PRK10762 171 ALTDTETESLFRVIRELKSQGRGIvYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
376-571 |
6.12e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 77.98 E-value: 6.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPG--QENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEdyQPQdwQDRiSAIF 453
Cdd:COG4525 8 HVSVRYPGggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPG--ADR-GVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 454 QDFVRYE-LDVKENIGYG----------DYKRSNH---LVAIQAAAKRsgaltMIDslpdkmdtqlgktfangiQLSGGQ 519
Cdd:COG4525 83 QKDALLPwLNVLDNVAFGlrlrgvpkaeRRARAEEllaLVGLADFARR-----RIW------------------QLSGGM 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502825101 520 WQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKS--MGLFISH 571
Cdd:COG4525 140 RQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITH 193
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
389-590 |
6.15e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 6.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDR-ISAIFQDFVR----YELDV 463
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgIVYISEDRKRdglvLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 464 KENIGYGDYKR-SNHLVAIQAAAKRSGALTMIDSLPDK---MDTQLGKtfangiqLSGGQWQRIAIARAYMRRASLYILD 539
Cdd:PRK10762 348 KENMSLTALRYfSRAGGSLKHADEQQAVSDFIRLFNIKtpsMEQAIGL-------LSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502825101 540 EPTAALDPAAEEEVFQDFQEIAQKSMGLFI--SHRYSTVKYADRIIVLDKGEV 590
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAEGLSIILvsSEMPEVLGMSDRILVMHEGRI 473
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
372-599 |
6.40e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.31 E-value: 6.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQ--DFVRYELDVKENIGYG------DYKRSNHLVaiQAAAKRSGALTMIDSLPDkmdtqlgktfangiQLSGGQWQRI 523
Cdd:PRK13652 83 VFQnpDDQIFSPTVEQDIAFGpinlglDEETVAHRV--SSALHMLGLEELRDRVPH--------------HLSGGEKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 524 AIARAYMRRASLYILDEPTAALDPAAEEEVFqDFQEIAQKSMGL---FISHRYSTV-KYADRIIVLDKGEVAEYGTHVEL 599
Cdd:PRK13652 147 AIAGVIAMEPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETYGMtviFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
388-588 |
9.86e-16 |
|
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: 76.60 E-value: 9.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 388 TLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGK--RIEDYQPQDWQDRISAIFQDFVRYELD--V 463
Cdd:cd03290 16 TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKneSEPSFEATRSRNRYSVAYAAQKPWLLNatV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 464 KENIGYGD-YKRSNHLVAIQAAAKRSGaltmIDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPT 542
Cdd:cd03290 96 EENITFGSpFNKQRYKAVTDACSLQPD----IDLLPFGDQTEIGE---RGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502825101 543 AALDPAAEEEVFQD-----FQEiaQKSMGLFISHRYSTVKYADRIIVLDKG 588
Cdd:cd03290 169 SALDIHLSDHLMQEgilkfLQD--DKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
362-571 |
1.02e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.51 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 362 LENVSSTEEGIQFLNVSFKYpgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLyTDY------EGIILLNGK 435
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRL-NDLipgfrvEGKVTFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 436 RIEDYQ--PQDWQDRISAIFQDFVRYELDVKENIGYG----DYKRS-NHLVAiqaAAKRSGALTmiDSLPDKMDTqlgkt 508
Cdd:PRK14243 78 NLYAPDvdPVEVRRRIGMVFQKPNPFPKSIYDNIAYGarinGYKGDmDELVE---RSLRQAALW--DEVKDKLKQ----- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 509 faNGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISH 571
Cdd:PRK14243 148 --SGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
389-601 |
1.23e-15 |
|
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: 75.64 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRL--YTDYEGIILLNGKRIEDYQPQD---------WQD--RISAI-FQ 454
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEErarlgiflaFQYppEIPGVkNA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 455 DFVRYeldvkenIGYGdykrsnhlvaiqaaakrsgaltmidslpdkmdtqlgktfangiqLSGGQWQRIAIARAYMRRAS 534
Cdd:cd03217 96 DFLRY-------VNEG--------------------------------------------FSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 535 LYILDEPTAALDPAAEEEVFQDFQEIAQKSMG-LFISHRYSTVKY--ADRIIVLDKGEVAEYGThVELLD 601
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSvLIITHYQRLLDYikPDRVHVLYDGRIVKSGD-KELAL 193
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
384-590 |
1.24e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.36 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 384 QENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEG----IILLN------GKRIEDYQPQDWQdrISAIF 453
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshIELLGrtvqreGRLARDIRKSRAN--TGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 454 QDF-VRYELDVKENIGYGD-------------YKRSNHLVAIQAAAKrsgaLTMIDSLPDKMDTqlgktfangiqLSGGQ 519
Cdd:PRK09984 93 QQFnLVNRLSVLENVLIGAlgstpfwrtcfswFTREQKQRALQALTR----VGMVHFAHQRVST-----------LSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 520 WQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSmGLFISHRYSTVKYA----DRIIVLDKGEV 590
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQND-GITVVVTLHQVDYAlrycERIVALRQGHV 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
359-607 |
1.28e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.35 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 359 EKTLENVSSTEEGIQFLNVSFKYPGQENYTLK---NVNFHIKPGETLALVGSNGSGKSTIVK----LLTRLYTD------ 425
Cdd:PRK13631 9 KLKVPNPLSDDIILRVKNLYCVFDEKQENELValnNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIKSKYGTiqvgdi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 426 --------YEGIILLNGKRIEDYQpqDWQDRISAIFQdFVRYEL---DVKENIGYGDYKRSNHlvAIQAAAKRSGALTMI 494
Cdd:PRK13631 89 yigdkknnHELITNPYSKKIKNFK--ELRRRVSMVFQ-FPEYQLfkdTIEKDIMFGPVALGVK--KSEAKKLAKFYLNKM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 495 DslpdkmdtqLGKTF--ANGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLF-ISH 571
Cdd:PRK13631 164 G---------LDDSYleRSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFvITH 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 502825101 572 RYSTV-KYADRIIVLDKGEVAEYGTHVELLDTNGIYA 607
Cdd:PRK13631 235 TMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
372-587 |
2.11e-15 |
|
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: 74.11 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIIllngkriedYQPQDwqdriSA 451
Cdd:cd03223 1 IELENLSLATP-DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPEG-----ED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFqdFVryeldvkenigygdykrsnhlvaiqaaAKRS--GALTMIDSLpdkmdtqlgkTFANGIQLSGGQWQRIAIARAY 529
Cdd:cd03223 66 LL--FL---------------------------PQRPylPLGTLREQL----------IYPWDDVLSGGEQQRLAFARLL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 530 MRRASLYILDEPTAALDPAAEEEVFQDFQEiaqKSMGLF-ISHRYSTVKYADRIIVLDK 587
Cdd:cd03223 107 LHKPKFVFLDEATSALDEESEDRLYQLLKE---LGITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
364-602 |
2.13e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.67 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 364 NVSSTEEGIQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTD-----YEGIILLNGKRIE 438
Cdd:PRK14271 14 DVDAAAPAMAAVNLTLGFAGKT--VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 439 DYQP-QDWQDRISAIFQDFVRYELDVKENIGYGdyKRSNHLVAIQ----AAAKRSGALTMIDSLPDKMDTqlgktfaNGI 513
Cdd:PRK14271 92 NYRDvLEFRRRVGMLFQRPNPFPMSIMDNVLAG--VRAHKLVPRKefrgVAQARLTEVGLWDAVKDRLSD-------SPF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 514 QLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYS-TVKYADRIIVLDKGEVAE 592
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVE 242
|
250
....*....|
gi 502825101 593 YGTHVELLDT 602
Cdd:PRK14271 243 EGPTEQLFSS 252
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
385-590 |
2.21e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 76.25 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 385 ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIiLLNGKriedyQP-QDWQDRISAIFQDfvrYEL-- 461
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGT-----APlAEAREDTRLMFQD---ARLlp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 462 --DVKENIGYG---DYkRSNHLVAIQAA--AKRSGaltmidSLPdkmdtqlgktfangIQLSGGQWQRIAIARAYMRRAS 534
Cdd:PRK11247 95 wkKVIDNVGLGlkgQW-RDAALQALAAVglADRAN------EWP--------------AALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 535 LYILDEPTAALDPAAEEEVfQDFQEIAQKSMG---LFISHRYS-TVKYADRIIVLDKGEV 590
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEM-QDLIESLWQQHGftvLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
372-603 |
3.03e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 76.31 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISA 451
Cdd:PRK13647 5 IEVEDLHFRYK-DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQD-----FvryELDVKENIGYGdyKRSNHLVAIQAAAKRSGALTMID--SLPDKMDTQLgktfangiqlSGGQWQRIA 524
Cdd:PRK13647 84 VFQDpddqvF---SSTVWDDVAFG--PVNMGLDKDEVERRVEEALKAVRmwDFRDKPPYHL----------SYGQKKRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 525 IARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS-HRYS-TVKYADRIIVLDKGEVAEYGTHVELLDT 602
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
.
gi 502825101 603 N 603
Cdd:PRK13647 229 D 229
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
389-614 |
3.34e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.49 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLT--RLYTDYEGIILLNGKRIEDYQPqdwQDR----ISAIFQ-------- 454
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSP---DERaragIFLAFQypveipgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 455 ---DFVRYELDvkenigygdykrsnhlvaiqaaAKRSGALTMIDSLP---DKMDT-QLGKTFAN-----GiqLSGGQWQR 522
Cdd:COG0396 93 svsNFLRTALN----------------------ARRGEELSAREFLKllkEKMKElGLDEDFLDryvneG--FSGGEKKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 523 IAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMG-LFISH-----RYstVKyADRIIVLDKGEVAEYGTH 596
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGiLIITHyqrilDY--IK-PDFVHVLVDGRIVKSGGK 225
|
250 260
....*....|....*....|
gi 502825101 597 --VELLDTNGiYARLFNLQA 614
Cdd:COG0396 226 elALELEEEG-YDWLKEEAA 244
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
389-588 |
3.85e-15 |
|
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: 75.16 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLN--GKRIEDYQPQDWQdrisaIFQdfVRyeldvKEN 466
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDLAQASPRE-----ILA--LR-----RRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 467 IGYgdykRSNHLVAI--------------------QAAAKRSGALtmidsLpdkmdTQLG----------KTFangiqlS 516
Cdd:COG4778 95 IGY----VSQFLRVIprvsaldvvaepllergvdrEEARARAREL-----L-----ARLNlperlwdlppATF------S 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 517 GGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIaqKSMG---LFISHRYSTVK-YADRIIVLDKG 588
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA--KARGtaiIGIFHDEEVREaVADRVVDVTPF 228
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
389-592 |
4.91e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.91 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYT--DYEGIILLNGKRIEDYQPQDWQDR-ISAIFQD--FVRYeLDV 463
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPhgSYEGEILFDGEVCRFKDIRDSEALgIVIIHQElaLIPY-LSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 464 KENIGYGDYKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTQLGKtfangiqLSGGQWQRIAIARAYMRRASLYILDEPTA 543
Cdd:NF040905 96 AENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTD-------IGVGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502825101 544 AL---DPAAEEEVFQDFQeiAQKSMGLFISHRYSTVKY-ADRIIVLDKGEVAE 592
Cdd:NF040905 169 ALneeDSAALLDLLLELK--AQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
389-593 |
6.40e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 78.07 E-value: 6.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRlytdyeGIILLNGKRIedYQpqdwQD-RISAIFQDFVRYELD----- 462
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNG------EVLLDDGRII--YE----QDlIVARLQQDPPRNVEGtvydf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 463 ----VKENIGY-GDYKRSNHLVAIQAAAKRsgaLTMIDSLPDKMDTQLGKTFANGIQ----------------LSGGqWQ 521
Cdd:PRK11147 87 vaegIEEQAEYlKRYHDISHLVETDPSEKN---LNELAKLQEQLDHHNLWQLENRINevlaqlgldpdaalssLSGG-WL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 522 R-IAIARAYMRRASLYILDEPTAALDPAAEE--EVF-QDFQeiaqksmG--LFISHRYSTV-KYADRIIVLDKGEVAEY 593
Cdd:PRK11147 163 RkAALGRALVSNPDVLLLDEPTNHLDIETIEwlEGFlKTFQ-------GsiIFISHDRSFIrNMATRIVDLDRGKLVSY 234
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
391-571 |
7.50e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.68 E-value: 7.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 391 NVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDFVRYELDVKENIGYg 470
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 471 dYKRSNHLVAIQAAAKrsgALTMIdSLPDKMDTQLGktfangiQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAE 550
Cdd:PRK13538 98 -YQRLHGPGDDEALWE---ALAQV-GLAGFEDVPVR-------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180
....*....|....*....|..
gi 502825101 551 EEVFQDFQEIAQKS-MGLFISH 571
Cdd:PRK13538 166 ARLEALLAQHAEQGgMVILTTH 187
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
372-552 |
8.71e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.74 E-value: 8.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDyqPQdwQDRiSA 451
Cdd:PRK11248 2 LQISHLYADYGGKP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--PG--AER-GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDfvryE-----LDVKENIGYGdykrsNHLVAIQAAAKRSGALTMIDslpdKMDTQ-LGKTFAngIQLSGGQWQRIAI 525
Cdd:PRK11248 75 VFQN----EgllpwRNVQDNVAFG-----LQLAGVEKMQRLEIAHQMLK----KVGLEgAEKRYI--WQLSGGQRQRVGI 139
|
170 180
....*....|....*....|....*..
gi 502825101 526 ARAYMRRASLYILDEPTAALDPAAEEE 552
Cdd:PRK11248 140 ARALAANPQLLLLDEPFGALDAFTREQ 166
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
389-601 |
1.33e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.52 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIED------------YQPQDwqdriSAIFQDf 456
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmhkrarlgigYLPQE-----ASIFRK- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 457 vryeLDVKENIgygdykrsnhLVAIQAAAK-RSGALTMIDSLPDKMD-TQLGKTfaNGIQLSGGQWQRIAIARAYMRRAS 534
Cdd:COG1137 93 ----LTVEDNI----------LAVLELRKLsKKEREERLEELLEEFGiTHLRKS--KAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 535 LYILDEPTAALDPAAEEEVfqdfQEI----AQKSMGLFIS-HRY-STVKYADRIIVLDKGEVAEYGTHVELLD 601
Cdd:COG1137 157 FILLDEPFAGVDPIAVADI----QKIirhlKERGIGVLITdHNVrETLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
389-585 |
1.63e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.21 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDFVRyeldvkenig 468
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL---------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 469 YGDYKRSNHLVAIQAAAKRSGALTMIDS-----LPDKMdtqLGKTFAngiQLSGGQWQRIAIAR--AYMRRASLyiLDEP 541
Cdd:PRK10247 93 FGDTVYDNLIFPWQIRNQQPDPAIFLDDlerfaLPDTI---LTKNIA---ELSGGEKQRISLIRnlQFMPKVLL--LDEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502825101 542 TAALDPAAEEEVFQDFQEIA-QKSMG-LFISHRYSTVKYADRIIVL 585
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVrEQNIAvLWVTHDKDEINHADKVITL 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
376-589 |
2.55e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.92 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQD-WQDRISAIFQ 454
Cdd:PRK10982 3 NISKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 455 DF--VRyELDVKENIGYGDYKRSNHLVAIQAAAKRSGALtmIDSLPDKMDTQlgktfANGIQLSGGQWQRIAIARAYMRR 532
Cdd:PRK10982 81 ELnlVL-QRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAI--FDELDIDIDPR-----AKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 533 ASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGL-FISHRYSTV-KYADRIIVLDKGE 589
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIvYISHKMEEIfQLCDEITILRDGQ 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
389-607 |
3.93e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.49 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDRISAIFQDF-VRYELDVKENI 467
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTsLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 GYGdykRSNHLV-------AIQAAAKRSGALTMIDSLPDKMDTQLgktfangiqlSGGQWQRIAIARAYMRRASLYILDE 540
Cdd:PRK09536 99 EMG---RTPHRSrfdtwteTDRAAVERAMERTGVAQFADRPVTSL----------SGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 541 PTAALDPAAEEEVFQDFQEIAQ--KSMGLFISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNGIYA 607
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLVDdgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRA 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
372-599 |
4.80e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 74.84 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLL--TRLYTDYEGIILLNGKRIED---------- 439
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHVALCEKcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 440 ----------YQPQD---W----------QDRISAIFQ-DFVRYELD-VKENIgygdyKRSNHLVAIQAAAKRSGALTMI 494
Cdd:TIGR03269 79 gepcpvcggtLEPEEvdfWnlsdklrrriRKRIAIMLQrTFALYGDDtVLDNV-----LEALEEIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 495 D--SLPDKMdTQLGKtfangiQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKS-MGLFISH 571
Cdd:TIGR03269 154 EmvQLSHRI-THIAR------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgISMVLTS 226
|
250 260 270
....*....|....*....|....*....|
gi 502825101 572 RYSTV--KYADRIIVLDKGEVAEYGTHVEL 599
Cdd:TIGR03269 227 HWPEVieDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
384-594 |
5.23e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.30 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 384 QENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLT-RLYTD-YEGIILLNGKRIEdyqpQDWQDRISAIFQDFVRY-E 460
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNnFTGTILANNRKPT----KQILKRTGFVTQDDILYpH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 461 LDVKENIGYGDYKRSNHLVAIQAaaKRSGALTMIDSL--PDKMDTQLGKTFANGIqlSGGQWQRIAIARAYMRRASLYIL 538
Cdd:PLN03211 155 LTVRETLVFCSLLRLPKSLTKQE--KILVAESVISELglTKCENTIIGNSFIRGI--SGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 539 DEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS-HRYSTVKYA--DRIIVLDKGEVAEYG 594
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSSRVYQmfDSVLVLSEGRCLFFG 289
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
376-590 |
7.45e-14 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 71.28 E-value: 7.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRiedYQPQDWQDrISAIFQD 455
Cdd:TIGR03740 5 NLSKRFGKQT--AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHP---WTRKDLHK-IGSLIES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 456 FVRYE-LDVKENIgygdykrsnHLVAIQAAAKRSgaltMIDSLPDKMD-TQLGKTFANgiQLSGGQWQRIAIARAYMRRA 533
Cdd:TIGR03740 79 PPLYEnLTARENL---------KVHTTLLGLPDS----RIDEVLNIVDlTNTGKKKAK--QFSLGMKQRLGIAIALLNHP 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 534 SLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFI-SHRYSTVKY-ADRIIVLDKGEV 590
Cdd:TIGR03740 144 KLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILsSHILSEVQQlADHIGIISEGVL 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
384-592 |
8.34e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.14 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 384 QENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDyegiilLNGKRIEDYQPQDWQDRISAIfqdfvryeldv 463
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG------TPVAGCVDVPDNQFGREASLI----------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 464 kENIG-YGDYKRSnhlVAIQAAAKRSGALTMIdslpdkmdtqlgKTFANgiqLSGGQWQRIAIARAYMRRASLYILDEPT 542
Cdd:COG2401 104 -DAIGrKGDFKDA---VELLNAVGLSDAVLWL------------RRFKE---LSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502825101 543 AALDPAAEEEVFQDFQEIAQKSMG--LFISHRYSTVKY--ADRIIVLDKGEVAE 592
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAGItlVVATHHYDVIDDlqPDLLIFVGYGGVPE 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
389-602 |
1.06e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 71.62 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYE------GIILLNGKRIEDYQPQDWQDRISAIFQDFVRY-EL 461
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 462 DVKENIGY----GDYKRSNHLVAIQAAAKRSgaLTMIDSLPDKMDTQLGktfangiQLSGGQWQRIAIARAYMRRASLYI 537
Cdd:PRK14246 106 SIYDNIAYplksHGIKEKREIKKIVEECLRK--VGLWKEVYDRLNSPAS-------QLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 538 LDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTV-KYADRIIVLDKGEVAEYGTHVELLDT 602
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
403-594 |
1.42e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.60 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 403 ALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDW----QDRISAIFQD---FVRYEldVKENIGYGdYKRS 475
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClppeKRRIGYVFQDarlFPHYK--VRGNLRYG-MAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 476 N--------HLVAIQAAAKRsgaltmidsLPdkmdtqlgktfangIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDP 547
Cdd:PRK11144 105 MvaqfdkivALLGIEPLLDR---------YP--------------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502825101 548 AAEEEVFQDFQEIAQ--KSMGLFISHRYSTV-KYADRIIVLDKGEVAEYG 594
Cdd:PRK11144 162 PRKRELLPYLERLAReiNIPILYVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
389-546 |
1.43e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.58 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRI----EDYQPQDWQDRISAIFQDFVRY-ELDV 463
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAKLRAKHVGFVFQSFMLIpTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 464 KENIGY-----GDYKRSNHLVAIqAAAKRSGALTMIDSLPdkmdtqlgktfangIQLSGGQWQRIAIARAYMRRASLYIL 538
Cdd:PRK10584 106 LENVELpallrGESSRQSRNGAK-ALLEQLGLGKRLDHLP--------------AQLSGGEQQRVALARAFNGRPDVLFA 170
|
....*...
gi 502825101 539 DEPTAALD 546
Cdd:PRK10584 171 DEPTGNLD 178
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
391-588 |
1.80e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.79 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 391 NVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDR-ISAIFQDfVRY--ELDVKENI 467
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgVVRTFQH-VRLfrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 gygdykrsnhLVAiQAAAKRSGALTMIDSLP-------DKMD------TQLGKT-FAN---GiQLSGGQWQRIAIARAYM 530
Cdd:PRK11300 102 ----------LVA-QHQQLKTGLFSGLLKTPafrraesEALDraatwlERVGLLeHANrqaG-NLAYGQQRRLEIARCMV 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502825101 531 RRASLYILDEPTAALDPAAEEEVFQDFQEIaQKSMG---LFISHRYSTV-KYADRIIVLDKG 588
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAEL-RNEHNvtvLLIEHDMKLVmGISDRIYVVNQG 230
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
392-547 |
2.01e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.88 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 392 VNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGK---RIEDYQPQDWQDRISAIFQDfvryeLDVKENIG 468
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatRGDRSRFMAYLGHLPGLKAD-----LSTLENLH 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 469 YgdykrSNHLVAIQAAAKRSGALTMIdSLPDKMDTQLGktfangiQLSGGQWQRIAIARAYMRRASLYILDEPTAALDP 547
Cdd:PRK13543 105 F-----LCGLHGRRAKQMPGSALAIV-GLAGYEDTLVR-------QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
352-595 |
3.33e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 352 DKPNVSEEKTLENVSSTEEGIQFLNVSFKYPGqenYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIIL 431
Cdd:PRK13409 321 PEPIEFEERPPRDESERETLVEYPDLTKKLGD---FSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 432 LNGKrIEdYQPQdwqdRISAIFQDFVRyelDVKENIGyGDYKRSNHLVAIqaaAKRSGaltmidsLPDKMDTQLGKtfan 511
Cdd:PRK13409 398 PELK-IS-YKPQ----YIKPDYDGTVE---DLLRSIT-DDLGSSYYKSEI---IKPLQ-------LERLLDKNVKD---- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 512 giqLSGGQWQRIAIARAYMRRASLYILDEPTAALDpaAEE-----EVFQDFQEIAQKSMgLFISHRYSTVKY-ADRIIVL 585
Cdd:PRK13409 454 ---LSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQrlavaKAIRRIAEEREATA-LVVDHDIYMIDYiSDRLMVF 527
|
250
....*....|
gi 502825101 586 DkGEVAEYGT 595
Cdd:PRK13409 528 E-GEPGKHGH 536
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
389-590 |
3.52e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDR-ISAIFQDfvRY------EL 461
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPED--RLgrglvpDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 462 DVKENIGYGDYKR---SNHLV----AIQAAAKRsgaltMIdslpDKMDTQLGKTFANGIQLSGGQWQRIAIARAYMRRAS 534
Cdd:COG3845 352 SVAENLILGRYRRppfSRGGFldrkAIRAFAEE-----LI----EEFDVRTPGPDTPARSLSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502825101 535 LYILDEPTAALDPAAEEEVFQdfQEIAQKSMG---LFIshryST-----VKYADRIIVLDKGEV 590
Cdd:COG3845 423 LLIAAQPTRGLDVGAIEFIHQ--RLLELRDAGaavLLI----SEdldeiLALSDRIAVMYEGRI 480
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
397-594 |
4.13e-13 |
|
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: 69.70 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 397 KPGETLALVGSNGSGKSTIVKLLTrlytdyeGIILLNGKRIEDyqPQDWQDRISAI--------FQDFVRYELDVKENIG 468
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILA-------GKLKPNLGKFDD--PPDWDEILDEFrgselqnyFTKLLEGDVKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 469 YGDykrsnhLVAIQAAAKRSGALTMIDSLpDKMDTQLGKTFANGI------QLSGGQWQRIAIARAYMRRASLYILDEPT 542
Cdd:cd03236 95 YVD------LIPKAVKGKVGELLKKKDER-GKLDELVDQLELRHVldrnidQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502825101 543 AALDPAAEEEVFQDFQEIAQ--KSMgLFISHRYSTVKYADRIIVLDKGEVAEYG 594
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEddNYV-LVVEHDLAVLDYLSDYIHCLYGEPGAYG 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
391-590 |
4.54e-13 |
|
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: 71.78 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 391 NVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYT-DYEGIILLNGKRIEDYQPQDW-QDRISAIFQDFVRY----ELDVK 464
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQAiRAGIAMVPEDRKRHgivpILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 465 ENIGYGDYKRSNHLVAIQAAAKrsgaLTMIDSLPDKMDTQLGKTFANGIQLSGGQWQRIAIARAYMRRASLYILDEPTAA 544
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAAE----LQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502825101 545 LDPAAEEEVFQDFQEIAQKSMGLFI--SHRYSTVKYADRIIVLDKGEV 590
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQEGVAIIVvsSELAEVLGLSDRVLVIGEGKL 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
352-595 |
4.77e-13 |
|
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: 72.12 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 352 DKPNVSEEKTLENVSSTEEGIQFLNVSFKYPGqenYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIIL 431
Cdd:COG1245 322 DEPIEFEVHAPRREKEEETLVEYPDLTKSYGG---FSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 432 LNgKRIEdYQPQdwqdRISAIFQDFVRYELD--VKENIGYGDYKrsNHLVaiqaaaKRSGaltmIDSLpdkMDTQLGKtf 509
Cdd:COG1245 399 ED-LKIS-YKPQ----YISPDYDGTVEEFLRsaNTDDFGSSYYK--TEII------KPLG----LEKL---LDKNVKD-- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 510 angiqLSGGQWQRIAIARAYMRRASLYILDEPTAALDpaAEE-----EVFQDFQEIAQKSMgLFISHRYSTVKY-ADRII 583
Cdd:COG1245 456 -----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQrlavaKAIRRFAENRGKTA-MVVDHDIYLIDYiSDRLM 527
|
250
....*....|..
gi 502825101 584 VLDkGEVAEYGT 595
Cdd:COG1245 528 VFE-GEPGVHGH 538
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
375-595 |
5.31e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.52 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 375 LNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDyEGII----LLNGKRIEDYQPQDWQ---- 446
Cdd:PRK09473 18 LRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAA-NGRIggsaTFNGREILNLPEKELNklra 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 447 DRISAIFQD-------FVRYELDVKENIGYgdYKRSNHLVAIQAAAKrsgaltMIDSLpdKMDTQLGKTFANGIQLSGGQ 519
Cdd:PRK09473 97 EQISMIFQDpmtslnpYMRVGEQLMEVLML--HKGMSKAEAFEESVR------MLDAV--KMPEARKRMKMYPHEFSGGM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 520 WQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQK--SMGLFISHRYSTVK-YADRIIVLDKGEVAEYGT 595
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAgICDKVLVMYAGRTMEYGN 245
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
375-599 |
6.71e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.16 E-value: 6.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 375 LNVSFkypGQENYTLK---NVNFHIKPGETLALVGSNGSGKS----TIVKLLtrlytDYEGIIL-----LNGKRIEDYQP 442
Cdd:PRK11022 9 LSVHF---GDESAPFRavdRISYSVKQGEVVGIVGESGSGKSvsslAIMGLI-----DYPGRVMaekleFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 443 QDWQDRISA----IFQDFVRyELDVKENIGY----------GDYKRSNH--------LVAIQAAAKRsgaltmIDSLPDk 500
Cdd:PRK11022 81 KERRNLVGAevamIFQDPMT-SLNPCYTVGFqimeaikvhqGGNKKTRRqraidllnQVGIPDPASR------LDVYPH- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 501 mdtqlgktfangiQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQK-SMGL-FISHRYSTV-K 577
Cdd:PRK11022 153 -------------QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALvLITHDLALVaE 219
|
250 260
....*....|....*....|..
gi 502825101 578 YADRIIVLDKGEVAEYGTHVEL 599
Cdd:PRK11022 220 AAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
391-590 |
7.81e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 7.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 391 NVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTD-YEGIILLNGKRIEDYQPQDWQDR-ISAIFQDFVRY----ELDVK 464
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGrWEGEIFIDGKPVKIRNPQQAIAQgIAMVPEDRKRDgivpVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 465 ENIGYGDYKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTqlgkTFANGIQLSGGQWQRIAIARAYMRRASLYILDEPTAA 544
Cdd:PRK13549 360 KNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTAS----PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502825101 545 LDPAAEEEVFQDFQEIAQKSMGL-FISHRYSTV-KYADRIIVLDKGEV 590
Cdd:PRK13549 436 IDVGAKYEIYKLINQLVQQGVAIiVISSELPEVlGLSDRVLVMHEGKL 483
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
361-546 |
8.23e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 8.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 361 TLENVSsteegiqflnVSFkypGQENyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDY 440
Cdd:PRK09544 6 SLENVS----------VSF---GQRR-VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 441 QPQDWQdrISAIFQDFVRYELDVKENIGYGDykrsnhlvaIQAAAKRSGALTMIDSLPDKmdtqlgktfangiqLSGGQW 520
Cdd:PRK09544 72 VPQKLY--LDTTLPLTVNRFLRLRPGTKKED---------ILPALKRVQAGHLIDAPMQK--------------LSGGET 126
|
170 180
....*....|....*....|....*.
gi 502825101 521 QRIAIARAYMRRASLYILDEPTAALD 546
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
389-600 |
9.41e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 9.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTD--------YEGIILLNGKRIEDYQPQDWQdRISAIFQDFVR-- 458
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarVTGDVTLNGEPLAAIDAPRLA-RLRAVLPQAAQpa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 459 YELDVKENIGYGDYKRsnhlvaiqaaAKRSGALTMIDSlpDKMDTQLGKTFANGI------QLSGGQWQRIAIARAY--- 529
Cdd:PRK13547 96 FAFSAREIVLLGRYPH----------ARRAGALTHRDG--EIAWQALALAGATALvgrdvtTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 530 ------MRRASLYILDEPTAALDPAAEEEVFQDFQEIAQK-SMG-LFISHRYS-TVKYADRIIVLDKGEVAEYGTHVELL 600
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGvLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
389-609 |
9.69e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 71.73 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILlnGKRIEDYQPQD-WqdrisaIFQDFVRyeldvkENI 467
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--AERSIAYVPQQaW------IMNATVR------GNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 GYGDYKRSNHLvaiqAAAKRSGALTM-IDSLPDKMDTQLGKtfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALD 546
Cdd:PTZ00243 742 LFFDEEDAARL----ADAVRVSQLEAdLAQLGGGLETEIGE---KGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 547 PAAEEEVFQD--FQEIAQKSMGLfISHRYSTVKYADRIIVLDKGEVAEYGTHVELLDTNgIYARL 609
Cdd:PTZ00243 815 AHVGERVVEEcfLGALAGKTRVL-ATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATL 877
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
385-594 |
1.75e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.94 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 385 ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLY-----TDYEGIILLNGKRI--EDYQPQDWQDRISAIFQDFV 457
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 458 RY-ELDVKENIGYGdyKRSNHLVA--------IQAAAKRSgalTMIDSLPDKMDTQLGktfangiQLSGGQWQRIAIARA 528
Cdd:PRK14267 96 PFpHLTIYDNVAIG--VKLNGLVKskkelderVEWALKKA---ALWDEVKDRLNDYPS-------NLSGGQRQRLVIARA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 529 YMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYS-TVKYADRIIVLDKGEVAEYG 594
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAqAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
389-603 |
2.80e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.80 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGII---------LLNGKRIEDY---------------QPQD 444
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknKKKTKEKEKVleklviqktrfkkikKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 445 WQDRISAIFQdFVRYEL---DVKENIGYGDYKRSnhlVAIQAAAKRSGALTMIDSLPDKMdtqLGKtfaNGIQLSGGQWQ 521
Cdd:PRK13651 103 IRRRVGVVFQ-FAEYQLfeqTIEKDIIFGPVSMG---VSKEEAKKRAAKYIELVGLDESY---LQR---SPFELSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 522 RIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFI-SHRYSTV-KYADRIIVLDKGEVAEYG-THVE 598
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILvTHDLDNVlEWTKRTIFFKDGKIIKDGdTYDI 252
|
....*
gi 502825101 599 LLDTN 603
Cdd:PRK13651 253 LSDNK 257
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
390-591 |
3.72e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.92 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 390 KNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDWQDR-ISAIFQDFVRYELDVKENIG 468
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARgLVYLPEDRQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 469 YGDYKRSNHLVAIQAAAKRSGALTmidslpDKMDTQLGKTFANGIQ----LSGGQWQRIAIARAYMRRASLYILDEPTAA 544
Cdd:PRK15439 360 WNVCALTHNRRGFWIKPARENAVL------ERYRRALNIKFNHAEQaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502825101 545 LDPAAEEEVFQDFQEIAQKSMG-LFISHRYSTV-KYADRIIVLDKGEVA 591
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAvLFISSDLEEIeQMADRVLVMHQGEIS 482
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
390-594 |
8.22e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.88 E-value: 8.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 390 KNVNFHIKPGETLALVGSNGSGKS-TIVKLLTRL---YTDYEGIILLNGKRIEdyqPQDWQDR-ISAIFQDfVRYELDVK 464
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVA---PCALRGRkIATIMQN-PRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 465 ENIgygdykRSNHLVAIQAAAKRSGALTMIDS-----LPDkmDTQLGKTFAngIQLSGGQWQRIAIARAYMRRASLYILD 539
Cdd:PRK10418 96 HTM------HTHARETCLALGKPADDATLTAAleavgLEN--AARVLKLYP--FEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502825101 540 EPTAALDPAAEEEVFQDFQEI-AQKSMG-LFISHRYSTV-KYADRIIVLDKGEVAEYG 594
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIvQKRALGmLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
389-595 |
1.35e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.88 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGkriedYQPqdWQDR------ISAIF----QdfVR 458
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVP--FKRRkefarrIGVVFgqrsQ--LW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 459 YELDVKE---------NIGYGDYKrsnhlvaiqaaaKRSGALTMIDSLPDKMDTQLGktfangiQLSGGQWQRIAIARAY 529
Cdd:COG4586 109 WDLPAIDsfrllkaiyRIPDAEYK------------KRLDELVELLDLGELLDTPVR-------QLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502825101 530 MRRASLYILDEPTAALDPAAEEEVfQDF-QEIAQKSmG---LFISHRYSTVKY-ADRIIVLDKGEVAEYGT 595
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAI-REFlKEYNRER-GttiLLTSHDMDDIEAlCDRVIVIDHGRIIYDGS 238
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
391-599 |
4.52e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 391 NVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEdyqPQDWQDR-----ISaifQDFVRY-ELDVK 464
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIATRrrvgyMS---QAFSLYgELTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 465 ENigygdykrsnhLV---------------AIQAAAKRSGALTMIDSLPDkmdtqlgktfangiQLSGGQWQRIAIARAY 529
Cdd:NF033858 358 QN-----------LElharlfhlpaaeiaaRVAEMLERFDLADVADALPD--------------SLPLGIRQRLSLAVAV 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502825101 530 MRRASLYILDEPTAALDPAAEEEVFQDFQEIA-QKSMGLFIS-HRYSTVKYADRIIVLDKGEVAEYGTHVEL 599
Cdd:NF033858 413 IHKPELLILDEPTSGVDPVARDMFWRLLIELSrEDGVTIFIStHFMNEAERCDRISLMHAGRVLASDTPAAL 484
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
388-591 |
4.86e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 388 TLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDwqdrisAIFQDFVryeLDVKENI 467
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE------AINHGFA---LVTEERR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 GYGDYKR----SNHLVA-IQAAAKRSGALT----------MIDSLPDKM---DTQLGktfangiQLSGGQWQRIAIARAY 529
Cdd:PRK10982 334 STGIYAYldigFNSLISnIRNYKNKVGLLDnsrmksdtqwVIDSMRVKTpghRTQIG-------SLSGGNQQKVIIGRWL 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502825101 530 MRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFI--SHRYSTVKYADRIIVLDKGEVA 591
Cdd:PRK10982 407 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIisSEMPELLGITDRILVMSNGLVA 470
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
374-594 |
8.39e-11 |
|
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: 61.89 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 374 FLNVSF--KYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDY---EGIILLNGkriEDYQPQDWQDR 448
Cdd:cd03233 6 WRNISFttGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG---IPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 449 ISAIF---QDFVRYELDVKENIGYgdykrsnhlvaiqaaakrsgALTMidslpdkmdtqLGKTFANGIqlSGGQWQRIAI 525
Cdd:cd03233 83 GEIIYvseEDVHFPTLTVRETLDF--------------------ALRC-----------KGNEFVRGI--SGGERKRVSI 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 526 ARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKS-MGLFIS------HRYSTVkyaDRIIVLDKGEVAEYG 594
Cdd:cd03233 130 AEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLkTTTFVSlyqasdEIYDLF---DKVLVLYEGRQIYYG 202
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
396-595 |
1.44e-10 |
|
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: 60.66 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 396 IKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEdYQPQDwqdrisaifqdfvryeldvkenigygdykrs 475
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-YKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 476 nhlvaiqaaakrsgaltmidslpdkmdtqlgktfangIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPA---AEEE 552
Cdd:cd03222 70 -------------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAAR 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502825101 553 VFQDFQEIAQKSMgLFISHRYSTVKY-ADRIIVLDkGEVAEYGT 595
Cdd:cd03222 113 AIRRLSEEGKKTA-LVVEHDLAVLDYlSDRIHVFE-GEPGVYGI 154
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
364-578 |
1.53e-10 |
|
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: 64.00 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 364 NVSSTEEGIQFLNVSFKYPGQEnYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQ 443
Cdd:TIGR00954 444 IVEYQDNGIKFENIPLVTPNGD-VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQ 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 444 -------DWQDRIsaIFQDFVryeLDVKENiGYGDYKRSNHLVAIQAA--AKRSGALtmiDSLPDKMDTqlgktfangiq 514
Cdd:TIGR00954 523 rpymtlgTLRDQI--IYPDSS---EDMKRR-GLSDKDLEQILDNVQLThiLEREGGW---SAVQDWMDV----------- 582
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 515 LSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEiaqKSMGLF-ISHRYSTVKY 578
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE---FGITLFsVSHRKSLWKY 644
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
372-600 |
1.68e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.50 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYpgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLtrlytdyEG-IILLNGKRIEDYQ--------- 441
Cdd:PRK10938 4 LQISQGTFRL--SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARAL-------AGeLPLLSGERQSQFShitrlsfeq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 442 -----PQDWQDR----ISAIFQDFVRYELDVKENiGYGDYKRSNHLvaiqaaAKRSGaltmIDSLpdkmdtqLGKTFang 512
Cdd:PRK10938 75 lqklvSDEWQRNntdmLSPGEDDTGRTTAEIIQD-EVKDPARCEQL------AQQFG----ITAL-------LDRRF--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 513 IQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGL-FISHRYSTV-KYADRIIVLDKGEV 590
Cdd:PRK10938 134 KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLvLVLNRFDEIpDFVQFAGVLADCTL 213
|
250
....*....|
gi 502825101 591 AEYGTHVELL 600
Cdd:PRK10938 214 AETGEREEIL 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
376-600 |
1.70e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.83 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLT--------RLYTDYEGIILL----NGKRIEDYQPQ 443
Cdd:PRK10895 8 NLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVgivprdagNIIIDDEDISLLplhaRARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 444 DwqdriSAIFQDFVRYE-----LDVKENIGYGDYK-RSNHLVaiqaaakrsgALTMIDSLPDKMdtqlgktfanGIQLSG 517
Cdd:PRK10895 86 E-----ASIFRRLSVYDnlmavLQIRDDLSAEQREdRANELM----------EEFHIEHLRDSM----------GQSLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 518 GQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHR--YSTVKYADRIIVLDKGEVAEYGT 595
Cdd:PRK10895 141 GERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHnvRETLAVCERAYIVSQGHLIAHGT 220
|
....*
gi 502825101 596 HVELL 600
Cdd:PRK10895 221 PTEIL 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
372-594 |
2.36e-10 |
|
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: 60.33 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKY--PGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTD--YEGIILLNGKRIEDYqpqdwqd 447
Cdd:cd03232 4 LTWKNLNYTVpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKN------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 448 risaiFQDFVRY--ELDVkenigygdykrsnHlvaiqaaakrSGALTMIDSLpdkmdtqlgkTF-ANGIQLSGGQWQRIA 524
Cdd:cd03232 77 -----FQRSTGYveQQDV-------------H----------SPNLTVREAL----------RFsALLRGLSVEQRKRLT 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502825101 525 IARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS-HRYSTV--KYADRIIVLDK-GEVAEYG 594
Cdd:cd03232 119 IGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTiHQPSASifEKFDRLLLLKRgGKTVYFG 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
376-589 |
3.58e-10 |
|
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: 62.65 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQEnYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLN-GKRIeDYQPQDWQdrisaifq 454
Cdd:TIGR03719 9 RVSKVVPPKK-EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKV-GYLPQEPQ-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 455 dfVRYELDVKENIGYGdykrsnhLVAIQAAAKRSGALTMIDSLPD---------------KMDTQLGKTFANGIQ----- 514
Cdd:TIGR03719 79 --LDPTKTVRENVEEG-------VAEIKDALDRFNEISAKYAEPDadfdklaaeqaelqeIIDAADAWDLDSQLEiamda 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 515 ------------LSGGQWQRIAIARAYMRRASLYILDEPTAALDpaAE-----EEVFQDFQE--IAqksmglfISH-RYS 574
Cdd:TIGR03719 150 lrcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD--AEsvawlERHLQEYPGtvVA-------VTHdRYF 220
|
250
....*....|....*
gi 502825101 575 TVKYADRIIVLDKGE 589
Cdd:TIGR03719 221 LDNVAGWILELDRGR 235
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
385-595 |
5.41e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.43 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 385 ENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLT--RLYTDYEGIILLNGKRIEDYQPQDWQDR-ISAIFQ------- 454
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEPEERAHLgIFLAFQypieipg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 455 ----DFVRyeldvkenIGYGDYKRSNHLVAIQaaakrsgALTMIDSLPDKMD-TQLGKTFAN-----GiqLSGGQWQRIA 524
Cdd:CHL00131 99 vsnaDFLR--------LAYNSKRKFQGLPELD-------PLEFLEIINEKLKlVGMDPSFLSrnvneG--FSGGEKKRNE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 525 IARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIA--QKSMgLFISHRYSTVKY--ADRIIVLDKGEVAEYGT 595
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtsENSI-ILITHYQRLLDYikPDYVHVMQNGKIIKTGD 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
392-591 |
1.23e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 392 VNFHIKPGETLALVGSNGSGKSTIVKLL---TRLYtdyEGIILLNGKRIEDYQPQDW---------QDR----ISAIfqd 455
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLygaTRRT---AGQVYLDGKPIDIRSPRDAiragimlcpEDRkaegIIPV--- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 456 fvryeLDVKENIGYGdyKRSNHLVA---IQAAAKRSGALTMIDSLpdKMDTQLGKTFAngIQLSGGQWQRIAIARAYMRR 532
Cdd:PRK11288 346 -----HSVADNINIS--ARRHHLRAgclINNRWEAENADRFIRSL--NIKTPSREQLI--MNLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502825101 533 ASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMG-LFISHRYSTV-KYADRIIVLDKGEVA 591
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAvLFVSSDLPEVlGVADRIVVMREGRIA 475
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
391-601 |
1.58e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.17 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 391 NVNFHIKPGETLALVGSNGSGKSTIVKLL-TRLYTDyEGIILLngkRIEDYQPQDWQDRISA------------IFQ--- 454
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALsARLAPD-AGEVHY---RMRDGQLRDLYALSEAerrrllrtewgfVHQhpr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 455 DFVRYELDVKENIG----------YGDykrsnhlvaIQAAAKRSGALTMIDslPDKMDtQLGKTFangiqlSGGQWQRIA 524
Cdd:PRK11701 100 DGLRMQVSAGGNIGerlmavgarhYGD---------IRATAGDWLERVEID--AARID-DLPTTF------SGGMQQRLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 525 IARAYMRRASLYILDEPTAALDPAAEEEVFqDFQEIAQKSMGL---FISHRYSTVK-YADRIIVLDKGEVAEYGTHVELL 600
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLL-DLLRGLVRELGLavvIVTHDLAVARlLAHRLLVMKQGRVVESGLTDQVL 240
|
.
gi 502825101 601 D 601
Cdd:PRK11701 241 D 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
356-600 |
2.16e-09 |
|
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: 60.20 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 356 VSEEKTLENVSSTEEGIQFLNVSFKYPGQENYTLK---NVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILL 432
Cdd:TIGR03269 264 VSEVEKECEVEVGEPIIKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 433 ngkRIEDyqpqDWQDR--------------ISAIFQDFVRY-ELDVKEN----IG------YGDYKRSNHLVAIQAAAKR 487
Cdd:TIGR03269 344 ---RVGD----EWVDMtkpgpdgrgrakryIGILHQEYDLYpHRTVLDNlteaIGlelpdeLARMKAVITLKMVGFDEEK 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 488 sgALTMIDSLPDkmdtqlgktfangiQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEiAQKSMG- 566
Cdd:TIGR03269 417 --AEEILDKYPD--------------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILK-AREEMEq 479
|
250 260 270
....*....|....*....|....*....|....*..
gi 502825101 567 --LFISHRYSTV-KYADRIIVLDKGEVAEYGTHVELL 600
Cdd:TIGR03269 480 tfIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
396-594 |
2.89e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 396 IKPGETLALVGSNGSGKSTIVKLLTrlytdyeGIILLNGKRIEDyqPQDWQDRISAI--------FQDFVRYELDVKENI 467
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILS-------GELIPNLGDYEE--EPSWDEVLKRFrgtelqnyFKKLYNGEIKVVHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 468 GYGDYkrsnhlVAIQAAAKRSGALT------MIDSLPDKMDtqLGKTFANGI-QLSGGQWQRIAIARAYMRRASLYILDE 540
Cdd:PRK13409 167 QYVDL------IPKVFKGKVRELLKkvdergKLDEVVERLG--LENILDRDIsELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502825101 541 PTAALDpaaeeeVFQDF------QEIAQKSMGLFISHRYSTVKY-ADRIIVLdKGEVAEYG 594
Cdd:PRK13409 239 PTSYLD------IRQRLnvarliRELAEGKYVLVVEHDLAVLDYlADNVHIA-YGEPGAYG 292
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
389-594 |
3.21e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.36 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGkriedyQPQDwqdriSAIFQDFVRY-----ELD- 462
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG------QPTR-----QALQKNLVAYvpqseEVDw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 463 -----VKENIGYGDYkrsNHLVAIQAAAKR-----SGALTMIDSLpDKMDTQLGktfangiQLSGGQWQRIAIARAYMRR 532
Cdd:PRK15056 92 sfpvlVEDVVMMGRY---GHMGWLRRAKKRdrqivTAALARVDMV-EFRHRQIG-------ELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 533 ASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS-HRYSTVKYADRIIVLDKGEVAEYG 594
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVStHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
398-589 |
3.72e-09 |
|
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: 55.84 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 398 PGETLALVGSNGSGKSTIVKLLTRLYT-DYEGIILLNGKRIEDYQPQDWQDRISAIfqdfvryeldvkenigygdykrsn 476
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGpPGGGVIYIDGEDILEEVLDQLLLIIVGG------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 477 hlvaiqaaakrsgaltmidslpdkmdtqlgktfaNGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQD 556
Cdd:smart00382 57 ----------------------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLL 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502825101 557 FQEIAQKSMG-------LFISHRYSTVK------YADRIIVLDKGE 589
Cdd:smart00382 103 EELRLLLLLKseknltvILTTNDEKDLGpallrrRFDRRIVLLLIL 148
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
376-558 |
4.93e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLtrlytdyegiillngkrIEDYQPQDWQDRIS----- 450
Cdd:PRK11147 324 NVNYQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM-----------------LGQLQADSGRIHCGtklev 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 451 AIFqDFVRYELD----VKENIGYGDYK-----RSNH-LVAIQA---AAKRsgALTmidslPDKmdtqlgktfangiQLSG 517
Cdd:PRK11147 385 AYF-DQHRAELDpektVMDNLAEGKQEvmvngRPRHvLGYLQDflfHPKR--AMT-----PVK-------------ALSG 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502825101 518 GQWQRIAIARAYMRRASLYILDEPTAALDpaAE-----EEVFQDFQ 558
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLD--VEtlellEELLDSYQ 487
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
383-592 |
7.41e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.64 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 383 GQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQPQDW----------QDRISAI 452
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAvkkgmayiteSRRDNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 453 FQDF-VRYELDVKENIGYGDYKRSNHLVAIQAAAKRSgaltmiDSLPDKMDTQLGKTFANGIQLSGGQWQRIAIARAYMR 531
Cdd:PRK09700 353 FPNFsIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTA------ENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCC 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502825101 532 RASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFI--SHRYSTVKYADRIIVLDKGEVAE 592
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMvsSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
372-602 |
8.92e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.50 E-value: 8.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTD----------YEGIILLngkRIEDYQ 441
Cdd:PRK15093 6 IRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvtadrmrFDDIDLL---RLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 442 PQDWQDR-ISAIFQDfVRYELDVKENIGYGdykrsnhlvAIQAAA--------------KRSGALTMIDSLPDKMDTQLG 506
Cdd:PRK15093 83 RRKLVGHnVSMIFQE-PQSCLDPSERVGRQ---------LMQNIPgwtykgrwwqrfgwRKRRAIELLHRVGIKDHKDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 507 KTFAngIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMG--LFISHRYSTV-KYADRII 583
Cdd:PRK15093 153 RSFP--YELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTtiLLISHDLQMLsQWADKIN 230
|
250
....*....|....*....
gi 502825101 584 VLDKGEVAEYGTHVELLDT 602
Cdd:PRK15093 231 VLYCGQTVETAPSKELVTT 249
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
372-555 |
9.07e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.33 E-value: 9.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYPGQEnYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRiedyqpqdwqdRISA 451
Cdd:PLN03073 509 ISFSDASFGYPGGP-LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-----------RMAV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDFVRyELDVKenigygdykrSNHLvaiqaaakrsgaLTMIDSLP----DKMDTQLGKTFANG---IQ----LSGGQW 520
Cdd:PLN03073 577 FSQHHVD-GLDLS----------SNPL------------LYMMRCFPgvpeQKLRAHLGSFGVTGnlaLQpmytLSGGQK 633
|
170 180 190
....*....|....*....|....*....|....*
gi 502825101 521 QRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQ 555
Cdd:PLN03073 634 SRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQ 668
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
372-571 |
1.52e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 372 IQFLNVSFKYpgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTrlyTD----YEGIILLNGKRiedyqpqdwqd 447
Cdd:PRK10938 261 IVLNNGVVSY--NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT---GDhpqgYSNDLTLFGRR----------- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 448 RISA--IFqdfvryelDVKENIGYG------DYKRSNHL--VAI----------QAAAKRSGALTM--IDSLpdKMDTQL 505
Cdd:PRK10938 325 RGSGetIW--------DIKKHIGYVssslhlDYRVSTSVrnVILsgffdsigiyQAVSDRQQKLAQqwLDIL--GIDKRT 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502825101 506 GKT-FANgiqLSGGQwQRIA-IARAYMRRASLYILDEPTAALDPAAEEEV--FQDfQEIAQ-KSMGLFISH 571
Cdd:PRK10938 395 ADApFHS---LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVrrFVD-VLISEgETQLLFVSH 460
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
397-546 |
1.53e-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: 57.49 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 397 KPGETLALVGSNGSGKSTIVKLLTrlytdyeGIILLNGKRIEDyqPQDWQD-----RISAI---FQDFVRYELDVKENIG 468
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-------GELKPNLGDYDE--EPSWDEvlkrfRGTELqdyFKKLANGEIKVAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 469 YGDY--KRSNHLV--AIQAAAKRSGALTMIDSLpdKMDTQLGKTFANgiqLSGGQWQRIAIARAYMRRASLYILDEPTAA 544
Cdd:COG1245 168 YVDLipKVFKGTVreLLEKVDERGKLDELAEKL--GLENILDRDISE---LSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
..
gi 502825101 545 LD 546
Cdd:COG1245 243 LD 244
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
391-595 |
2.06e-08 |
|
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: 57.72 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 391 NVNFHikPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNGKRIEDYQpqdwqdrisaifqDFVRYELDV--KENIG 468
Cdd:TIGR01257 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNL-------------DAVRQSLGMcpQHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 469 YGDYKRSNHLVAIQAAAKRSGALTMIDSLPDKMDTQLG-KTFANGIQLSGGQWQRIAIARAYMRRASLYILDEPTAALDP 547
Cdd:TIGR01257 1015 FHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502825101 548 AAEEEVFQDFQEIAQKSMGLFISHRYSTVK-YADRIIVLDKGEVAEYGT 595
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
389-597 |
8.17e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.33 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKlltrlytdyEGIILLNGKRIEDYQPQdwQDRISAIFQDFVRYELDVkeNIG 468
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFLPK--FSRNKLIFIDQLQFLIDV--GLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 469 YgdykrsnhlvaiqaaakrsgaLTmidsLPDKMDTqlgktfangiqLSGGQWQRIAIARAYMRRA--SLYILDEPTAALD 546
Cdd:cd03238 78 Y---------------------LT----LGQKLST-----------LSGGELQRVKLASELFSEPpgTLFILDEPSTGLH 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502825101 547 PAAEEEVFQDFQEIAQKSMGL-FISHRYSTVKYADRIIVLDKGEvAEYGTHV 597
Cdd:cd03238 122 QQDINQLLEVIKGLIDLGNTViLIEHNLDVLSSADWIIDFGPGS-GKSGGKV 172
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
389-594 |
1.03e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETLALVGSNGSGKSTIVKLLT-RLY---TDYEGIILLNGKRIEDYQPQDWQDRISAIFQDFVRYELDVK 464
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsNTDgfhIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 465 ENIGYGDYKRSNH----LVAIQAAAKRSGALTM-IDSLPDKMDTQLGKTFANGIqlSGGQWQRIAIARAYMRRASLYILD 539
Cdd:TIGR00956 157 ETLDFAARCKTPQnrpdGVSREEYAKHIADVYMaTYGLSHTRNTKVGNDFVRGV--SGGERKRVSIAEASLGGAKIQCWD 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 540 EPTAALDPAAEEEVFQDFQEIAQ--KSMGLFISHRYSTVKYA--DRIIVLDKGEVAEYG 594
Cdd:TIGR00956 235 NATRGLDSATALEFIRALKTSANilDTTPLVAIYQCSQDAYElfDKVIVLYEGYQIYFG 293
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
376-550 |
1.32e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQEnYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEG-IILLNGKRIeDYQPQDWQdrisaifq 454
Cdd:PRK11819 11 RVSKVVPPKK-QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGIKV-GYLPQEPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 455 dfVRYELDVKENI--GYGDYK----RSNHLVA--------IQAAAKRSGAL-TMIDS------------------LPDKm 501
Cdd:PRK11819 81 --LDPEKTVRENVeeGVAEVKaaldRFNEIYAayaepdadFDALAAEQGELqEIIDAadawdldsqleiamdalrCPPW- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502825101 502 DTQLGKtfangiqLSGGQWQRIAIARAYMRRASLYILDEPTAALDpaAE 550
Cdd:PRK11819 158 DAKVTK-------LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD--AE 197
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
348-588 |
6.21e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 348 PESTDKPNVSEEKTLEnvSSTEEGIQF---LNVSFKYPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLT-RLY 423
Cdd:TIGR00956 737 DLTDESDDVNDEKDME--KESGEDIFHwrnLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAeRVT 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 424 TDY--EGIILLNGK-------RIEDYQPQdwqdrisaifQDFVRYELDVKENIGYGDYKRSNHLVAIQAAAKRSGALTMI 494
Cdd:TIGR00956 815 TGVitGGDRLVNGRpldssfqRSIGYVQQ----------QDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKL 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 495 DSLPDKMDTQLGKTfanGIQLSGGQWQRIAIARAYMRR-ASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS-HR 572
Cdd:TIGR00956 885 LEMESYADAVVGVP---GEGLNVEQRKRLTIGVELVAKpKLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTiHQ 961
|
250
....*....|....*...
gi 502825101 573 YSTVKYA--DRIIVLDKG 588
Cdd:TIGR00956 962 PSAILFEefDRLLLLQKG 979
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
390-583 |
3.39e-06 |
|
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: 48.23 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 390 KNVNFHIKPGETlALVGSNGSGKSTIVklltrlytdyEGI--IL-------LNGKRIEDyqpqdwqdrisAIF------- 453
Cdd:cd03278 14 DKTTIPFPPGLT-AIVGPNGSGKSNII----------DAIrwVLgeqsaksLRGEKMSD-----------VIFagsetrk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 454 -QDFVRYELdVKENigygdykrSNHLVAI--QaaakrsGALTMIDSLPDKMDTQLGktfangiQLSGGQWQRIAIA---- 526
Cdd:cd03278 72 pANFAEVTL-TFDN--------SDGRYSIisQ------GDVSEIIEAPGKKVQRLS-------LLSGGEKALTALAllfa 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502825101 527 --RAymRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADRII 583
Cdd:cd03278 130 ifRV--RPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLY 186
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
348-595 |
7.32e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 49.63 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 348 PESTDKPNVSEEKTLENVSSTEEGIQFLNVSFK-YPGQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDY 426
Cdd:TIGR01257 1913 PIFDEDDDVAEERQRIISGGNKTDILRLNELTKvYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVT 1992
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 427 EGIILLNGKRIedyqpqdwQDRISaifqdfvryelDVKENIGY-GDYKRSNHLVAIQA-----AAKRSGALTMIDSLPDK 500
Cdd:TIGR01257 1993 SGDATVAGKSI--------LTNIS-----------DVHQNMGYcPQFDAIDDLLTGREhlylyARLRGVPAEEIEKVANW 2053
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 501 MDTQLGKT-FANGI--QLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFI-SHRYSTV 576
Cdd:TIGR01257 2054 SIQSLGLSlYADRLagTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLtSHSMEEC 2133
|
250 260
....*....|....*....|
gi 502825101 577 K-YADRIIVLDKGEVAEYGT 595
Cdd:TIGR01257 2134 EaLCTRLAIMVKGAFQCLGT 2153
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
372-444 |
1.01e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 1.01e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502825101 372 IQFLNVSFkypgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLT--RLYTDYEGIILLNGKRIEDYQPQD 444
Cdd:PRK09580 4 IKDLHVSV----EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED 74
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
515-585 |
1.03e-05 |
|
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: 47.61 E-value: 1.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 515 LSGGQWQRIAIARAYMRRAS---LYILDEPTAALDPAAEEEVFQDFQEIAQKsmG---LFISHRYSTVKYADRIIVL 585
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDK--GntvVVIEHNLDVIKCADWIIDL 244
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
513-583 |
1.13e-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: 45.81 E-value: 1.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502825101 513 IQLSGGQWQRIAIA----RAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQK-SMGLFISHRYSTVKYADRII 583
Cdd:cd03227 76 LQLSGGEKELSALAlilaLASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLI 151
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
389-612 |
1.30e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 47.69 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 389 LKNVNFHIKPGETlALVGSNGSGKSTIVKLLTRLYTDYEGIILlngkRIEDY----QPQDWQDRISAIFQDFVRYELD-- 462
Cdd:COG3593 14 IKDLSIELSDDLT-VLVGENNSGKSSILEALRLLLGPSSSRKF----DEEDFylgdDPDLPEIEIELTFGSLLSRLLRll 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 463 --------VKENIGYGDYKRSNHLVAIQAAAKRSG---------ALTMIDSLPDKMDTQLGKTFANGIQL------SGGQ 519
Cdd:COG3593 89 lkeedkeeLEEALEELNEELKEALKALNELLSEYLkelldgldlELELSLDELEDLLKSLSLRIEDGKELpldrlgSGFQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 520 W-QRIAIARAYMR-----RASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFIS-HRYSTVKYA--DRIIVLDKGEV 590
Cdd:COG3593 169 RlILLALLSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITtHSPHLLSEVplENIRRLRRDSG 248
|
250 260
....*....|....*....|..
gi 502825101 591 AEYGTHVELLDTNGIYARLFNL 612
Cdd:COG3593 249 GTTSTKLIDLDDEDLRKLLRYL 270
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
514-599 |
3.60e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.27 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 514 QLSGGQWQRIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRY--STVKYADRIIVLDKGEVA 591
Cdd:NF000106 144 KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVIDRGRVI 223
|
....*...
gi 502825101 592 EYGTHVEL 599
Cdd:NF000106 224 ADGKVDEL 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
515-585 |
3.72e-05 |
|
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: 46.93 E-value: 3.72e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 515 LSGGQWQRIAIARAYMRRA---SLYILDEPTAAL---DPAAEEEVFQdfQEIAQKSMGLFISHRYSTVKYADRIIVL 585
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLhfdDIKKLLEVLQ--RLVDKGNTVVVIEHNLDVIKTADYIIDL 904
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
399-546 |
6.43e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 399 GETLALVGSNGSGKSTIVK------------------------------LLTRLYTDYEGIILLNGK----------RIE 438
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRymamhaidgipkncqilhveqevvgddttaLQCVLNTDIERTQLLEEEaqlvaqqrelEFE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 439 DYQPQDWQDRISAIFQDFVRYELdvkENIgygdYKRSNHLVAIQAAAKRSGALTMIDSLPDkMDTQLGKTFangiqlSGG 518
Cdd:PLN03073 283 TETGKGKGANKDGVDKDAVSQRL---EEI----YKRLELIDAYTAEARAASILAGLSFTPE-MQVKATKTF------SGG 348
|
170 180
....*....|....*....|....*...
gi 502825101 519 QWQRIAIARAYMRRASLYILDEPTAALD 546
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
515-583 |
2.62e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.02 E-value: 2.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502825101 515 LSGGQWQRIAIARAYMRRAS--LYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFI-SHRYSTVKYADRII 583
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVvEHDEDTIRAADHVI 209
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
376-605 |
3.19e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 376 NVSFKYPGQEnyTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIIllngKRIED----YQPQDwqdrISA 451
Cdd:PRK15064 324 NLTKGFDNGP--LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KWSENanigYYAQD----HAY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 452 IFQDfvryELDVKENIgyGDYKRSNHL-VAIQAAAKRsgaltMIDSLPDkmdtqLGKTFANgiqLSGGQWQRIAIARAYM 530
Cdd:PRK15064 394 DFEN----DLTLFDWM--SQWRQEGDDeQAVRGTLGR-----LLFSQDD-----IKKSVKV---LSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 531 RRASLYILDEPTAALDPAAEE------EVFQdfqeiaqksmG--LFISH-RYSTVKYADRIIVLDKGEVAEY-GTHVELL 600
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIEslnmalEKYE----------GtlIFVSHdREFVSSLATRIIEITPDGVVDFsGTYEEYL 524
|
....*
gi 502825101 601 DTNGI 605
Cdd:PRK15064 525 RSQGI 529
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
515-602 |
5.22e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 515 LSGGQWQRIAIARAYMRRAS--LYILDEPTAALDPAAEEEVFQDFQEIA-QKSMGLFISHRYSTVKYADRIIVLDK---- 587
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRdQGNTVLLVEHDEQMISLADRIIDIGPgagi 556
|
90
....*....|....*..
gi 502825101 588 --GEVAEYGTHVELLDT 602
Cdd:PRK00635 557 fgGEVLFNGSPREFLAK 573
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
515-542 |
7.44e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 7.44e-04
10 20 30
....*....|....*....|....*....|.
gi 502825101 515 LSGGQWQRIAIARAYMRRAS---LYILDEPT 542
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPT 857
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
515-545 |
1.01e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 1.01e-03
10 20 30
....*....|....*....|....*....|....
gi 502825101 515 LSGGQWQRIAIARAYMRRA---SLYILDEPTAAL 545
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGL 864
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
515-585 |
1.22e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502825101 515 LSGGQWQRIAIAR---AYMRRASLYILDEPTAAL---DPAAEEEVFQDFqeIAQKSMGLFISHRYSTVKYADRIIVL 585
Cdd:PRK00635 810 LSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLhthDIKALIYVLQSL--THQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
306-546 |
1.25e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 306 SLIAYFQAVNTTQKTSN------ELMYMVFNMHQNNLYMtqlFSFlNVPESTDKPNVSEEKtlenvssteegiqflnVSF 379
Cdd:PRK10636 261 SYIDRFRAKATKAKQAQsrikmlERMELIAPAHVDNPFH---FSF-RAPESLPNPLLKMEK----------------VSA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 380 KYpgQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGII-LLNGKRIEDY-QPQdwqdrisaifQDFV 457
Cdd:PRK10636 321 GY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFaQHQ----------LEFL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 458 RyeldvkenigyGDYKRSNHLVAIqaaAKRSGALTMIDSL------PDKMDTQLGktfangiQLSGGQWQRIAIARAYMR 531
Cdd:PRK10636 389 R-----------ADESPLQHLARL---APQELEQKLRDYLggfgfqGDKVTEETR-------RFSGGEKARLVLALIVWQ 447
|
250
....*....|....*
gi 502825101 532 RASLYILDEPTAALD 546
Cdd:PRK10636 448 RPNLLLLDEPTNHLD 462
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
506-583 |
1.63e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 506 GKTFANGIQLSGGQWQRIAIA---RAYMRRAS-LYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYADR 581
Cdd:TIGR02168 1081 GKKNQNLSLLSGGEKALTALAllfAIFKVKPApFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQ 1160
|
..
gi 502825101 582 II 583
Cdd:TIGR02168 1161 LY 1162
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
383-434 |
2.12e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.03 E-value: 2.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 502825101 383 GQENYTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYTDYEGIILLNG 434
Cdd:PRK13545 34 GEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
506-583 |
2.30e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 506 GKTFANGIQLSGGQWQRIAIA-----RAYmRRASLYILDEPTAALDPAAEEEVFQDFQEIAQKSMGLFISHRYSTVKYAD 580
Cdd:pfam02463 1069 GKGVKNLDLLSGGEKTLVALAlifaiQKY-KPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKAD 1147
|
...
gi 502825101 581 RII 583
Cdd:pfam02463 1148 KLV 1150
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
514-583 |
3.18e-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: 39.13 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502825101 514 QLSGGQWQ------RIAIARAYMRRASLYILDEPTAALDPAAEEEVFQDFQEiAQKSMGLF----ISHRYSTVKYADRII 583
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIE-ERKSQKNFqlivITHDEELVDAADHIY 193
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
387-424 |
7.84e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 7.84e-03
10 20 30
....*....|....*....|....*....|....*...
gi 502825101 387 YTLKNVNFHIKPGETLALVGSNGSGKSTIVKLLTRLYT 424
Cdd:pfam13555 10 GTFDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLV 47
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
395-416 |
9.72e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.76 E-value: 9.72e-03
|
| |
