|
Name |
Accession |
Description |
Interval |
E-value |
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-671 |
0e+00 |
|
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: 672.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDTGkPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGHVVNGSIKLDGEEIAGAKQ 97
Cdd:COG4172 5 PLLSVEDLSVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 98 SEFDKLRGTKMGLVPQDPMSNLNPVWRIGTQVKEALKAnnmdvaHEkrsalakalagdevevkgnddetflgakelpelm 177
Cdd:COG4172 84 RELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRL------HR---------------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 178 teakkalteaGVSGEAfdkavARftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmdDRIAG 257
Cdd:COG4172 124 ----------GLSGAA-----AR----------------------------------------------------ARALE 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 LLSEAGLPDAATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHD 337
Cdd:COG4172 137 LLERVGIPDPERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 338 LGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSLAsqriisAKERGEDADALLDhhiagestlekse 417
Cdd:COG4172 217 LGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRKLLAAEPRGD------PRPVPPDAPPLLE------------- 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 418 hiitVDHLTKEFKLP-----RKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLkPTSGKVFYEGRDTSTF 492
Cdd:COG4172 278 ----ARDLKVWFPIKrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGL 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 493 KSKDLLGFRRHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIG-DKKWRANRVKELLDMVEMPASVMGRYPNELSGGQRQ 571
Cdd:COG4172 353 SRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGlSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQ 432
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 572 RIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDE 651
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQ 512
|
650 660
....*....|....*....|
gi 2545376782 652 VFDHPQKQYTRDLLDAIPGG 671
Cdd:COG4172 513 VFDAPQHPYTRALLAAAPLL 532
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-670 |
0e+00 |
|
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: 647.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTtdtGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGHVvNGSIKLDGEEIAGAKq 97
Cdd:COG1123 3 PLLEVRDLSVRYP---GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI-SGEVLLDGRDLLELS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 98 sefDKLRGTKMGLVPQDPMSNLNPVwRIGTQVKEALKANNMdvahekrsalakalagdevevkgnddetflgakelpelm 177
Cdd:COG1123 78 ---EALRGRRIGMVFQDPMTQLNPV-TVGDQIAEALENLGL--------------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 178 teakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvTGSTMDDRIAG 257
Cdd:COG1123 115 ---------------------------------------------------------------------SRAEARARVLE 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 LLSEAGLpdaATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHD 337
Cdd:COG1123 126 LLEAVGL---ERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHD 202
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 338 LGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQhpytkrLVAAAPSLASQRIISAKERgedadalldhhiagestlEKSE 417
Cdd:COG1123 203 LGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ------ALAAVPRLGAARGRAAPAA------------------AAAE 258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 418 HIITVDHLTKEFKLPRKKEmFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDL 497
Cdd:COG1123 259 PLLEVRNLSKRYPVRGKGG-VRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 498 LGFRRHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVMGRYPNELSGGQRQRIAIAR 577
Cdd:COG1123 338 RELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIAR 417
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 578 AMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQ 657
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
650
....*....|...
gi 2545376782 658 KQYTRDLLDAIPG 670
Cdd:COG1123 498 HPYTRALLAAVPS 510
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
416-669 |
1.28e-133 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 396.02 E-value: 1.28e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKEFK-----LPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTS 490
Cdd:COG4608 4 AEPLLEVRDLKKHFPvrgglFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 491 TFKSKDLLGFRRHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVMGRYPNELSGGQR 570
Cdd:COG4608 84 GLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 571 QRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTD 650
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRD 243
|
250
....*....|....*....
gi 2545376782 651 EVFDHPQKQYTRDLLDAIP 669
Cdd:COG4608 244 ELYARPLHPYTQALLSAVP 262
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-669 |
7.64e-133 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 404.62 E-value: 7.64e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFTTDtGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTG-HVVNGSIKLDGE-----EI 92
Cdd:PRK10261 12 VLAVENLNIAFMQE-QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGgLVQCDKMLLRRRsrqviEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 93 AGAKQSEFDKLRGTKMGLVPQDPMSNLNPVWRIGTQVKEALKannmdvahekrsaLAKALAGDEVevkgnddetflgake 172
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIR-------------LHQGASREEA--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 173 lpelMTEAKKalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmd 252
Cdd:PRK10261 143 ----MVEAKR---------------------------------------------------------------------- 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 driagLLSEAGLPDAATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVL 332
Cdd:PRK10261 149 -----MLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVI 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 333 FITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSLASQR---------IISAKERGEDADAll 403
Cdd:PRK10261 224 FITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAAVPQLGAMKgldyprrfpLISLEHPAKQEPP-- 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 404 dhhiAGESTLEKSEHIITVDHLTKEFKL-----PRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPT 478
Cdd:PRK10261 302 ----IEQDTVVDGEPILQVRNLVTRFPLrsgllNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 479 SGKVFYEGRDTSTFKSKDLLGFRRHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVM 558
Cdd:PRK10261 378 GGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHA 457
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 559 GRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVM 638
Cdd:PRK10261 458 WRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVM 537
|
650 660 670
....*....|....*....|....*....|.
gi 2545376782 639 QHGKLVEHATTDEVFDHPQKQYTRDLLDAIP 669
Cdd:PRK10261 538 YLGQIVEIGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-665 |
2.53e-128 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 389.83 E-value: 2.53e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTtDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPgTGHVV--NGSIKLDGEEIAGA 95
Cdd:PRK15134 4 PLLAIENLSVAFR-QQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLP-SPPVVypSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 96 KQSEFDKLRGTKMGLVPQDPMSNLNPVWRIGTQVKEALKANNmdvahekrsalakalagdevevkgnddetflgakelpe 175
Cdd:PRK15134 82 SEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHR-------------------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 176 lmteakkalteaGVSGEAfdkavARftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmdDRI 255
Cdd:PRK15134 124 ------------GMRREA-----AR----------------------------------------------------GEI 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 256 AGLLSEAGLPDAATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFIT 335
Cdd:PRK15134 135 LNCLDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFIT 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 336 HDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSLASQRIisakerGEDADALLDhhiagestlek 415
Cdd:PRK15134 215 HNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLNSEPSGDPVPL------PEPASPLLD----------- 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 sehiitVDHLTKEFklPRKKEMFK-------AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLkPTSGKVFYEGRD 488
Cdd:PRK15134 278 ------VEQLQVAF--PIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQP 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 489 TSTFKSKDLLGFRRHVQPVFQNPYGSLDPMYSIFRSIEEPLRIH-KIGDKKWRANRVKELLDMVEMPASVMGRYPNELSG 567
Cdd:PRK15134 349 LHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSG 428
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 568 GQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHA 647
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
650
....*....|....*...
gi 2545376782 648 TTDEVFDHPQKQYTRDLL 665
Cdd:PRK15134 509 DCERVFAAPQQEYTRQLL 526
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
419-669 |
2.87e-123 |
|
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: 369.00 E-value: 2.87e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFKLPRKKemFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKP---TSGKVFYEGRDTSTFKSK 495
Cdd:COG0444 1 LLEVRNLKVYFPTRRGV--VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 496 DLLGFR-RHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEM--PASVMGRYPNELSGGQRQR 572
Cdd:COG0444 79 ELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 573 IAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEV 652
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250
....*....|....*..
gi 2545376782 653 FDHPQKQYTRDLLDAIP 669
Cdd:COG0444 239 FENPRHPYTRALLSSIP 255
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
419-647 |
1.58e-114 |
|
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: 342.95 E-value: 1.58e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFklPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLL 498
Cdd:cd03257 1 LLEVKNLSVSF--PTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 GFRRHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVK-ELLDMVEMPASVMGRYPNELSGGQRQRIAIAR 577
Cdd:cd03257 79 IRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVlLLLVGVGLPEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 578 AMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHA 647
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-388 |
3.26e-114 |
|
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: 345.88 E-value: 3.26e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFTTDTGkPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhVVNGSIKLDGEEIAGAKQS 98
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPG-ITSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 99 EFDKLRGTKMGLVPQDPMSNLNPVWRIGTQVKEALKAnnmdvaHEKRSalakalagdevevkgnddetflgakelpelmt 178
Cdd:COG0444 79 ELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRI------HGGLS-------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 179 eakkalteagvsgeafdKAVARftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmdDRIAGL 258
Cdd:COG0444 121 -----------------KAEAR----------------------------------------------------ERAIEL 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 LSEAGLPDAATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDL 338
Cdd:COG0444 132 LERVGLPDPERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDL 211
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2545376782 339 GLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSLASQR 388
Cdd:COG0444 212 GVVAEIADRVAVMYAGRIVEEGPVEELFENPRHPYTRALLSSIPRLDPDG 261
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
420-670 |
1.01e-110 |
|
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: 334.08 E-value: 1.01e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFklPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDllg 499
Cdd:COG1124 2 LEVRNLSVSY--GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDkkwRANRVKELLDMVEMPASVMGRYPNELSGGQRQRIAIARAM 579
Cdd:COG1124 77 FRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPD---REERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQKQ 659
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
250
....*....|.
gi 2545376782 660 YTRDLLDAIPG 670
Cdd:COG1124 234 YTRELLAASLA 244
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
416-670 |
1.81e-93 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 292.25 E-value: 1.81e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKEFklPRKKEMF------KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDT 489
Cdd:PRK11308 2 QQPLLQAIDLKKHY--PVKRGLFkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 490 STFKSKDLLGFRRHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVMGRYPNELSGGQ 569
Cdd:PRK11308 80 LKADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 570 RQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATT 649
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239
|
250 260
....*....|....*....|.
gi 2545376782 650 DEVFDHPQKQYTRDLLDAIPG 670
Cdd:PRK11308 240 EQIFNNPRHPYTQALLSATPR 260
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
416-671 |
8.70e-90 |
|
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: 289.66 E-value: 8.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKEFKLPrkKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKP----TSGKVFYEGRDTST 491
Cdd:COG4172 3 SMPLLSVEDLSVAFGQG--GGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 492 FKSKDLLGFR-RHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHK-IGDKKWRAnRVKELLDMVEM--PASVMGRYPNELSG 567
Cdd:COG4172 81 LSERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRgLSGAAARA-RALELLERVGIpdPERRLDAYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 568 GQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHA 647
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQG 239
|
250 260
....*....|....*....|....
gi 2545376782 648 TTDEVFDHPQKQYTRDLLDAIPGG 671
Cdd:COG4172 240 PTAELFAAPQHPYTRKLLAAEPRG 263
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
19-360 |
4.26e-86 |
|
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: 269.38 E-value: 4.26e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFTTDTGkPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLpgtgHVVNGSIKLDGEEIAGAKQS 98
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL----KPTSGSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 99 EFdKLRGTKMGLVPQDPMSNLNPVWRIGTQVKEALKANNMDVAHEKRsalakalagdevevkgnddetflgakelpelmt 178
Cdd:cd03257 76 LR-KIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEAR--------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 179 eakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmddRIAGL 258
Cdd:cd03257 122 ---------------------------------------------------------------------------KEAVL 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 LSEAGLPDAATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDL 338
Cdd:cd03257 127 LLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDL 206
|
330 340
....*....|....*....|..
gi 2545376782 339 GLAAERAQHIVVMYKGQVVESG 360
Cdd:cd03257 207 GVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-384 |
2.48e-83 |
|
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: 272.16 E-value: 2.48e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAKQ 97
Cdd:COG1123 259 PLLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTS----GSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 98 SEFDKLRGtKMGLVPQDPMSNLNPVWRIGTQVKEALKANNMdvahekrsalakalagdevevkgnddetflgakelpelm 177
Cdd:COG1123 335 RSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGL--------------------------------------- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 178 teakkalteagvsgeafdkavarftnewVPGSETRwrvaddlikagvaddlikagvaddqawylakkyvtgstmdDRIAG 257
Cdd:COG1123 375 ----------------------------LSRAERR----------------------------------------ERVAE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 LLSEAGLPDAAtrARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHD 337
Cdd:COG1123 387 LLERVGLPPDL--ADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHD 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2545376782 338 LGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSL 384
Cdd:COG1123 465 LAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPSL 511
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
412-669 |
7.35e-80 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 256.94 E-value: 7.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 412 TLEKSEHIITVDHLTKEFKLPRKKEMF-------KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFY 484
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDIKDGKQWFwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 485 EGRDTSTFKSKDLLGFRRHVQPVFQNPYGSLDPMYSIFRSIEEPLRIH--KIGDKKWRaNRVKELLDMVEMPASVMGRYP 562
Cdd:PRK15079 81 LGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYhpKLSRQEVK-DRVKAMMLKVGLLPNLINRYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 563 NELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGK 642
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
250 260
....*....|....*....|....*..
gi 2545376782 643 LVEHATTDEVFDHPQKQYTRDLLDAIP 669
Cdd:PRK15079 240 AVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
417-665 |
1.94e-79 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 253.61 E-value: 1.94e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 417 EHIITVDHLTKEFK----LPRKKEmFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGR--DTS 490
Cdd:COG4167 2 SALLEVRNLSKTFKyrtgLFRRQQ-FEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHklEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 491 TFKskdllgFR-RHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVMGRYPNELSGGQ 569
Cdd:COG4167 81 DYK------YRcKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 570 RQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATT 649
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKT 234
|
250
....*....|....*.
gi 2545376782 650 DEVFDHPQKQYTRDLL 665
Cdd:COG4167 235 AEVFANPQHEVTKRLI 250
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
419-673 |
6.55e-77 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 249.61 E-value: 6.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFklPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLL 498
Cdd:COG1135 1 MIELENLSKTF--PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 GFRRHVQPVFQNpygsldpmYSIFRS------IEEPLRIHKIgDKKWRANRVKELLDMVEMPASvMGRYPNELSGGQRQR 572
Cdd:COG1135 79 AARRKIGMIFQH--------FNLLSSrtvaenVALPLEIAGV-PKAEIRKRVAELLELVGLSDK-ADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 573 IAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEV 652
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
250 260
....*....|....*....|.
gi 2545376782 653 FDHPQKQYTRDLLDAIPGGKL 673
Cdd:COG1135 229 FANPQSELTRRFLPTVLNDEL 249
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
9-384 |
2.42e-74 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 242.71 E-value: 2.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 9 MLAMQKEHGPLLEVKDLAIDFTTDTGKpVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGHVvNGSIKLD 88
Cdd:PRK09473 2 VPLAQQQADALLDVKDLRVTFSTPDGD-VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRI-GGSATFN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 89 GEEIAGAKQSEFDKLRGTKMGLVPQDPMSNLNPVWRIGTQVKEALKAnnmdvaHEKrsaLAKAlagdevevkgnddetfl 168
Cdd:PRK09473 80 GREILNLPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLML------HKG---MSKA----------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 169 gakelpelmteakkalteagvsgEAFDKAVarftnewvpgsetrwRVADdlikagvaddlikagvaddqawylAKKyvtg 248
Cdd:PRK09473 134 -----------------------EAFEESV---------------RMLD------------------------AVK---- 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 249 stmddriagllseagLPDAATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLG 328
Cdd:PRK09473 148 ---------------MPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFN 212
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 329 TAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSL 384
Cdd:PRK09473 213 TAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPRL 268
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
419-657 |
9.93e-72 |
|
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: 232.09 E-value: 9.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFKLPRKKemFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLL 498
Cdd:cd03258 1 MIELKNVSKVFGDTGGK--VTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 GFRRHVQPVFQNpYGSLDPMySIFRSIEEPLRIHKIgDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARA 578
Cdd:cd03258 79 KARRRIGMIFQH-FNLLSSR-TVFENVALPLEIAGV-PKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 579 MALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQ 657
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
419-668 |
2.32e-71 |
|
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: 232.39 E-value: 2.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFK---LPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSK 495
Cdd:TIGR02769 2 LLEVRDVTHTYRtggLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 496 DLLGFRRHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVMGRYPNELSGGQRQRIAI 575
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 576 ARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEH--ATTDEVF 653
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEEcdVAQLLSF 241
|
250
....*....|....*
gi 2545376782 654 DHPQkqyTRDLLDAI 668
Cdd:TIGR02769 242 KHPA---GRNLQSAV 253
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-385 |
5.41e-71 |
|
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: 239.97 E-value: 5.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDTG------KPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvngSIKLDGEE 91
Cdd:COG4172 274 PLLEARDLKVWFPIKRGlfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEG-----EIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 92 IAGAKQSEFDKLRgTKMGLVPQDPMSNLNPVWRIGTQVKEALKAnnmdvaHEkrsalakalagdevevkgnddetflgak 171
Cdd:COG4172 349 LDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRV------HG---------------------------- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 172 elPELmteakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvTGSTM 251
Cdd:COG4172 394 --PGL----------------------------------------------------------------------SAAER 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 252 DDRIAGLLSEAGLpDAATRARqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAV 331
Cdd:COG4172 402 RARVAEALEEVGL-DPAARHR-YPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAY 479
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 332 LFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSLA 385
Cdd:COG4172 480 LFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
417-669 |
2.34e-70 |
|
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: 237.88 E-value: 2.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 417 EHIITVDHLTKEFKlprkKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPT---SGKVFYEGRDTSTFK 493
Cdd:COG1123 2 TPLLEVRDLSVRYP----GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 494 SKDLlgfRRHVQPVFQNPYGSLDPMySIFRSIEEPLRIHKIGDKKWRAnRVKELLDMVEMpASVMGRYPNELSGGQRQRI 573
Cdd:COG1123 78 EALR---GRRIGMVFQDPMTQLNPV-TVGDQIAEALENLGLSRAEARA-RVLELLEAVGL-ERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 574 AIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVF 653
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
250
....*....|....*.
gi 2545376782 654 DHPQKqytrdlLDAIP 669
Cdd:COG1123 232 AAPQA------LAAVP 241
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
419-668 |
1.61e-69 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 227.65 E-value: 1.61e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFK---LPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSK 495
Cdd:PRK10419 3 LLNVSGLSHHYAhggLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 496 DLLGFRRHVQPVFQNPYGSLDPMYSIFRSIEEPLRiHKIG-DKKWRANRVKELLDMVEMPASVMGRYPNELSGGQRQRIA 574
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLR-HLLSlDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 575 IARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEV-- 652
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKlt 241
|
250
....*....|....*.
gi 2545376782 653 FDHPQkqyTRDLLDAI 668
Cdd:PRK10419 242 FSSPA---GRVLQNAV 254
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-390 |
4.60e-66 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 220.37 E-value: 4.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDTG------KPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEE 91
Cdd:COG4608 6 PLLEVRDLKKHFPVRGGlfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTS----GEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 92 IAGAKQSEFDKLRgTKMGLVPQDPMSNLNPVWRIGTQVKEALKANNMdvahekrsalakalagdevevkgnddetflgak 171
Cdd:COG4608 82 ITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGL--------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 172 elpelmteakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyVTGSTM 251
Cdd:COG4608 128 --------------------------------------------------------------------------ASKAER 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 252 DDRIAGLLSEAGL-PDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTA 330
Cdd:COG4608 134 RERVAELLELVGLrPEHADR---YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLT 210
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 331 VLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSL----ASQRII 390
Cdd:COG4608 211 YLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQALLSAVPVPdperRRERIV 274
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
420-668 |
1.77e-62 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 211.58 E-value: 1.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKLPRKKemFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLG 499
Cdd:PRK11153 2 IELKNISKVFPQGGRT--IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQ--NPYGSldpmYSIFRSIEEPLRIHKIGDKKWRAnRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIAR 577
Cdd:PRK11153 80 ARRQIGMIFQhfNLLSS----RTVFDNVALPLELAGTPKAEIKA-RVTELLELVGL-SDKADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 578 AMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQ 657
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
250
....*....|.
gi 2545376782 658 KQYTRDLLDAI 668
Cdd:PRK11153 234 HPLTREFIQST 244
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-386 |
2.38e-62 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 210.75 E-value: 2.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFTtDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGHVVNGSIKLDGEEIAGAKQS 98
Cdd:PRK11022 3 LLNVDKLSVHFG-DESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 99 EFDKLRGTKMGLVPQDPMSNLNPVWRIGTQVKEALKAnnmdvaHEkrsalakalagdevevkgnddetflgakelpelmt 178
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKV------HQ----------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 179 eakkalteagvsgeafdkavarftnewvpGSETRWRvaddlikagvaddlikagvaddqawylakkyvtgstmDDRIAGL 258
Cdd:PRK11022 121 -----------------------------GGNKKTR-------------------------------------RQRAIDL 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 LSEAGLPDAATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDL 338
Cdd:PRK11022 135 LNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDL 214
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2545376782 339 GLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSLAS 386
Cdd:PRK11022 215 ALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALPEFAQ 262
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-384 |
1.57e-61 |
|
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: 205.81 E-value: 1.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFTTDTGKpVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAkqs 98
Cdd:COG1124 1 MLEVRNLSVSYGQGGRR-VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS----GEVTFDGRPVTRR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 99 eFDKLRGTKMGLVPQDPMSNLNPVWRIGTQVKEALKANNMDvahekrsalakalagdevevkgnddetflgakelpelmt 178
Cdd:COG1124 73 -RRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLP--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 179 eakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgsTMDDRIAGL 258
Cdd:COG1124 113 -----------------------------------------------------------------------DREERIAEL 121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 LSEAGLPDAAtrARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDL 338
Cdd:COG1124 122 LEQVGLPPSF--LDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDL 199
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2545376782 339 GLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSL 384
Cdd:COG1124 200 AVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRELLAASLAF 245
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
416-660 |
3.52e-60 |
|
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: 201.75 E-value: 3.52e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKEFklprkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSK 495
Cdd:COG1127 2 SEPMIEVRNLTKSF------GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 496 DLLGFRRHVQPVFQNP--YGSLdpmySIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPaSVMGRYPNELSGGQRQRI 573
Cdd:COG1127 76 ELYELRRRIGMLFQGGalFDSL----TVFENVAFPLREHTDLSEAEIRELVLEKLELVGLP-GAADKMPSELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 574 AIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVF 653
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
250
....*....|
gi 2545376782 654 --DHPQ-KQY 660
Cdd:COG1127 231 asDDPWvRQF 240
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
417-645 |
9.89e-60 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 199.88 E-value: 9.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 417 EHIITVDHLTKEFklPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKD 496
Cdd:COG1136 2 SPLLELRNLTKSY--GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 497 LLGFRR-HVQPVFQNPYgsLDPMYSIFRSIEEPLRIHKIGDKKwRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAI 575
Cdd:COG1136 80 LARLRRrHIGFVFQFFN--LLPELTALENVALPLLLAGVSRKE-RRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 576 ARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRqIADEVVVMQHGKLVE 645
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
420-643 |
2.08e-59 |
|
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: 198.87 E-value: 2.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlpRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLG 499
Cdd:cd03255 1 IELKNLSKTYG--GGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRR-HVQPVFQNPYgsLDPMYSIFRSIEEPLRIHKIGDKKWRAnRVKELLDMVEMPASvMGRYPNELSGGQRQRIAIARA 578
Cdd:cd03255 79 FRRrHIGFVFQSFN--LLPDLTALENVELPLLLAGVPKKERRE-RAEELLERVGLGDR-LNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 579 MALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRqIADEVVVMQHGKL 643
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
419-668 |
2.54e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 196.75 E-value: 2.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFKLprkkemFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTsTFKSKDLL 498
Cdd:COG1126 1 MIEIENLHKSFGD------LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDIN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 GFRRHVQPVFQNPygSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASvMGRYPNELSGGQRQRIAIARA 578
Cdd:COG1126 74 KLRRKVGMVFQQF--NLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADK-ADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 579 MALDPDVIVCDEAVSALD-VLVQDqVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQ 657
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDpELVGE-VLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQ 228
|
250
....*....|.
gi 2545376782 658 KQYTRDLLDAI 668
Cdd:COG1126 229 HERTRAFLSKV 239
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
442-660 |
2.70e-58 |
|
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: 196.57 E-value: 2.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 442 DDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLGFRRHVQPVFQNP--YGSLdpmy 519
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQSGalFDSL---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 SIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVmGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLV 599
Cdd:cd03261 93 TVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 600 QDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVF--DHPQ-KQY 660
Cdd:cd03261 172 SGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPLvRQF 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
420-667 |
3.27e-58 |
|
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: 196.75 E-value: 3.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFkskDLLG 499
Cdd:cd03295 1 IEFENVTKRYG-----GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ---DPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNPygSLDPMYSIFRSIEEPLRIHKIGDKKWRAnRVKELLDMVEM-PASVMGRYPNELSGGQRQRIAIARA 578
Cdd:cd03295 73 LRRKIGYVIQQI--GLFPHMTVEENIALVPKLLKWPKEKIRE-RADELLALVGLdPAEFADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 579 MALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQK 658
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
|
....*....
gi 2545376782 659 QYTRDLLDA 667
Cdd:cd03295 230 DFVAEFVGA 238
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
419-657 |
1.36e-57 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 198.78 E-value: 1.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFKlprkkeMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfkskDLL 498
Cdd:COG3842 5 ALELENVSKRYG------DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-----GLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 GFRRHVQPVFQNpYgSLDPMYSIFRSIEEPLRIHKIgDKKWRANRVKELLDMVEMPAsVMGRYPNELSGGQRQRIAIARA 578
Cdd:COG3842 74 PEKRNVGMVFQD-Y-ALFPHLTVAENVAFGLRMRGV-PKAEIRARVAELLELVGLEG-LADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 579 MALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHD----LAvvrqIADEVVVMQHGKLVEHATTDEVFD 654
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIEQVGTPEEIYE 225
|
...
gi 2545376782 655 HPQ 657
Cdd:COG3842 226 RPA 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
419-671 |
1.93e-57 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 203.40 E-value: 1.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFKlpRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLkPT------SGKVFYEGRDTSTF 492
Cdd:PRK15134 5 LLAIENLSVAFR--QQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 493 KSKDLLGFR-RHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKiGDKKwRANRVKEL--LDMV--EMPASVMGRYPNELSG 567
Cdd:PRK15134 82 SEQTLRGVRgNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHR-GMRR-EAARGEILncLDRVgiRQAAKRLTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 568 GQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHA 647
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQN 239
|
250 260
....*....|....*....|....
gi 2545376782 648 TTDEVFDHPQKQYTRDLLDAIPGG 671
Cdd:PRK15134 240 RAATLFSAPTHPYTQKLLNSEPSG 263
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
412-669 |
9.50e-57 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 195.71 E-value: 9.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 412 TLEKSEHIITVDHLTKEFKLPrkKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKP---TSGKVFYEGRD 488
Cdd:PRK09473 5 AQQQADALLDVKDLRVTFSTP--DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 489 TSTFKSKDLLGFR-RHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASV--MGRYPNEL 565
Cdd:PRK09473 83 ILNLPEKELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARkrMKMYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 566 SGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVE 645
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
250 260
....*....|....*....|....
gi 2545376782 646 HATTDEVFDHPQKQYTRDLLDAIP 669
Cdd:PRK09473 243 YGNARDVFYQPSHPYSIGLLNAVP 266
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
420-658 |
1.30e-56 |
|
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: 191.78 E-value: 1.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTkeFKLPRKKemfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTstfKSKDLLG 499
Cdd:COG1122 1 IELENLS--FSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNPygslDpmYSIF-RSIEE----PLRIHKIgDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIA 574
Cdd:COG1122 73 LRRKVGLVFQNP----D--DQLFaPTVEEdvafGPENLGL-PREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 575 IARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFD 654
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
....
gi 2545376782 655 HPQK 658
Cdd:COG1122 224 DYEL 227
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
39-381 |
2.47e-55 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 188.35 E-value: 2.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 39 AVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGHVVNGSIKLDGEEIAGAKqsefdkLRGTKMGLVPQDPMSN 118
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 119 LNPVWRIGTQVKEALKAnnmdvaHEKRSALAKALagdevevkgnddetflgakelpelMTEAkkalteagvsgeafdkav 198
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRS------LGKLSKQARAL------------------------ILEA------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 199 arftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmddriaglLSEAGLPDAATRARQFPHEF 278
Cdd:TIGR02770 107 ------------------------------------------------------------LEAVGLPDPEEVLKKYPFQL 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVE 358
Cdd:TIGR02770 127 SGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVE 206
|
330 340
....*....|....*....|...
gi 2545376782 359 SGPSLEVLQHPQHPYTKRLVAAA 381
Cdd:TIGR02770 207 RGTVKEIFYNPKHETTRKLLSAH 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
420-665 |
2.73e-55 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 192.28 E-value: 2.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprkkeMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKS-KDll 498
Cdd:COG1118 3 IEVRNISKRFG------SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPpRE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 gfrRHVQPVFQNPygSLDPMYSIFRSIEEPLRIHKIGDKKWRAnRVKELLDMVEMP--AsvmGRYPNELSGGQRQRIAIA 576
Cdd:COG1118 75 ---RRVGFVFQHY--ALFPHMTVAENIAFGLRVRPPSKAEIRA-RVEELLELVQLEglA---DRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 577 RAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHP 656
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
....*....
gi 2545376782 657 QKQYTRDLL 665
Cdd:COG1118 226 ATPFVARFL 234
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
419-669 |
8.17e-55 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 190.34 E-value: 8.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFKlpRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLL----KPTSGKVFYEGRDTSTFKS 494
Cdd:PRK11022 3 LLNVDKLSVHFG--DESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 495 K---DLLGfrRHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMP--ASVMGRYPNELSGGQ 569
Cdd:PRK11022 81 KerrNLVG--AEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 570 RQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATT 649
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
250 260
....*....|....*....|
gi 2545376782 650 DEVFDHPQKQYTRDLLDAIP 669
Cdd:PRK11022 239 HDIFRAPRHPYTQALLRALP 258
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
420-647 |
1.36e-54 |
|
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: 185.80 E-value: 1.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKLPRkkemfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfkskDLLG 499
Cdd:cd03259 1 LELKGLSKTYGSVR------ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-----GVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNPygSLDPMYSIFRSIEEPLRIHKIGDKKWRAnRVKELLDMVEMPAsVMGRYPNELSGGQRQRIAIARAM 579
Cdd:cd03259 70 ERRNIGMVFQDY--ALFPHLTVAENIAFGLKLRGVPKAEIRA-RVRELLELVGLEG-LLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHA 647
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
416-669 |
3.84e-53 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 193.53 E-value: 3.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKEFKLPRKKemFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGR-------- 487
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQK--IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 488 --DTSTFKSKDLLGFR-RHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPAS--VMGRYP 562
Cdd:PRK10261 87 viELSEQSAAQMRHVRgADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAqtILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 563 NELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGK 642
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260
....*....|....*....|....*..
gi 2545376782 643 LVEHATTDEVFDHPQKQYTRDLLDAIP 669
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYTRALLAAVP 273
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
420-669 |
2.03e-52 |
|
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: 182.07 E-value: 2.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEF-KLPR-----------KKEMFK------AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGK 481
Cdd:cd03294 1 IKIKGLYKIFgKNPQkafkllakgksKEEILKktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 482 VFYEGRDTSTFKSKDLLGFRRH-VQPVFQNpYGsLDPMYSIFRSIEEPLRIHKIGdKKWRANRVKELLDMVEMPASvMGR 560
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKkISMVFQS-FA-LLPHRTVLENVAFGLEVQGVP-RAEREERAAEALELVGLEGW-EHK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 561 YPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLV----QDQVLRllndLQAEKGLSYLFITHDLAVVRQIADEVV 636
Cdd:cd03294 157 YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIrremQDELLR----LQAELQKTIVFITHDLDEALRLGDRIA 232
|
250 260 270
....*....|....*....|....*....|...
gi 2545376782 637 VMQHGKLVEHATTDEVFDHPQKQYTRDLLDAIP 669
Cdd:cd03294 233 IMKDGRLVQVGTPEEILTNPANDYVREFFRGVD 265
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
416-668 |
2.01e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 178.74 E-value: 2.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKEFklPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGrdtstfksK 495
Cdd:COG1116 4 AAPALELRGVSKRF--PTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--------K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 496 DLLGFRRHVQPVFQNPygSLDPMYSIFRSIEEPLRIHKIGDKKWRAnRVKELLDMVEMpASVMGRYPNELSGGQRQRIAI 575
Cdd:COG1116 74 PVTGPGPDRGVVFQEP--ALLPWLTVLDNVALGLELRGVPKAERRE-RARELLELVGL-AGFEDAYPHQLSGGMRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 576 ARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDL--AVVrqIADEVVVMQH--GKLVE------ 645
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVdeAVF--LADRVVVLSArpGRIVEeidvdl 227
|
250 260
....*....|....*....|....*
gi 2545376782 646 -HATTDEVFDHPQ-KQYTRDLLDAI 668
Cdd:COG1116 228 pRPRDRELRTSPEfAALRAEILDLL 252
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
417-665 |
3.05e-51 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 178.83 E-value: 3.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 417 EHIITVDHLTKEFK----LPRKKEMfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTS-- 490
Cdd:PRK15112 2 ETLLEVRNLSKTFRyrtgWFRRQTV-EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 491 --TFKSKdllgfrrHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVMGRYPNELSGG 568
Cdd:PRK15112 81 dySYRSQ-------RIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 569 QRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHAT 648
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
250
....*....|....*..
gi 2545376782 649 TDEVFDHPQKQYTRDLL 665
Cdd:PRK15112 234 TADVLASPLHELTKRLI 250
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
420-657 |
5.15e-51 |
|
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: 177.15 E-value: 5.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFklprkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDllg 499
Cdd:cd03296 3 IEVRNVSKRF------GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 frRHVQPVFQNpYGSLDPMySIFRSIEEPLRIHKIGDKKWRAN---RVKELLDMVEMpASVMGRYPNELSGGQRQRIAIA 576
Cdd:cd03296 74 --RNVGFVFQH-YALFRHM-TVFDNVAFGLRVKPRSERPPEAEiraKVHELLKLVQL-DWLADRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 577 RAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHP 656
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
.
gi 2545376782 657 Q 657
Cdd:cd03296 229 A 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
420-657 |
2.37e-50 |
|
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: 175.12 E-value: 2.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFklprkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfkskDLLG 499
Cdd:cd03300 1 IELENVSKFY------GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-----NLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNpYgSLDPMYSIFRSIEEPLRIHKIgDKKWRANRVKELLDMVEMPAsVMGRYPNELSGGQRQRIAIARAM 579
Cdd:cd03300 70 HKRPVNTVFQN-Y-ALFPHLTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQLEG-YANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQ 657
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
420-652 |
4.15e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 174.48 E-value: 4.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprkkeMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTstfkSKDLLG 499
Cdd:COG1131 1 IEVRGLTKRYG------DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNPygSLDPmysiFRSIEEPL----RIHKIgDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAI 575
Cdd:COG1131 71 VRRRIGYVPQEP--ALYP----DLTVRENLrffaRLYGL-PRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 576 ARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEV 652
Cdd:COG1131 143 ALALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
420-638 |
9.20e-50 |
|
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: 173.04 E-value: 9.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFklPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGrdtstfksKDLLG 499
Cdd:cd03293 1 LEVRNVSKTY--GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNPygSLDPMYSIFRSIEEPLRIHKIGDKKWRAnRVKELLDMVEMPASVmGRYPNELSGGQRQRIAIARAM 579
Cdd:cd03293 71 PGPDRGYVFQQD--ALLPWLTVLDNVALGLELQGVPKAEARE-RAEELLELVGLSGFE-NAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDL--AVVrqIADEVVVM 638
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIdeAVF--LADRVVVL 205
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
419-669 |
2.59e-49 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 175.84 E-value: 2.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFKLPRKKemFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLL 498
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKT--IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 GFRRHVQPVFQnpYGSLDPMYSIFRSIEEPLRIHKIGDKKWRaNRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARA 578
Cdd:TIGR02314 79 KARRQIGMIFQ--HFNLLSSRTVFGNVALPLELDNTPKDEIK-RKVTELLALVGL-GDKHDSYPSNLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 579 MALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQ- 657
Cdd:TIGR02314 155 LASNPKVLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKt 234
|
250
....*....|....*.
gi 2545376782 658 ---KQYTRDLLD-AIP 669
Cdd:TIGR02314 235 plaQKFIRSTLHlSIP 250
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
420-642 |
2.03e-48 |
|
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: 167.75 E-value: 2.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprkkeMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTfKSKDLLG 499
Cdd:cd03229 1 LELKNVSKRYG------QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTD-LEDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNPygSLDPMYSIFRSIEEPLrihkigdkkwranrvkelldmvempasvmgrypnelSGGQRQRIAIARAM 579
Cdd:cd03229 74 LRRRIGMVFQDF--ALFPHLTVLENIALGL------------------------------------SGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGK 642
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
422-642 |
1.55e-47 |
|
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: 166.49 E-value: 1.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 422 VDHLTkeFKLPRKKEmfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfR 501
Cdd:cd03225 2 LKNLS--FSYPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 502 RHVQPVFQNPYGSLdpmysIFRSIEE----PLRIHKIgDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIAR 577
Cdd:cd03225 75 RKVGLVFQNPDDQF-----FGPTVEEevafGLENLGL-PEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 578 AMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGK 642
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
420-656 |
2.41e-47 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 170.64 E-value: 2.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprkkeMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDllg 499
Cdd:COG3839 4 LELENVSKSYG------GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 frRHVQPVFQNPygSLDPMYSIFRSIEEPLRIHKIgDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAM 579
Cdd:COG3839 75 --RNIAMVFQSY--ALYPHMTVYENIAFPLKLRKV-PKAEIDRRVREAAELLGL-EDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHP 656
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
438-652 |
2.68e-47 |
|
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: 166.59 E-value: 2.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 438 FKAVDDVSFSVKRGTTLAIVGESGSGKST---VANMVLHLLK--PTSGKVFYEGRDTSTfKSKDLLGFRRHVQPVFQNPy 512
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIPgaPDEGEVLLDGKDIYD-LDVDVLELRRRVGMVFQKP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 513 gSLDPMySIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVMGR-YPNELSGGQRQRIAIARAMALDPDVIVCDEA 591
Cdd:cd03260 91 -NPFPG-SIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545376782 592 VSALDVLVQDQVLRLLNDLQAEkgLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEV 652
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
419-645 |
3.84e-47 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 166.00 E-value: 3.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFklPRKKEmfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLL 498
Cdd:COG2884 1 MIRFENVSKRY--PGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 GFRRHVQPVFQNpYGSLDPMySIFRSIEEPLRIHKIGDKKWRAnRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARA 578
Cdd:COG2884 76 YLRRRIGVVFQD-FRLLPDR-TVYENVALPLRVTGKSRKEIRR-RVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 579 MALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAeKGLSYLFITHDLAVVRQIADEVVVMQHGKLVE 645
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-397 |
3.96e-47 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 169.37 E-value: 3.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDTG--KP---VHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEI 92
Cdd:PRK11308 4 PLLQAIDLKKHYPVKRGlfKPerlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTG----GELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 93 AGAKQSEfDKLRGTKMGLVPQDPMSNLNPVWRIGTQVKEALKANNMDVAHEKRsalAKALAgdevevkgnddetflgake 172
Cdd:PRK11308 80 LKADPEA-QKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERR---EKALA------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 173 lpelmteakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmd 252
Cdd:PRK11308 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 driagLLSEAGL-PDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAV 331
Cdd:PRK11308 137 -----MMAKVGLrPEHYDR---YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSY 208
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 332 LFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSL----ASQRIisaKERGE 397
Cdd:PRK11308 209 VFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATPRLnpddRRERI---KLTGE 275
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
420-658 |
4.36e-47 |
|
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: 167.22 E-value: 4.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTkeFKLPRKKEmfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTfkSKDLLG 499
Cdd:TIGR04520 1 IEVENVS--FSYPESEK--PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EENLWE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNP----YGSLdpmysifrsIEE------------PLRIHKigdkkwranRVKELLDMVEMpASVMGRYPN 563
Cdd:TIGR04520 75 IRKKVGMVFQNPdnqfVGAT---------VEDdvafglenlgvpREEMRK---------RVDEALKLVGM-EDFRDREPH 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 564 ELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKL 643
Cdd:TIGR04520 136 LLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKI 214
|
250
....*....|....*
gi 2545376782 644 VEHATTDEVFDHPQK 658
Cdd:TIGR04520 215 VAEGTPREIFSQVEL 229
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
12-381 |
6.04e-47 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 166.91 E-value: 6.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 12 MQKEHGPLLEVKDLAIDFTtDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEE 91
Cdd:COG4107 1 MTNEEQPLLSVRGLSKRYG-PGCGTVVACRDVSFDLYPGEVLGIVGESGSGKST----LLKCLYFDLAPTSGSVYYRDRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 92 -----IAGAKQSEFDKLRGTKMGLVPQDPMSNLNpvwrigtqvkealkannMDVAhekrsalakalAGdevevkGNddet 166
Cdd:COG4107 76 ggprdLFALSEAERRRLRRTDWGMVYQNPRDGLR-----------------MDVS-----------AG------GN---- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 167 flgakelpelmteakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagVADDLIKAGvaddqawylAKKYv 246
Cdd:COG4107 118 ---------------------------------------------------------IAERLMAAG---------ERHY- 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 247 tgSTMDDRIAGLLSEAGLPdaATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDS 326
Cdd:COG4107 131 --GDIRARALEWLERVEIP--LERIDDLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRE 206
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 327 LGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAA 381
Cdd:COG4107 207 LGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
424-669 |
1.38e-46 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 168.16 E-value: 1.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 424 HLTKEFKLPrkKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKP----TSGKVFYEGRD---TSTFKSKD 496
Cdd:COG4170 8 NLTIEIDTP--QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDllkLSPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 497 LLGfrRHVQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDK-----KWRANRVKELLDMV--EMPASVMGRYPNELSGGQ 569
Cdd:COG4170 86 IIG--REIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVgiKDHKDIMNSYPHELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 570 RQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATT 649
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPT 243
|
250 260
....*....|....*....|
gi 2545376782 650 DEVFDHPQKQYTRDLLDAIP 669
Cdd:COG4170 244 EQILKSPHHPYTKALLRSMP 263
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
394-652 |
8.34e-46 |
|
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: 173.87 E-value: 8.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 394 ERGEDADALLDHHIAGEstleksehiITVDHLTkeFKLPRKKEmfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLH 473
Cdd:COG2274 457 EREEGRSKLSLPRLKGD---------IELENVS--FRYPGDSP--PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 474 LLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPYgsldpmysIF-RSIEEPLRIHK--IGDKK-WRANRVKELLD 549
Cdd:COG2274 524 LYEPTSGRILIDGIDLRQIDPASL---RRQIGVVLQDVF--------LFsGTIRENITLGDpdATDEEiIEAARLAGLHD 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 550 MVE-MPA------SVMGRypnELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLsyLFIT 622
Cdd:COG2274 593 FIEaLPMgydtvvGEGGS---NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTV--IIIA 667
|
250 260 270
....*....|....*....|....*....|
gi 2545376782 623 HDLAVVRQiADEVVVMQHGKLVEHATTDEV 652
Cdd:COG2274 668 HRLSTIRL-ADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
427-665 |
8.86e-46 |
|
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: 162.50 E-value: 8.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 427 KEFKLprkkemfkavDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKdllgfRRHVQP 506
Cdd:cd03299 11 KEFKL----------KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 507 VFQNPYgsLDPMYSIFRSIEEPLRiHKIGDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVI 586
Cdd:cd03299 76 VPQNYA--LFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 587 VCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQKQYTRDLL 665
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-383 |
1.13e-45 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 165.46 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDTGkPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGHVVNGSIKLDGEEIAGAKQ 97
Cdd:COG4170 2 PLLDIRNLTIEIDTPQG-RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 98 SEFDKLRGTKMGLVPQDPMSNLNPVWRIGTQVKEALkannmdvahekrsalakalagdevevkgnDDETFLGakelpelm 177
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAI-----------------------------PSWTFKG-------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 178 teakkalteagvsgeafdkavaRFTNEWvpgsetRWRvaddlikagvaddlikagvaddqawylaKKYVtgstmddrIAg 257
Cdd:COG4170 124 ----------------------KWWQRF------KWR----------------------------KKRA--------IE- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 LLSEAGLPDAATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHD 337
Cdd:COG4170 139 LLHRVGIKDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHD 218
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2545376782 338 LGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPS 383
Cdd:COG4170 219 LESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALLRSMPD 264
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
419-671 |
6.81e-45 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 160.61 E-value: 6.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFklPRKKemfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLL 498
Cdd:COG3638 2 MLELRNLSKRY--PGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 GFRRHVQPVFQNPY-------------GSLdPMYSIFRSIeepLRIHKIGDKkwraNRVKELLDMVEMPASVMGRyPNEL 565
Cdd:COG3638 77 RLRRRIGMIFQQFNlvprlsvltnvlaGRL-GRTSTWRSL---LGLFPPEDR----ERALEALERVGLADKAYQR-ADQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 566 SGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLve 645
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV-- 225
|
250 260
....*....|....*....|....*.
gi 2545376782 646 hattdeVFDHPQKQYTRDLLDAIPGG 671
Cdd:COG3638 226 ------VFDGPPAELTDAVLREIYGG 245
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
420-642 |
8.63e-45 |
|
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: 157.54 E-value: 8.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTkeFKLPRKKEmfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlg 499
Cdd:cd03228 1 IEFKNVS--FSYPGRPK--PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 fRRHVQPVFQNPYgsldpmysIF-RSIEEplrihkigdkkwranrvkelldmvempasvmgrypNELSGGQRQRIAIARA 578
Cdd:cd03228 75 -RKNIAYVPQDPF--------LFsGTIRE-----------------------------------NILSGGQRQRIAIARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 579 MALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLsyLFITHDLAVVRQiADEVVVMQHGK 642
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
419-668 |
1.77e-44 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 159.71 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFKlPRKkemfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFkskDLL 498
Cdd:PRK11701 6 LLSVRGLTKLYG-PRK-----GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLR---DLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 GF----RRHVQP-----VFQNPYGSLDPMYSIFRSIEEPLRihKIGDKKWRANRVKEL--LDMVEMPASVMGRYPNELSG 567
Cdd:PRK11701 77 ALseaeRRRLLRtewgfVHQHPRDGLRMQVSAGGNIGERLM--AVGARHYGDIRATAGdwLERVEIDAARIDDLPTTFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 568 GQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHA 647
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
250 260
....*....|....*....|.
gi 2545376782 648 TTDEVFDHPQKQYTRDLLDAI 668
Cdd:PRK11701 235 LTDQVLDDPQHPYTQLLVSSV 255
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
40-384 |
2.31e-43 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 156.78 E-value: 2.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 40 VRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGHVVNGSIKLDGEEIAGAKqsefdkLRGTKMGLVPQDPMSNL 119
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVAPCA------LRGRKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 120 NPVWRIGTQVKEALKAnnmdvahekrsalakalagdevevkgnddetflgakelpelmteakkalteagvsgeafdkava 199
Cdd:PRK10418 93 NPLHTMHTHARETCLA---------------------------------------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 200 rftnewvpgsetrwrvaddlikagvaddlikAGVADDqawylakkyvtgstmDDRIAGLLSEAGLPDAATRARQFPHEFS 279
Cdd:PRK10418 109 -------------------------------LGKPAD---------------DATLTAALEAVGLENAARVLKLYPFEMS 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 280 GGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVES 359
Cdd:PRK10418 143 GGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQ 222
|
330 340
....*....|....*....|....*
gi 2545376782 360 GPSLEVLQHPQHPYTKRLVAAAPSL 384
Cdd:PRK10418 223 GDVETLFNAPKHAVTRSLVSAHLAL 247
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
442-643 |
4.86e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 154.20 E-value: 4.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 442 DDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFkskDLLGFRRHVQPVFQNPYgsldpmysI 521
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM---PPPEWRRQVAYVPQEPA--------L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 522 FR-SIEEPL-RIHKIGDKKWRANRVKELLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLV 599
Cdd:COG4619 86 WGgTVRDNLpFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPEN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2545376782 600 QDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKL 643
Cdd:COG4619 166 TRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
415-675 |
5.05e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 155.25 E-value: 5.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 415 KSEHIITVDHLTkeFKLPRKKemfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfKS 494
Cdd:COG1121 2 MMMPAIELENLT--VSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR--RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 495 KDLLGF---RRHVQPVFqnpygsldPMysifrSIEE--------PLRIHKIGDKKWRAnRVKELLDMVEMpASVMGRYPN 563
Cdd:COG1121 74 RRRIGYvpqRAEVDWDF--------PI-----TVRDvvlmgrygRRGLFRRPSRADRE-AVDEALERVGL-EDLADRPIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 564 ELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGkL 643
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-L 216
|
250 260 270
....*....|....*....|....*....|..
gi 2545376782 644 VEHATTDEVFdhpqkqyTRDLLDAIPGGKLQL 675
Cdd:COG1121 217 VAHGPPEEVL-------TPENLSRAYGGPVAL 241
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
422-657 |
8.25e-43 |
|
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: 154.52 E-value: 8.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 422 VDHLTKEFKlprkkeMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDL--LG 499
Cdd:cd03219 3 VRGLTKRFG------GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRhvqpVFQNPygsldpmySIFR--SIEEPLRI-------HKIGDKKWRA------NRVKELLDMVEMpASVMGRYPNE 564
Cdd:cd03219 77 IGR----TFQIP--------RLFPelTVLENVMVaaqartgSGLLLARARReerearERAEELLERVGL-ADLADRPAGE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 565 LSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:cd03219 144 LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
250
....*....|...
gi 2545376782 645 EHATTDEVFDHPQ 657
Cdd:cd03219 223 AEGTPDEVRNNPR 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
12-382 |
8.74e-43 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 157.56 E-value: 8.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 12 MQKEHGPLLEVKDLAIDFTTDTGKP--------VHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnG 83
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDIKDGKQwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATD----G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 84 SIKLDGEEIAGAKQSEFDKLRgTKMGLVPQDPMSNLNPVWRIGTQVKEALKannmdvahekrsalakalagdevevkgnd 163
Cdd:PRK15079 77 EVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLR----------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 164 deTFLgakelPELmteakkalteagvsgeafdkavarftnewvPGSETRWRVADDLIKAGVaddlikagvaddqawylak 243
Cdd:PRK15079 127 --TYH-----PKL------------------------------SRQEVKDRVKAMMLKVGL------------------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 244 kyvtgstmddriagllseagLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHML 323
Cdd:PRK15079 151 --------------------LPNLINR---YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL 207
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 324 TDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAP 382
Cdd:PRK15079 208 QREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
441-667 |
4.20e-42 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 153.32 E-value: 4.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKP----TSGKVFYEGRDTStfkSKDLLGfrRHVQPVFQNPYGSLD 516
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVA---PCALRG--RKIATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 517 PMYSIFRSIEEPLRihKIGdKKWRANRVKELLDMV--EMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSA 594
Cdd:PRK10418 94 PLHTMHTHARETCL--ALG-KPADDATLTAALEAVglENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 595 LDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQKQYTRDLLDA 667
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
420-668 |
6.35e-42 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 152.32 E-value: 6.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKLPRkkemfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDtstfKSKDLLG 499
Cdd:COG4555 2 IEVENLSKKYGKVP------ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED----VRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNPYgsldpMYSiFRSIEEPLR----IHKIGDKKWRAnRVKELLDMVEMPaSVMGRYPNELSGGQRQRIAI 575
Cdd:COG4555 72 ARRQIGVLPDERG-----LYD-RLTVRENIRyfaeLYGLFDEELKK-RIEELIELLGLE-EFLDRRVGELSTGMKKKVAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 576 ARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVfdh 655
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL--- 219
|
250
....*....|...
gi 2545376782 656 pQKQYTRDLLDAI 668
Cdd:COG4555 220 -REEIGEENLEDA 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
420-645 |
9.79e-42 |
|
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: 150.87 E-value: 9.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprkkeMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDllg 499
Cdd:cd03301 1 VELENVTKRFG------NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 frRHVQPVFQNpYgSLDPMYSIFRSIEEPLRIHKIGDK--KWRANRVKELLDMVEmpasVMGRYPNELSGGQRQRIAIAR 577
Cdd:cd03301 72 --RDIAMVFQN-Y-ALYPHMTVYDNIAFGLKLRKVPKDeiDERVREVAELLQIEH----LLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 578 AMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVE 645
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
408-651 |
1.38e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 159.56 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 408 AGESTLEKSEHIITVDHLTkeFKLPRKKEmfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGR 487
Cdd:COG1132 328 PGAVPLPPVRGEIEFENVS--FSYPGDRP---VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 488 DTSTFKSKDLlgfRRHVQPVFQNPYgsldpmysIF-RSIEEPLRIHKIG---DKKWRANRVKELLDMVE-MP---ASVMG 559
Cdd:COG1132 403 DIRDLTLESL---RRQIGVVPQDTF--------LFsGTIRENIRYGRPDatdEEVEEAAKAAQAHEFIEaLPdgyDTVVG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 560 RYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDV----LVQDQVLRLLndlqaeKGLSYLFITHDLAVVRQiADEV 635
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTeteaLIQEALERLM------KGRTTIVIAHRLSTIRN-ADRI 544
|
250
....*....|....*.
gi 2545376782 636 VVMQHGKLVEHATTDE 651
Cdd:COG1132 545 LVLDDGRIVEQGTHEE 560
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
441-591 |
4.71e-41 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 146.64 E-value: 4.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDtstFKSKDLLGFRRHVQPVFQNPygSLDPMYS 520
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKEIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 521 IFRSIEEPLRIHKIGD--KKWRANRVKELLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEA 591
Cdd:pfam00005 76 VRENLRLGLLLKGLSKreKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
420-668 |
6.01e-41 |
|
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: 149.64 E-value: 6.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLG 499
Cdd:cd03256 1 IEVENLSKTYP-----NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNP-------------YGSLDPMySIFRSIeepLRIHKIGDKkwraNRVKELLDMVEMpASVMGRYPNELS 566
Cdd:cd03256 76 LRRQIGMIFQQFnlierlsvlenvlSGRLGRR-STWRSL---FGLFPKEEK----QRALAALERVGL-LDKAYQRADQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 567 GGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLveh 646
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI--- 223
|
250 260
....*....|....*....|..
gi 2545376782 647 attdeVFDHPQKQYTRDLLDAI 668
Cdd:cd03256 224 -----VFDGPPAELTDEVLDEI 240
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
420-643 |
1.11e-40 |
|
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: 147.68 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprkkeMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTsTFKSKDLLG 499
Cdd:cd03262 1 IEIKNLHKSFG------DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNPYgsLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAM 579
Cdd:cd03262 74 LRQKVGMVFQQFN--LFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKL 643
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
417-658 |
1.28e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 149.78 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 417 EHIITVDHLTkeFKLPRKKEMfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRdtsTFKSKD 496
Cdd:PRK13635 3 EEIIRVEHIS--FRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 497 LLGFRRHVQPVFQNP----YGSL---DPMYSI-FRSIEEPLRIhkigdkkwraNRVKELLDMVEMpASVMGRYPNELSGG 568
Cdd:PRK13635 76 VWDVRRQVGMVFQNPdnqfVGATvqdDVAFGLeNIGVPREEMV----------ERVDQALRQVGM-EDFLNREPHRLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 569 QRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHAT 648
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGT 223
|
250
....*....|
gi 2545376782 649 TDEVFDHPQK 658
Cdd:PRK13635 224 PEEIFKSGHM 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
419-668 |
1.58e-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: 148.65 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTkeFKLPRKKemfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLl 498
Cdd:COG1120 1 MLEAENLS--VGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 gfRRHVQPVFQNPYGSLDpmYSIFRSIEEPLRIHKIGDKKWRAN---RVKELLDMVEMpASVMGRYPNELSGGQRQRIAI 575
Cdd:COG1120 74 --ARRIAYVPQEPPAPFG--LTVRELVALGRYPHLGLFGRPSAEdreAVEEALERTGL-EHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 576 ARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFdh 655
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL-- 226
|
250
....*....|...
gi 2545376782 656 pqkqyTRDLLDAI 668
Cdd:COG1120 227 -----TPELLEEV 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
438-663 |
1.86e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 148.65 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 438 FKAVDDVSFSVKRGTTLAIVGESGSGKSTvanmvlhLLK---------P---TSGKVFYEGRDTSTfKSKDLLGFRRHVQ 505
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKST-------LLRclnrmndliPgarVEGEILLDGEDIYD-PDVDVVELRRRVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 506 PVFQ--NPYgsldPMySIFRSIEEPLRIHKIGDKKWRANRVKELL----------DMVEMPASvmgrypnELSGGQRQRI 573
Cdd:COG1117 96 MVFQkpNPF----PK-SIYDNVAYGLRLHGIKSKSELDEIVEESLrkaalwdevkDRLKKSAL-------GLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 574 AIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkglsY--LFITHDLAVVRQIADEVVVMQHGKLVEHATTDE 651
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD----YtiVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQ 239
|
250
....*....|..
gi 2545376782 652 VFDHPQKQYTRD 663
Cdd:COG1117 240 IFTNPKDKRTED 251
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
397-651 |
8.00e-40 |
|
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: 154.15 E-value: 8.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 397 EDADALLD----HHIAGESTLEKSEHI-ITVDHLTkeFKLPRKKEmfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMV 471
Cdd:COG4988 309 EKIFALLDapepAAPAGTAPLPAAGPPsIELEDVS--FSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 472 LHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPYgsldpmysIFR-SIEEPLRIHKIG---DKKWRANRVKEL 547
Cdd:COG4988 384 LGFLPPYSGSILINGVDLSDLDPASW---RRQIAWVPQNPY--------LFAgTIRENLRLGRPDasdEELEAALEAAGL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 548 LDMVE-MP---ASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLsyLFITH 623
Cdd:COG4988 453 DEFVAaLPdglDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV--ILITH 530
|
250 260
....*....|....*....|....*...
gi 2545376782 624 DLAVVRQiADEVVVMQHGKLVEHATTDE 651
Cdd:COG4988 531 RLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
420-651 |
6.57e-39 |
|
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: 143.28 E-value: 6.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFklprkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfksKDLLG 499
Cdd:cd03265 1 IEVENLVKKY------GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNPygSLDPMYSIFRSIEEPLRIHKIGDKKWRaNRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAM 579
Cdd:cd03265 71 VRRRIGIVFQDL--SVDDELTGWENLYIHARLYGVPGAERR-ERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDE 651
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
420-643 |
6.74e-39 |
|
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: 141.38 E-value: 6.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprkkeMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKdllg 499
Cdd:cd03230 1 IEVRNLSKRYG------KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNPygSLDPMYSifrsieeplrihkigdkkwranrVKELLDmvempasvmgrypneLSGGQRQRIAIARAM 579
Cdd:cd03230 71 VKRRIGYLPEEP--SLYENLT-----------------------VRENLK---------------LSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKL 643
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-382 |
8.52e-39 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 152.32 E-value: 8.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDTG------KPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEE 91
Cdd:PRK10261 312 PILQVRNLVTRFPLRSGllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG----GEIIFNGQR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 92 IAGAKQSEFDKLRgTKMGLVPQDPMSNLNPVWRIGTQVKEALKANNMdvahekrsalakalagdevevkgnddetflgak 171
Cdd:PRK10261 388 IDTLSPGKLQALR-RDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGL--------------------------------- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 172 elpelmteakkalteagvsgeafdkavarftnewVPGSETRWRVaddlikagvaddlikagvaddqAWYLAKkyvtgstm 251
Cdd:PRK10261 434 ----------------------------------LPGKAAAARV----------------------AWLLER-------- 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 252 ddriAGLLSEaglpdaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAV 331
Cdd:PRK10261 450 ----VGLLPE--------HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAY 517
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 332 LFITHDLGLaAERAQH-IVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAP 382
Cdd:PRK10261 518 LFISHDMAV-VERISHrVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
456-660 |
1.31e-38 |
|
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: 145.71 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 456 IVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSkdllgFRRHVQPVFQNpYgSLDPMYSIFRSIEEPLRIHKIg 535
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP-----HLRHINMVFQS-Y-ALFPHMTVEENVAFGLKMRKV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 536 DKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKG 615
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2545376782 616 LSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQKQY 660
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
18-380 |
1.51e-38 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 143.53 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTtdtgkPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLG-LLPGTGHVVNGSIKLDGEEIAGAK 96
Cdd:PRK11701 5 PLLSVRGLTKLYG-----PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSArLAPDAGEVHYRMRDGQLRDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 97 QSEFDKLRGTKMGLVPQDPMSNLNPVWRIGTQVKEALKAnnmdvahekrsalakalagdevevkgnddetfLGAKELPEL 176
Cdd:PRK11701 80 EAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLMA--------------------------------VGARHYGDI 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 177 MTEAkkalteagvsgeafdkavarftnewvpgseTRWrvaddlikagvaddlikagvaddqawyLAKKYVTGSTMDDRia 256
Cdd:PRK11701 128 RATA------------------------------GDW---------------------------LERVEIDAARIDDL-- 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 257 gllseaglpdaatrarqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITH 336
Cdd:PRK11701 149 ------------------PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTH 210
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2545376782 337 DLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAA 380
Cdd:PRK11701 211 DLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
441-644 |
2.80e-38 |
|
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: 139.88 E-value: 2.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQnpygsldpmys 520
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---ARKIAYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 521 ifrsieeplrihkigdkkwrANRVKELLDMVEmpasvmgRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQ 600
Cdd:cd03214 81 --------------------ALELLGLAHLAD-------RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2545376782 601 DQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
413-657 |
3.25e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 142.97 E-value: 3.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 413 LEKSEHIITVDHLTKEFKlprKKEMFkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEgrdTSTF 492
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQ---SDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYN---NQAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 493 KSKDLLGFRRHVQPVFQNP----YGSLdPMYSIFRSIEEPLRIHkigDKKWRanRVKELLDMVEMPASVmGRYPNELSGG 568
Cdd:PRK13648 74 TDDNFEKLRKHIGIVFQNPdnqfVGSI-VKYDVAFGLENHAVPY---DEMHR--RVSEALKQVDMLERA-DYEPNALSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 569 QRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHAT 648
Cdd:PRK13648 147 QKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGT 225
|
....*....
gi 2545376782 649 TDEVFDHPQ 657
Cdd:PRK13648 226 PTEIFDHAE 234
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
420-676 |
5.91e-38 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 144.46 E-value: 5.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFklprkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDllg 499
Cdd:PRK10851 3 IEIANIKKSF------GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 frRHVQPVFQNpYGSLDPMySIFRSIEEPLRI---HKIGDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIA 576
Cdd:PRK10851 74 --RKVGFVFQH-YALFRHM-TVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQL-AHLADRYPAQLSGGQKQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 577 RAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHP 656
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
250 260
....*....|....*....|....*..
gi 2545376782 657 QKQYTRDLLD-------AIPGGKLQLG 676
Cdd:PRK10851 229 ATRFVLEFMGevnrlqgTIRGGQFHVG 255
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
416-653 |
7.26e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 142.05 E-value: 7.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTkeFKLPRKKEMfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfkSK 495
Cdd:PRK13632 4 KSVMIKVENVS--FSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS---KE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 496 DLLGFRRHVQPVFQNPygslDPMYsIFRSIEEP----LRIHKIGDKKWRAnRVKELLDMVEMpASVMGRYPNELSGGQRQ 571
Cdd:PRK13632 77 NLKEIRKKIGIIFQNP----DNQF-IGATVEDDiafgLENKKVPPKKMKD-IIDDLAKKVGM-EDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 572 RIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDE 651
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKE 228
|
..
gi 2545376782 652 VF 653
Cdd:PRK13632 229 IL 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
439-642 |
9.33e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 137.76 E-value: 9.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQnpygsldpm 518
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL---RRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 519 ysifrsieeplrihkigdkkwranrvkelldmvempasvmgrypneLSGGQRQRIAIARAMALDPDVIVCDEAVSALDVL 598
Cdd:cd00267 81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2545376782 599 VQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGK 642
Cdd:cd00267 115 SRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
420-654 |
1.13e-37 |
|
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: 140.06 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTkeFKLPRKKEmfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlg 499
Cdd:cd03251 1 VEFKNVT--FRYPGDGP--PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 fRRHVQPVFQNPYgsldpmysIFR-SIEEPLRIHKIG---DKKWRANRVKELLDMV-EMPA---SVMGRYPNELSGGQRQ 571
Cdd:cd03251 75 -RRQIGLVSQDVF--------LFNdTVAENIAYGRPGatrEEVEEAARAANAHEFImELPEgydTVIGERGVKLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 572 RIAIARAMALDPDVIVCDEAVSALDV----LVQDQVLRLLndlqaeKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHA 647
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTeserLVQAALERLM------KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
....*..
gi 2545376782 648 TTDEVFD 654
Cdd:cd03251 219 THEELLA 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
378-651 |
3.69e-37 |
|
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: 146.45 E-value: 3.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 378 VAAAPSLASQ--RIISAKER-GEDADALLDHHIAGESTLEKSEHIITVDHLTkeFKLPrkKEMFKAVDDVSFSVKRGTTL 454
Cdd:COG4987 289 LAPLPAAAQHlgRVRAAARRlNELLDAPPAVTEPAEPAPAPGGPSLELEDVS--FRYP--GAGRPVLDGLSLTLPPGERV 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 455 AIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPYgsldpmysIFR-SIEEPLRIHK 533
Cdd:COG4987 365 AIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---RRRIAVVPQRPH--------LFDtTLRENLRLAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 534 IG---DKKWRA-NRVkELLDMVE-MPA---SVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLR 605
Cdd:COG4987 434 PDatdEELWAAlERV-GLGDWLAaLPDgldTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLA 512
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2545376782 606 LLNDLQAEKGLsyLFITHDLAVVRQiADEVVVMQHGKLVEHATTDE 651
Cdd:COG4987 513 DLLEALAGRTV--LLITHRLAGLER-MDRILVLEDGRIVEQGTHEE 555
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
438-669 |
3.83e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 140.30 E-value: 3.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 438 FKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRdTSTFKSKD--LLGFRRHVQPVFQNPYGSL 515
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDI-TITHKTKDkyIRPVRKRIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 516 --DpmySIFRSIEeplrihkIGDKKWRAN--RVKE----LLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIV 587
Cdd:PRK13646 99 feD---TVEREII-------FGPKNFKMNldEVKNyahrLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 588 CDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDhpQKQYTRDLLDA 667
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK--DKKKLADWHIG 246
|
..
gi 2545376782 668 IP 669
Cdd:PRK13646 247 LP 248
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
18-358 |
4.45e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 138.25 E-value: 4.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDTGKpVHAVRDANFTVYPGQWVAIVGESGSGKSTsAMAVLGLL--PGTGhvvngSIKLDGEEIAGA 95
Cdd:COG1136 3 PLLELRNLTKSYGTGEGE-VTALRGVSLSIEAGEFVAIVGPSGSGKST-LLNILGGLdrPTSG-----EVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 96 KQSEFDKLRGTKMGLVPQDPmsNLNPVWrigtqvkealkannmdvahekrSALakalagDEVEvkgnddetflgakeLPe 175
Cdd:COG1136 76 SERELARLRRRHIGFVFQFF--NLLPEL----------------------TAL------ENVA--------------LP- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 176 lmteakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddLIKAGVADDQAwylakkyvtgstmDDRI 255
Cdd:COG1136 111 ----------------------------------------------------LLLAGVSRKER-------------RERA 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 256 AGLLSEAGLPDaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFIT 335
Cdd:COG1136 126 RELLERVGLGD---RLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVT 202
|
330 340
....*....|....*....|...
gi 2545376782 336 HDLGLAAeRAQHIVVMYKGQVVE 358
Cdd:COG1136 203 HDPELAA-RADRVIRLRDGRIVS 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
439-658 |
4.49e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 140.16 E-value: 4.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRD-TSTFKSKDLLGFRRHVQPVFQNPYGSL-- 515
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERViTAGKKNKKLKPLRKKVGIVFQFPEHQLfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 516 ---------DPMYsiFRSIEEplrihkigDKKWRAnrvKELLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVI 586
Cdd:PRK13634 101 etvekdicfGPMN--FGVSEE--------DAKQKA---REMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 587 VCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQK 658
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
428-651 |
6.05e-37 |
|
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: 138.06 E-value: 6.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 428 EFKLPRKKEMfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPV 507
Cdd:cd03249 7 SFRYPSRPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL---RSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 508 FQNP---YGSL--DPMYSIFRSIEEPLRihkigdkkwRANRVKELLDMVEM-P---ASVMGRYPNELSGGQRQRIAIARA 578
Cdd:cd03249 83 SQEPvlfDGTIaeNIRYGKPDATDEEVE---------EAAKKANIHDFIMSlPdgyDTLVGERGSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 579 MALDPDVIVCDEAVSALDVLVQDQVLRLLNdlQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDE 651
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALD--RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
441-656 |
8.81e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 141.01 E-value: 8.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTsTFKSKDllgfRRHVQPVFQNpYgSLDPMYS 520
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQ----QRDICMVFQS-Y-ALFPHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 521 IFRSIEEPLRIHKIGdKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQ 600
Cdd:PRK11432 95 LGENVGYGLKMLGVP-KEERKQRVKEALELVDL-AGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 601 DQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHP 656
Cdd:PRK11432 173 RSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
439-676 |
9.82e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 139.19 E-value: 9.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRD-TSTFKSKDLLGFRRHVQPVFQNPYGSLDP 517
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHiTPETGNKNLKKLRKKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 518 mYSIFRSIEEPLRIHKIGDKKWRaNRVKELLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDV 597
Cdd:PRK13641 101 -NTVLKDVEFGPKNFGFSEDEAK-EKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 598 LVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHP---QKQYTRDLLDAIPGGKLQ 674
Cdd:PRK13641 179 EGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKewlKKHYLDEPATSRFASKLE 257
|
..
gi 2545376782 675 LG 676
Cdd:PRK13641 258 KG 259
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
440-654 |
1.15e-36 |
|
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: 136.97 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPYgsldpmy 519
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---RSMIGVVLQDTF------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 sIF-RSIEEPLRIHK--IGDKKW-RANRVKELLDMVE-MP---ASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEA 591
Cdd:cd03254 88 -LFsGTIMENIRLGRpnATDEEViEAAKEAGAHDFIMkLPngyDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 592 VSALDV----LVQDQVLRLLndlqaeKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDEVFD 654
Cdd:cd03254 167 TSNIDTetekLIQEALEKLM------KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
18-380 |
2.25e-36 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 137.66 E-value: 2.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDTG----KPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIa 93
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGlfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTS----GEILINGHKL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 94 gakQSEFDKLRGTKMGLVPQDPMSNLNPVWRIGTQVKEALKANnmdvahekrsalakalagdevevkgnddeTFLGAKEL 173
Cdd:COG4167 78 ---EYGDYKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLN-----------------------------TDLTAEER 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 174 PELmteakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagVADDLIKAGVADDQAWYlakkyvtgstmdd 253
Cdd:COG4167 126 EER-----------------------------------------------IFATLRLVGLLPEHANF------------- 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 254 riagllseaglpdaatrarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLF 333
Cdd:COG4167 146 --------------------YPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIY 205
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2545376782 334 ITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAA 380
Cdd:COG4167 206 VSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHEVTKRLIES 252
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
443-644 |
3.31e-36 |
|
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: 135.50 E-value: 3.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTlAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGR---DTStfKSKDLLGFRRHVQPVFQNpyGSLDPMY 519
Cdd:cd03297 16 KIDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSR--KKINLPPQQRKIGLVFQQ--YALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 SIFRSIEEPLRIHKIGDKKWRANRVKELLDMvempASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLV 599
Cdd:cd03297 91 NVRENLAFGLKRKRNREDRISVDELLDLLGL----DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2545376782 600 QDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
439-653 |
3.57e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 137.49 E-value: 3.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTsTFKSKDLLGFRRHVQPVFQNPYGSLDPM 518
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDIRKKVGLVFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 519 ySIFRSIEEPLRIHKIGDKKWRaNRVKELLDMVEMPASVM-GRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDV 597
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIE-NRVKRAMNIVGLDYEDYkDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 598 LVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVF 653
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
440-638 |
4.52e-36 |
|
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: 134.97 E-value: 4.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfKSKDLLGFrrhvqpVFQNPygSLDPMY 519
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--KERKRIGY------VPQRR--SIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 SIfrSIEE--------PLRIHKIGDKKWRAnRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEA 591
Cdd:cd03235 84 PI--SVRDvvlmglygHKGLFRRLSKADKA-KVDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545376782 592 VSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVM 638
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
438-657 |
6.89e-36 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 135.53 E-value: 6.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 438 FKAVDDVSFSVKRGTTLAIVGESGSGKSTVANmVLHLLK-PTSGKVFYEGRD---TSTFKSKDLLGFRRHVQPVFQNpYg 513
Cdd:COG4161 15 HQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLEtPDSGQLNIAGHQfdfSQKPSEKAIRLLRQKVGMVFQQ-Y- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 514 SLDPMYSIFRS-IEEPLRIHKIGDKKWRAnRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAV 592
Cdd:COG4161 92 NLWPHLTVMENlIEAPCKVLGLSKEQARE-KAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 593 SALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTdEVFDHPQ 657
Cdd:COG4161 170 AALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQ 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
439-660 |
7.59e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 135.14 E-value: 7.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANmVLHLLK-PTSGKVFYEGRD---TSTFKSKDLLGFRRHVQPVFQNpYgS 514
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEmPRSGTLNIAGNHfdfSKTPSDKAIRELRRNVGMVFQQ-Y-N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 515 LDPMYSIFRS-IEEPLRIHKIgDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVS 593
Cdd:PRK11124 93 LWPHLTVQQNlIEAPCRVLGL-SKDQALARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545376782 594 ALDVLVQDQVLRLLNDLQaEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEvFDHPQ----KQY 660
Cdd:PRK11124 171 ALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQteafKNY 239
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
420-651 |
1.17e-35 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 142.41 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTkeFKLPRKKEmfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlg 499
Cdd:PRK13657 335 VEFDDVS--FSYDNSRQ---GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 fRRHVQPVFQnpygslDPMysIF-RSIEEPLRIHKIG---DKKWRANRVKELLDMVEMPAS----VMGRYPNELSGGQRQ 571
Cdd:PRK13657 408 -RRNIAVVFQ------DAG--LFnRSIEDNIRVGRPDatdEEMRAAAERAQAHDFIERKPDgydtVVGERGRQLSGGERQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 572 RIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQaeKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDE 651
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDE 555
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
420-666 |
1.19e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 134.88 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprKKEMFKAVDdvsFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKS----K 495
Cdd:PRK11264 4 IEVKNLVKKFH---GQTVLHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 496 DLL-GFRRHVQPVFQNpyGSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIA 574
Cdd:PRK11264 78 GLIrQLRQHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 575 IARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFD 654
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
250
....*....|..
gi 2545376782 655 HPQKQYTRDLLD 666
Cdd:PRK11264 234 DPQQPRTRQFLE 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-381 |
1.73e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 141.00 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 10 LAMQKEHGPLLEVKDLAIDFTTDTG------KPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGtghvvNG 83
Cdd:PRK15134 266 VPLPEPASPLLDVEQLQVAFPIRKGilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-----QG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 84 SIKLDGEEIAGAKQSEFDKLRgTKMGLVPQDPMSNLNPVWRIGTQVKEALKannmdVAHEKRSALAKalagdevevkgnd 163
Cdd:PRK15134 341 EIWFDGQPLHNLNRRQLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLR-----VHQPTLSAAQR------------- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 164 detflgakelpelmteakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylak 243
Cdd:PRK15134 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 244 kyvtgstmDDRIAGLLSEAGLpDAATRARqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHML 323
Cdd:PRK15134 402 --------EQQVIAVMEEVGL-DPETRHR-YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 324 TDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAA 381
Cdd:PRK15134 472 QQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLALS 529
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
416-653 |
2.33e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 135.22 E-value: 2.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKEFKLPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfKSK 495
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 496 DLLGFRRHVQPVFQNPYGSLdpmysIFRSIEE------------PLRIHKigdkkwranRVKELLDMVEMpaSVMGRY-P 562
Cdd:PRK13633 79 NLWDIRNKAGMVFQNPDNQI-----VATIVEEdvafgpenlgipPEEIRE---------RVDESLKKVGM--YEYRRHaP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 563 NELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQiADEVVVMQHGK 642
Cdd:PRK13633 143 HLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGK 221
|
250
....*....|.
gi 2545376782 643 LVEHATTDEVF 653
Cdd:PRK13633 222 VVMEGTPKEIF 232
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
18-381 |
3.87e-35 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 133.80 E-value: 3.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTtdtgkPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLG-LLPGTGHVVNGSIKLDGEEIAGAK 96
Cdd:TIGR02323 2 PLLQVSGLSKSYG-----GGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrLAPDHGTATYIMRSGAELELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 97 QSEFDKLRGTKMGLVPQDPMSNLNPVWRIGTQVKEALKAnnmdvahekrsalakalagdevevkgnddetfLGAKELPEL 176
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMA--------------------------------IGARHYGNI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 177 MTEAKKALTEAGvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlIKAGVADDQawylakkyvtgstmddria 256
Cdd:TIGR02323 125 RATAQDWLEEVE----------------------------------------IDPTRIDDL------------------- 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 257 gllseaglpdaatrarqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITH 336
Cdd:TIGR02323 146 ------------------PRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTH 207
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2545376782 337 DLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAA 381
Cdd:TIGR02323 208 DLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-386 |
3.96e-35 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 135.70 E-value: 3.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDTGkPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGHVVNGSIKLDGEEIAGAKQ 97
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDG-WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 98 SEFDKLRGTKMGLVPQDPMSNLNPVWRIGTQVKEAlkannmdvahekrsalakalagdevevkgnddetflgakelpelm 177
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQN--------------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 178 teakkalteagvsgeafdkavarftnewVPGS--ETRWRvaddlikagvaddlikagvaddQAWYLAKKyvtgstmddRI 255
Cdd:PRK15093 116 ----------------------------IPGWtyKGRWW----------------------QRFGWRKR---------RA 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 256 AGLLSEAGLPDAATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFIT 335
Cdd:PRK15093 137 IELLHRVGIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLIS 216
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2545376782 336 HDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSLAS 386
Cdd:PRK15093 217 HDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQALIRAIPDFGS 267
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
415-653 |
1.08e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 134.21 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 415 KSEHIITVDHLTKEFKlPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKV----FYEGRDTS 490
Cdd:PRK13631 17 SDDIILRVKNLYCVFD-EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 491 TF---------KSKDLLGFRRHVQPVFQNPygsldpMYSIFR-SIEEPLRIHKI--GDKKWRA-NRVKELLDMVEMPASV 557
Cdd:PRK13631 96 NHelitnpyskKIKNFKELRRRVSMVFQFP------EYQLFKdTIEKDIMFGPValGVKKSEAkKLAKFYLNKMGLDDSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 558 MGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVV 637
Cdd:PRK13631 170 LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIV 248
|
250
....*....|....*.
gi 2545376782 638 MQHGKLVEHATTDEVF 653
Cdd:PRK13631 249 MDKGKILKTGTPYEIF 264
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
438-651 |
1.13e-34 |
|
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: 131.58 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 438 FKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDtstFKSKDLLGFRRHVQPVFQNP------ 511
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD---IREVTLDSLRRAIGVVPQDTvlfndt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 512 ------YGSLDpmySIFRSIEEPLRIHKIGDKkwranrvkelldMVEMP---ASVMGRYPNELSGGQRQRIAIARAMALD 582
Cdd:cd03253 91 igynirYGRPD---ATDEEVIEAAKAAQIHDK------------IMRFPdgyDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 583 PDVIVCDEAVSALDVLVQDQVLRLLNDLQaeKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDE 651
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
417-678 |
1.80e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 132.55 E-value: 1.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 417 EHIITVDHLTkeFKLPRKKEMFkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfkSKD 496
Cdd:PRK13650 2 SNIIEVKNLT--FKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 497 LLGFRRHVQPVFQNPygslDPMYsIFRSIEEPLRI---HKIGDKKWRANRVKELLDMVEMPASVMgRYPNELSGGQRQRI 573
Cdd:PRK13650 76 VWDIRHKIGMVFQNP----DNQF-VGATVEDDVAFgleNKGIPHEEMKERVNEALELVGMQDFKE-REPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 574 AIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVrQIADEVVVMQHGKlVEHATTdevf 653
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQ-VESTST---- 223
|
250 260
....*....|....*....|....*..
gi 2545376782 654 dhPQKQYTR--DLldaipggkLQLGLD 678
Cdd:PRK13650 224 --PRELFSRgnDL--------LQLGLD 240
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
419-669 |
2.78e-34 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 133.39 E-value: 2.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFKLPrkKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKpTSGKVfyeGRDTSTFKSKDLL 498
Cdd:PRK15093 3 LLDIRNLTIEFKTS--DGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRV---TADRMRFDDIDLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 GF----RR-----HVQPVFQNPYGSLDPMYSIFRSIEEPL-----------RIHkigdkkWRANRVKELLDMVEM--PAS 556
Cdd:PRK15093 77 RLspreRRklvghNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtykgrwwqRFG------WRKRRAIELLHRVGIkdHKD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 557 VMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVV 636
Cdd:PRK15093 151 AMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKIN 230
|
250 260 270
....*....|....*....|....*....|...
gi 2545376782 637 VMQHGKLVEHATTDEVFDHPQKQYTRDLLDAIP 669
Cdd:PRK15093 231 VLYCGQTVETAPSKELVTTPHHPYTQALIRAIP 263
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
442-665 |
3.12e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 130.60 E-value: 3.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 442 DDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLgFRRHVQPVFQNPYgsLDPMYSI 521
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL-IRQEAGMVFQQFY--LFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 522 FRSIE-EPLRIHkiGDKKWRANRV-KELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLV 599
Cdd:PRK09493 95 LENVMfGPLRVR--GASKEEAEKQaRELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 600 QDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQKQYTRDLL 665
Cdd:PRK09493 172 RHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-652 |
3.22e-34 |
|
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: 137.24 E-value: 3.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIDFttdtgKPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSikldGEEIagakqse 99
Cdd:TIGR03269 1 IEVKNLTKKF-----DGKEVLKNISFTIEEGEVLGILGRSGAGKSV----LMHVLRGMDQYEPTS----GRII------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 fdklrgTKMGLVPQdpMSNLNPVWRIGTQVKEAlkannmdvahekrsalAKALAGDEVEVKGNDDETFLGAKELPELMte 179
Cdd:TIGR03269 61 ------YHVALCEK--CGYVERPSKVGEPCPVC----------------GGTLEPEEVDFWNLSDKLRRRIRKRIAIM-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 180 akkalteagvsgeaFDKAVARFTNEwvpgsetrwRVADDLIKAgvaddLIKAGVADDQAWYLAKKYVTGSTMDDRIAGLl 259
Cdd:TIGR03269 115 --------------LQRTFALYGDD---------TVLDNVLEA-----LEEIGYEGKEAVGRAVDLIEMVQLSHRITHI- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 260 seaglpdaatrARqfphEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLG 339
Cdd:TIGR03269 166 -----------AR----DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 340 LAAERAQHIVVMYKGQVVESGPSLEVLQhpqhpytkRLVAAAPSLASQRIIsakERGEDADALLDhhiagestleKSEHI 419
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEVVA--------VFMEGVSEVEKECEV---EVGEPIIKVRN----------VSKRY 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDhltkefklprkKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYE-GRDTSTFKSKDLL 498
Cdd:TIGR03269 290 ISVD-----------RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPD 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 GFRRHVQPVfqnpyGSLDPMYSIF--RSIEEPLrIHKIG---DKKWRANRVKELLDMV----EMPASVMGRYPNELSGGQ 569
Cdd:TIGR03269 359 GRGRAKRYI-----GILHQEYDLYphRTVLDNL-TEAIGlelPDELARMKAVITLKMVgfdeEKAEEILDKYPDELSEGE 432
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 570 RQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATT 649
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
...
gi 2545376782 650 DEV 652
Cdd:TIGR03269 513 EEI 515
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
437-643 |
5.12e-34 |
|
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: 129.06 E-value: 5.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 437 MFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLGFRRHVQPVFQNpyGSLD 516
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 517 PMYSIFRSIEEPLRIHKIGDKKWRaNRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALD 596
Cdd:cd03292 91 PDRNVYENVAFALEVTGVPPREIR-KRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545376782 597 VLVQDQVLRLLNDLQAeKGLSYLFITHDLAVVRQIADEVVVMQHGKL 643
Cdd:cd03292 169 PDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
445-665 |
1.68e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 128.33 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 445 SFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfkskDLLGFRRHVQPVFQNpyGSLDPMYSIFRS 524
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT-----ALPPAERPVSMLFQE--NNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 525 IEepLRIH---KIGDKKWRanRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQD 601
Cdd:COG3840 92 IG--LGLRpglKLTAEQRA--QVEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 602 QVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQKQYTRDLL 665
Cdd:COG3840 167 EMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
416-657 |
1.73e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 129.92 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTkeFKLPRKKEmfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSK 495
Cdd:PRK13640 2 KDNIVEFKHVS--FTYPDSKK--PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 496 DLLGFRRHVQPVFQNPYGSL-------DPMYSI-FRSIEEPlRIHKIgdkkwrANRVKELLDMVEMPASvmgrYPNELSG 567
Cdd:PRK13640 78 TVWDIREKVGIVFQNPDNQFvgatvgdDVAFGLeNRAVPRP-EMIKI------VRDVLADVGMLDYIDS----EPANLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 568 GQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHA 647
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQG 225
|
250
....*....|
gi 2545376782 648 TTDEVFDHPQ 657
Cdd:PRK13640 226 SPVEIFSKVE 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-652 |
1.91e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 134.38 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTtdtgkPVHAVRDANFTVYPGQWVAIVGESGSGKSTsAMAVL-GLLPGTGhvvnGSIKLDGEE--IAG 94
Cdd:COG1129 3 PLLEMRGISKSFG-----GVKALDGVSLELRPGEVHALLGENGAGKST-LMKILsGVYQPDS----GEILLDGEPvrFRS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 95 AKQSEfdklrgtKMG--LVPQDPmsNLnpvwrigtqvkealkANNMDVAhekrsalakalagdevevkgndDETFLGake 172
Cdd:COG1129 73 PRDAQ-------AAGiaIIHQEL--NL---------------VPNLSVA----------------------ENIFLG--- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 173 lpelmteakkalteagvsgeafdkavarftnewvpgsetRWRVaddlikagvaddliKAGVADDQAwylakkyvtgstMD 252
Cdd:COG1129 104 ---------------------------------------REPR--------------RGGLIDWRA------------MR 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 DRIAGLLSEAGLP-DAATRARqfphEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAV 331
Cdd:COG1129 119 RRARELLARLGLDiDPDTPVG----DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAI 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 332 LFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHpqhpytkRLVAAapslasqrIIsakerGEDADALLDHHIAges 411
Cdd:COG1129 194 IYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTED-------ELVRL--------MV-----GRELEDLFPKRAA--- 250
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 412 tlEKSEHIITVDHLTKEfklprkkemfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTsT 491
Cdd:COG1129 251 --APGEVVLEVEGLSVG----------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-R 317
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 492 FKS-------------KDllgfrRHVQPVFQNpygsldpmysifRSIEEPL------RIHKIG--DKKWRANRVKELLDM 550
Cdd:COG1129 318 IRSprdairagiayvpED-----RKGEGLVLD------------LSIRENItlasldRLSRGGllDRRRERALAEEYIKR 380
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 551 VEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQ 630
Cdd:COG1129 381 LRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLG 459
|
650 660
....*....|....*....|....*..
gi 2545376782 631 IADEVVVMQHGKLV-----EHATTDEV 652
Cdd:COG1129 460 LSDRILVMREGRIVgeldrEEATEEAI 486
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
420-644 |
2.33e-33 |
|
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: 125.62 E-value: 2.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFklprkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLg 499
Cdd:cd03216 1 LELRGITKRF------GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 fRRHVQPVFQnpygsldpmysifrsieeplrihkigdkkwranrvkelldmvempasvmgrypneLSGGQRQRIAIARAM 579
Cdd:cd03216 74 -RAGIAMVYQ-------------------------------------------------------LSVGERQMVEIARAL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-370 |
2.46e-33 |
|
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: 127.83 E-value: 2.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAidFTTDTGKPvhAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEIagaKQSE 99
Cdd:COG1122 1 IELENLS--FSYPGGTP--ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT----SGEVLVDGKDI---TKKN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 FDKLRgTKMGLVPQDPMSNLnpvwrIGTQVKEalkannmDVAhekrsalakalagdevevkgnddetFlgakelpelmte 179
Cdd:COG1122 70 LRELR-RKVGLVFQNPDDQL-----FAPTVEE-------DVA-------------------------F------------ 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 180 akkALTEAGVSGEafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgsTMDDRIAGLL 259
Cdd:COG1122 100 ---GPENLGLPRE---------------------------------------------------------EIRERVEEAL 119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 260 SEAGLPDAATRArqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLG 339
Cdd:COG1122 120 ELVGLEHLADRP---PHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLD 195
|
330 340 350
....*....|....*....|....*....|.
gi 2545376782 340 LAAERAQHIVVMYKGQVVESGPSLEVLQHPQ 370
Cdd:COG1122 196 LVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
443-656 |
3.70e-33 |
|
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: 130.99 E-value: 3.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVK-RGTTlAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGR---DTStfKSKDLLGFRRHVQPVFQNPygSLDPM 518
Cdd:COG4148 17 DVDFTLPgRGVT-ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSA--RGIFLPPHRRRIGYVFQEA--RLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 519 YSIFRSIEEPLRIHKIGDKKWRANRVKELLDMvempASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVL 598
Cdd:COG4148 92 LSVRGNLLYGRKRAPRAERRISFDEVVELLGI----GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 599 VQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHP 656
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
425-668 |
5.05e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 131.69 E-value: 5.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 425 LTKEFKLpRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLGFRRH- 503
Cdd:PRK10070 29 LSKEQIL-EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKk 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 504 VQPVFQNpyGSLDPMYSIFRSIEEPLRIHKIGDKKwRANRVKELLDMVEMPASVMGrYPNELSGGQRQRIAIARAMALDP 583
Cdd:PRK10070 108 IAMVFQS--FALMPHMTVLDNTAFGMELAGINAEE-RREKALDALRQVGLENYAHS-YPDELSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 584 DVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQKQYTRD 663
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRT 263
|
....*
gi 2545376782 664 LLDAI 668
Cdd:PRK10070 264 FFRGV 268
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
440-657 |
7.31e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.89 E-value: 7.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTvanMVLHL---LKPTSGKVFYEGRDTStFKSKDLLGFRRHVQPVFQNPYGSLd 516
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKST---LFLHFngiLKPTSGEVLIKGEPIK-YDKKSLLEVRKTVGIVFQNPDDQL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 517 pmysIFRSIEE-----PLRIHKigDKKWRANRVKELLDMVEMPASvMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEA 591
Cdd:PRK13639 92 ----FAPTVEEdvafgPLNLGL--SKEEVEKRVKEALKAVGMEGF-ENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 592 VSALDVLVQDQVLRLLNDLQaEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQ 657
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
440-654 |
1.01e-32 |
|
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: 126.45 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFkskDLLGFRRHVQPVFQNpygslDPMY 519
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRRQVGVVLQE-----NVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 SifRSIEEPLRIHKIGDKKWRANRVKELLD----MVEMPA---SVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAV 592
Cdd:cd03252 89 N--RSIRDNIALADPGMSMERVIEAAKLAGahdfISELPEgydTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 593 SALDVLVQDQVLRLLNDLQAekGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDEVFD 654
Cdd:cd03252 167 SALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
443-656 |
1.02e-32 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 134.46 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPYgsldpMYSif 522
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL---HRQVALVGQEPV-----LFS-- 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 523 RSIEEPLR--IHKIGDKKWRANRVKELLD--MVEMPA---SVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSAL 595
Cdd:TIGR00958 569 GSVRENIAygLTDTPDEEIMAAAKAANAHdfIMEFPNgydTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545376782 596 DVlvqdQVLRLLNDLQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDEVFDHP 656
Cdd:TIGR00958 649 DA----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
20-356 |
1.26e-32 |
|
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: 125.29 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIDFTTDtGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTsAMAVLGLLpgtGHVVNGSIKLDGEEIAGAKQSE 99
Cdd:cd03255 1 IELKNLSKTYGGG-GEKVQALKGVSLSIEKGEFVAIVGPSGSGKST-LLNILGGL---DRPTSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 FDKLRGTKMGLVPQDPmsNLNPVwrigtqvkealkannmdvahekRSALakalagDEVEvkgnddetflgakeLPelmte 179
Cdd:cd03255 76 LAAFRRRHIGFVFQSF--NLLPD----------------------LTAL------ENVE--------------LP----- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 180 akkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddLIKAGVADDQAwylakkyvtgstmDDRIAGLL 259
Cdd:cd03255 107 ------------------------------------------------LLLAGVPKKER-------------RERAEELL 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 260 SEAGLPDaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLG 339
Cdd:cd03255 126 ERVGLGD---RLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE 202
|
330
....*....|....*..
gi 2545376782 340 LaAERAQHIVVMYKGQV 356
Cdd:cd03255 203 L-AEYADRIIELRDGKI 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
410-656 |
1.47e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 129.68 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 410 ESTLEKSeHIITVDHLTKEFklprkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDT 489
Cdd:PRK09452 6 KQPSSLS-PLVELRGISKSF------DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 490 StfkskDLLGFRRHVQPVFQNpYgSLDPMYSIFRSIEEPLRIHKIGDKKWRAnRVKELLDMVEMpASVMGRYPNELSGGQ 569
Cdd:PRK09452 79 T-----HVPAENRHVNTVFQS-Y-ALFPHMTVFENVAFGLRMQKTPAAEITP-RVMEALRMVQL-EEFAQRKPHQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 570 RQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATT 649
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
....*..
gi 2545376782 650 DEVFDHP 656
Cdd:PRK09452 230 REIYEEP 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
387-655 |
1.74e-32 |
|
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: 132.53 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 387 QRIISAKERgedADALLDHHI---AGESTLEKSEHIITVDHLTKEFKlPRKKEmfkAVDDVSFSVKRGTTLAIVGESGSG 463
Cdd:TIGR02203 298 QRGLAAAES---LFTLLDSPPekdTGTRAIERARGDVEFRNVTFRYP-GRDRP---ALDSISLVIEPGETVALVGRSGSG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 464 KSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPYGSLDpmySIFRSIEEPlRIHKIGDKK-WRAN 542
Cdd:TIGR02203 371 KSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL---RRQVALVSQDVVLFND---TIANNIAYG-RTEQADRAEiERAL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 543 RVKELLDMVE-MPA---SVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDV----LVQDQVLRLLndlqaeK 614
Cdd:TIGR02203 444 AAAYAQDFVDkLPLgldTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNeserLVQAALERLM------Q 517
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2545376782 615 GLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDEVFDH 655
Cdd:TIGR02203 518 GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLAR 557
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
416-657 |
1.76e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 126.24 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKEFKlprKKEMFKAVddvSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSK 495
Cdd:PRK10619 2 SENKLNVIDLHKRYG---EHEVLKGV---SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 496 D----------LLGFRRHVQPVFQNpYGSLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKeLLDMVEMPASVMGRYPNEL 565
Cdd:PRK10619 76 DgqlkvadknqLRLLRTRLTMVFQH-FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVK-YLAKVGIDERAQGKYPVHL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 566 SGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVE 645
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
250
....*....|..
gi 2545376782 646 HATTDEVFDHPQ 657
Cdd:PRK10619 233 EGAPEQLFGNPQ 244
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
415-668 |
3.63e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 128.41 E-value: 3.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 415 KSEHIIT----VDHLTKEFklprkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTS 490
Cdd:PRK11607 11 KTRKALTplleIRNLTKSF------DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 491 tfkskdllgfrrHVQPvFQNPYGSLDPMYSIF--RSIEEPLRIHKIGDKKWRA---NRVKELLDMVEMpASVMGRYPNEL 565
Cdd:PRK11607 85 ------------HVPP-YQRPINMMFQSYALFphMTVEQNIAFGLKQDKLPKAeiaSRVNEMLGLVHM-QEFAKRKPHQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 566 SGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVE 645
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
250 260
....*....|....*....|...
gi 2545376782 646 HATTDEVFDHPQKQYTRDLLDAI 668
Cdd:PRK11607 231 IGEPEEIYEHPTTRYSAEFIGSV 253
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
418-656 |
4.56e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 125.69 E-value: 4.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 418 HIITVDHLTKEFKLPRKkemfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfkSKDL 497
Cdd:PRK13652 2 HLIETRDLCYSYSGSKE-----ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT---KENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 498 LGFRRHVQPVFQNPYgslDPMYSifRSIEEPLRIHKIG---DKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIA 574
Cdd:PRK13652 74 REVRKFVGLVFQNPD---DQIFS--PTVEQDIAFGPINlglDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 575 IARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFD 654
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
|
..
gi 2545376782 655 HP 656
Cdd:PRK13652 228 QP 229
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
420-651 |
4.69e-32 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 132.39 E-value: 4.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprkKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFkskDLLG 499
Cdd:TIGR03797 452 IEVDRVTFRYR----PDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL---DVQA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNpyGSLDPMySIFRSI--EEPLRIhkigDKKWRANRVKELL-DMVEMPasvMGRYP------NELSGGQR 570
Cdd:TIGR03797 525 VRRQLGVVLQN--GRLMSG-SIFENIagGAPLTL----DEAWEAARMAGLAeDIRAMP---MGMHTviseggGTLSGGQR 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 571 QRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKglsyLFITHDLAVVRQiADEVVVMQHGKLVEHATTD 650
Cdd:TIGR03797 595 QRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR----IVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYD 669
|
.
gi 2545376782 651 E 651
Cdd:TIGR03797 670 E 670
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
419-655 |
9.63e-32 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 123.65 E-value: 9.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFKL----------------PRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKV 482
Cdd:COG1134 4 MIEVENVSKSYRLyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 483 FYEGRDTStfkskdLLGFRrhvqpvfqnpyGSLDPMYS-----IFRSieeplRIHKIGDKKwranrVKELLDMVE----- 552
Cdd:COG1134 84 EVNGRVSA------LLELG-----------AGFHPELTgreniYLNG-----RLLGLSRKE-----IDEKFDEIVefael 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 553 -----MPasvMGRYpnelSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQaEKGLSYLFITHDLAV 627
Cdd:COG1134 137 gdfidQP---VKTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELR-ESGRTVIFVSHSMGA 208
|
250 260
....*....|....*....|....*...
gi 2545376782 628 VRQIADEVVVMQHGKLVEHATTDEVFDH 655
Cdd:COG1134 209 VRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
419-644 |
2.51e-31 |
|
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: 121.71 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFKLPRKKemFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTST--FKSKD 496
Cdd:cd03266 1 MITADALTKRFRDVKKT--VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 497 LLGFrrhvqpvFQNPYGSLDPMySIFRSIEEPLRIHKIGDKKWRAnRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIA 576
Cdd:cd03266 79 RLGF-------VSDSTGLYDRL-TARENLEYFAGLYGLKGDELTA-RLEELADRLGM-EELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 577 RAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
420-644 |
2.69e-31 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 121.46 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprkKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKdllg 499
Cdd:cd03263 1 LQIRNLTKTYK----KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNpygslDPMYSIFrSIEEPLRIHKI--GDKKWRANRVKE-LLDMVEMPaSVMGRYPNELSGGQRQRIAIA 576
Cdd:cd03263 73 ARQSLGYCPQF-----DALFDEL-TVREHLRFYARlkGLPKSEIKEEVElLLRVLGLT-DKANKRARTLSGGMKRKLSLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 577 RAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQaeKGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
416-651 |
3.66e-31 |
|
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: 121.77 E-value: 3.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKEFKLPRkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVAnMVLH-LLKPTSGKVFYEGRDTSTFKS 494
Cdd:COG4181 5 SAPIIELRGLTKTVGTGA--GELTILKGISLEVEAGESVAIVGASGSGKSTLL-GLLAgLDRPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 495 KDLLGFR-RHVQPVFQNpygsldpmysiFRSI-----EE----PLRIHKIGDKKWRAnrvKELLDMVEMpASVMGRYPNE 564
Cdd:COG4181 82 DARARLRaRHVGFVFQS-----------FQLLptltaLEnvmlPLELAGRRDARARA---RALLERVGL-GHRLDHYPAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 565 LSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLV 644
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLV 225
|
....*..
gi 2545376782 645 EHATTDE 651
Cdd:COG4181 226 EDTAATA 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
19-366 |
6.42e-31 |
|
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: 121.69 E-value: 6.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFTtdtGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAKQS 98
Cdd:COG1120 1 MLEAENLSVGYG---GRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSS----GEVLLDGRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 99 EfdklRGTKMGLVPQDPmsnlnpvwrigtqvkealkannmdvahekrsalakalagdevevkgnddetflgakELPELMT 178
Cdd:COG1120 72 E----LARRIAYVPQEP--------------------------------------------------------PAPFGLT 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 179 eakkalteagvsgeAFDkAVAR----FTNEWvpgseTRWRVADDLIkagVADDLIKAGVADdqawyLAKKYVTgstmddr 254
Cdd:COG1120 92 --------------VRE-LVALgrypHLGLF-----GRPSAEDREA---VEEALERTGLEH-----LADRPVD------- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 255 iagllseaglpdaatrarqfphEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFI 334
Cdd:COG1120 137 ----------------------ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMV 194
|
330 340 350
....*....|....*....|....*....|..
gi 2545376782 335 THDLGLAAERAQHIVVMYKGQVVESGPSLEVL 366
Cdd:COG1120 195 LHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
443-652 |
7.94e-31 |
|
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: 124.07 E-value: 7.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRD-TSTFKSKDLLGFRRHVQPVFQNpyGSLDPMYSI 521
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlFDSRKGIFLPPEKRRIGYVFQE--ARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 522 FRSIEEPLRIHKIGDKKWRANRVKELLDMvempASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQD 601
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERVIELLGI----GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2545376782 602 QVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEV 652
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
438-655 |
8.55e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 122.42 E-value: 8.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 438 FKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRD--TSTFKSKDLLGFRRHVQPVFQNPygsl 515
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipANLKKIKEVKRLRKEIGLVFQFP---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 516 dpMYSIFR-SIEEPLR---IHKIGDKKWRANRVKELLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEA 591
Cdd:PRK13645 100 --EYQLFQeTIEKDIAfgpVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 592 VSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDH 655
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
416-652 |
9.02e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.67 E-value: 9.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKEFklPRkkemFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStFKS- 494
Cdd:COG1129 1 AEPLLEMRGISKSF--GG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 495 KDLLgfRRHVQPVFQNPygSLDPMYSIFRSI---EEPLRIHKIGDKKWRAnRVKELLDMVEM---PASVMGrypnELSGG 568
Cdd:COG1129 74 RDAQ--AAGIAIIHQEL--NLVPNLSVAENIflgREPRRGGLIDWRAMRR-RARELLARLGLdidPDTPVG----DLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 569 QRQRIAIARAMALDPDVIVCDEAVSAL---DVlvqDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKLVE 645
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLterEV---ERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVG 220
|
....*..
gi 2545376782 646 HATTDEV 652
Cdd:COG1129 221 TGPVAEL 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
420-652 |
2.06e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 121.73 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEF--KLPRKkemFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRD--------- 488
Cdd:PRK13651 3 IKVKNIVKIFnkKLPTE---LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 489 ------------TSTFKSKDLLGFRRHVQPVFQNPygsldpMYSIFRS-IEEPLRIHKI--GDKKWRA-NRVKELLDMVE 552
Cdd:PRK13651 80 kekvleklviqkTRFKKIKKIKEIRRRVGVVFQFA------EYQLFEQtIEKDIIFGPVsmGVSKEEAkKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 553 MPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQaEKGLSYLFITHDLAVVRQIA 632
Cdd:PRK13651 154 LDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWT 232
|
250 260
....*....|....*....|
gi 2545376782 633 DEVVVMQHGKLVEHATTDEV 652
Cdd:PRK13651 233 KRTIFFKDGKIIKDGDTYDI 252
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
443-648 |
2.60e-30 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 119.15 E-value: 2.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVanmvLHLL----KPTSGKVFYEGRDTSTFKSKDLLGFRRHvQPVFQNPYGSLDPM 518
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTL----LHLLggldTPTSGDVIFNGQPMSKLSSAAKAELRNQ-KLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 519 YSIFRSIEEPLRIHKIGDKKWRaNRVKELLDMVEMPASVMGRyPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVL 598
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEIN-SRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2545376782 599 VQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEvVVMQHGKLVEHAT 648
Cdd:PRK11629 180 NADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDGRLTAELS 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
20-431 |
5.69e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 121.34 E-value: 5.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIDFTTDtGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamavlgLLpgtgHVVN-------GSIKLDGEEI 92
Cdd:COG1135 2 IELENLSKTFPTK-GGPVTALDDVSLTIEKGEIFGIIGYSGAGKST-------LI----RCINllerptsGSVLVDGVDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 93 AGAKQSEFDKLRgTKMGLVPQDpmSNLnpvwrigtqvkeaLKANNmdvahekrsalakalagdeveVKGNddetflgake 172
Cdd:COG1135 70 TALSERELRAAR-RKIGMIFQH--FNL-------------LSSRT---------------------VAEN---------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 173 lpelmteakkalteagvsgeafdkavarftnewvpgsetrwrVADDLIKAGVADDLIKAgvaddqawylakkyvtgstmd 252
Cdd:COG1135 103 ------------------------------------------VALPLEIAGVPKAEIRK--------------------- 119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 dRIAGLLSEAGLPDaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVL 332
Cdd:COG1135 120 -RVAELLELVGLSD---KADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIV 195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 333 FITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSLA-SQRIISAKERGEDADALLDHHIAGES 411
Cdd:COG1135 196 LITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFLPTVLNDElPEELLARLREAAGGGRLVRLTFVGES 275
|
410 420
....*....|....*....|
gi 2545376782 412 TlekSEHIITvdHLTKEFKL 431
Cdd:COG1135 276 A---DEPLLS--ELARRFGV 290
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
438-652 |
5.97e-30 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 117.92 E-value: 5.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 438 FKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLgfRRHVQPVFQNPygsldp 517
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--RAGIGYVPEGR------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 518 mySIFR--SIEEPLR----IHKIGDKKWRANRVKELL-DMVEMpasvMGRYPNELSGGQRQRIAIARAMALDPDVIVCDE 590
Cdd:cd03224 85 --RIFPelTVEENLLlgayARRRAKRKARLERVYELFpRLKER----RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 591 AVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEV 652
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
17-351 |
6.88e-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: 118.65 E-value: 6.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 17 GPLLEVKDLAIDFTTDTGkPVHAVRDANFTVYPGQWVAIVGESGSGKST--SAMAvlGLLPGTGhvvnGSIKLDGEEIAG 94
Cdd:COG1116 5 APALELRGVSKRFPTGGG-GVTALDDVSLTVAAGEFVALVGPSGCGKSTllRLIA--GLEKPTS----GEVLVDGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 95 AkqsefdklrGTKMGLVPQDPmsNLNPvWRigtqvkealkannmdvahekrSALakalagDEVEVkgnddetflgakelp 174
Cdd:COG1116 78 P---------GPDRGVVFQEP--ALLP-WL---------------------TVL------DNVAL--------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 175 elmteakkALTEAGVSgeafdKAVARftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmdDR 254
Cdd:COG1116 104 --------GLELRGVP-----KAERR----------------------------------------------------ER 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 255 IAGLLSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDvtVQKRIL--DHLHMLTDSLGTAVL 332
Cdd:COG1116 119 ARELLELVGLAGFEDA---YPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALD--ALTRERlqDELLRLWQETGKTVL 193
|
330
....*....|....*....
gi 2545376782 333 FITHDLGLAAERAQHIVVM 351
Cdd:COG1116 194 FVTHDVDEAVFLADRVVVL 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
440-660 |
6.93e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 119.32 E-value: 6.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFkSKdLLGFRRHVQPVFQNPYGSLdpmy 519
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF-SK-LQGIRKLVGIVFQNPETQF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 sIFRSIEEPLrihKIGDKK--WRANRVKELLDMVeMPASVMGRY----PNELSGGQRQRIAIARAMALDPDVIVCDEAVS 593
Cdd:PRK13644 91 -VGRTVEEDL---AFGPENlcLPPIEIRKRVDRA-LAEIGLEKYrhrsPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 594 ALDVLVQDQVLRLLNDLQaEKGLSYLFITHDLAVVrQIADEVVVMQHGKLVEHATTDEVFDHPQKQY 660
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
18-376 |
1.09e-29 |
|
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: 117.77 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTtdtGKPVHavRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAKQ 97
Cdd:COG1127 4 PMIEVRNLTKSFG---DRVVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDS----GEILVDGQDITGLSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 98 SEFDKLRgTKMGLVPQ-----DPMSnlnpvwrigtqVKEalkanNmdVAhekrsalakalagdevevkgnddetflgake 172
Cdd:COG1127 75 KELYELR-RRIGMLFQggalfDSLT-----------VFE-----N--VA------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 173 LPelMTEAKKaLTEAgvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgsTMD 252
Cdd:COG1127 105 FP--LREHTD-LSEA--------------------------------------------------------------EIR 119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 DRIAGLLSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALD-VTVqkRILDHL-HMLTDSLGTA 330
Cdd:COG1127 120 ELVLEKLELVGLPGAADK---MPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpITS--AVIDELiRELRDELGLT 194
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2545376782 331 VLFITHDLGLAAERAQHIVVMYKGQVVESGPsLEVLQHPQHPYTKR 376
Cdd:COG1127 195 SVVVTHDLDSAFAIADRVAVLADGKIIAEGT-PEELLASDDPWVRQ 239
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
443-661 |
1.38e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 117.84 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLK------PTSGKVFYEGRDTSTFkskDLLGFRRHVQPVFQ--NPYgs 514
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQI---DAIKLRKEVGMVFQqpNPF-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 515 ldPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVMGRY---PNELSGGQRQRIAIARAMALDPDVIVCDEA 591
Cdd:PRK14246 103 --PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 592 VSALDVLVQDQVLRLLNDLQAEkgLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQKQYT 661
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
443-644 |
1.50e-29 |
|
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: 116.44 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDllgfrRHVQPVFQ--NPYGSLDPMYS 520
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-----RPVSMLFQenNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 521 IFRSIEEPLRIHKIGDKkwranRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQ 600
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQ-----AIEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2545376782 601 DQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:cd03298 165 AEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
419-676 |
2.35e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 119.04 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFKLPRKKEMFK---------------AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVF 483
Cdd:COG4586 1 IIEVENLSKTYRVYEKEPGLKgalkglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 484 YEGRDtstfKSKDLLGFRRHVQPVFQN---------PYGSLDpmysIFRsieeplRIHKIGDKKWRaNRVKELLDMVEMp 554
Cdd:COG4586 81 VLGYV----PFKRRKEFARRIGVVFGQrsqlwwdlpAIDSFR----LLK------AIYRIPDAEYK-KRLDELVELLDL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 555 ASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADE 634
Cdd:COG4586 145 GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDR 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2545376782 635 VVVMQHGKLVEHATTDEVFDH--PQKQYTRDLLDAIPGGKLQLG 676
Cdd:COG4586 225 VIVIDHGRIIYDGSLEELKERfgPYKTIVLELAEPVPPLELPRG 268
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
440-638 |
3.36e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 116.89 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTfkskdlLGFRRHVqpVFQNpyGSLDPMY 519
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG------PGADRGV--VFQK--DALLPWL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 SIFRSIEEPLRIHKIGdKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLV 599
Cdd:COG4525 92 NVLDNVAFGLRLRGVP-KAERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2545376782 600 QDQVLRLLNDLQAEKGLSYLFITHDL--AVVrqIADEVVVM 638
Cdd:COG4525 170 REQMQELLLDVWQRTGKGVFLITHSVeeALF--LATRLVVM 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-367 |
5.69e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 115.55 E-value: 5.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIDFttdtgKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAgakqSE 99
Cdd:COG1131 1 IEVRGLTKRY-----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTS----GEVRVLGEDVA----RD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 FDKLRGtKMGLVPQDPmsNLNPVWRigtqVKEALKannmdvahekrsalakalagdevevkgnddetflgakelpelmte 179
Cdd:COG1131 68 PAEVRR-RIGYVPQEP--ALYPDLT----VRENLR--------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 180 akkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawYLAKKY-VTGSTMDDRIAGL 258
Cdd:COG1131 96 ------------------------------------------------------------FFARLYgLPRKEARERIDEL 115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 LSEAGLPDAA-TRARQFphefSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHD 337
Cdd:COG1131 116 LELFGLTDAAdRKVGTL----SGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHY 190
|
330 340 350
....*....|....*....|....*....|
gi 2545376782 338 LGLAAERAQHIVVMYKGQVVESGPSLEVLQ 367
Cdd:COG1131 191 LEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-375 |
6.84e-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: 115.29 E-value: 6.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIDFTtdtGKPVHavRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAKQSE 99
Cdd:cd03261 1 IELRGLTKSFG---GRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS----GEVLIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 FDKLRgTKMGLVPQDpmsnlnpvwrigtqvkealkannmdvahekrSALakalagdevevkgnddetflgakelpelmte 179
Cdd:cd03261 72 LYRLR-RRMGMLFQS-------------------------------GAL------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 180 akkalteagvsgeaFDkavarftnewvpgSETrwrvaddlikagvaddlikagVADDQAWYLAKKYVTGSTMDDRIAGL- 258
Cdd:cd03261 89 --------------FD-------------SLT---------------------VFENVAFPLREHTRLSEEEIREIVLEk 120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 LSEAGLPDAAtraRQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDL 338
Cdd:cd03261 121 LEAVGLRGAE---DLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDL 197
|
330 340 350
....*....|....*....|....*....|....*..
gi 2545376782 339 GLAAERAQHIVVMYKGQVVESGPsLEVLQHPQHPYTK 375
Cdd:cd03261 198 DTAFAIADRIAVLYDGKIVAEGT-PEELRASDDPLVR 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
409-655 |
8.50e-29 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 121.66 E-value: 8.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 409 GESTLEKSEHIITVDHLTkeFKLPRKKEMfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRD 488
Cdd:PRK11176 331 GKRVIERAKGDIEFRNVT--FTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 489 TSTFKSKDLlgfRRHVQPVFQN------------PYGSLDpMYSIfRSIEeplrihkigdkkwRANRVKELLDMVE-MPA 555
Cdd:PRK11176 407 LRDYTLASL---RNQVALVSQNvhlfndtianniAYARTE-QYSR-EQIE-------------EAARMAYAMDFINkMDN 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 556 ---SVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKglSYLFITHDLAVVRQiA 632
Cdd:PRK11176 469 gldTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-A 545
|
250 260
....*....|....*....|...
gi 2545376782 633 DEVVVMQHGKLVEHATTDEVFDH 655
Cdd:PRK11176 546 DEILVVEDGEIVERGTHAELLAQ 568
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
41-646 |
9.77e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 120.94 E-value: 9.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 41 RDANFTVYPGQWVAIVGESGSGKSTsamavlgLLpgtgHVVNGSIKLDGEEIAGAKqsefdklrGTKMGLVPQDPmsnln 120
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKST-------LL----KILAGELEPDSGEVSIPK--------GLRIGYLPQEP----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 121 pvwrigtqvkealkannmdVAHEKRSALakalagdevevkgndDETFLGAKELPELMTEAKKALTEAGVSGEafdkavar 200
Cdd:COG0488 71 -------------------PLDDDLTVL---------------DTVLDGDAELRALEAELEELEAKLAEPDE-------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 201 ftnewvpgsetrwrvadDLIKAGVADDLIkagvADDQAWylakkyvtgsTMDDRIAGLLSEAGLPDAATRARqfPHEFSG 280
Cdd:COG0488 109 -----------------DLERLAELQEEF----EALGGW----------EAEARAEEILSGLGFPEEDLDRP--VSELSG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 281 GMRQRALIAIGLACRPDLLIADEPTSALDV-TVQKriL-DHLHmltdSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVE 358
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLeSIEW--LeEFLK----NYPGTVLVVSHDRYFLDRVATRILELDRGKLTL 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 359 -SGP-------SLEVLQHPQHPYTK-------------RLVAAApSLASQ-----------RIISAKERGEDAdalldhH 406
Cdd:COG0488 230 yPGNysayleqRAERLEQEAAAYAKqqkkiakeeefirRFRAKA-RKAKQaqsrikaleklEREEPPRRDKTV------E 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 407 IAGESTLEKSEHIITVDHLTKEFKlprKKEMFkavDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYeG 486
Cdd:COG0488 303 IRFPPPERLGKKVLELEGLSKSYG---DKTLL---DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-G 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 487 RDTStfkskdlLG-FRRHVQpvfqnpygSLDPMYSIFRSIEEplrihkiGDKKWRANRVKELL-------DMVEMPASVm 558
Cdd:COG0488 376 ETVK-------IGyFDQHQE--------ELDPDKTVLDELRD-------GAPGGTEQEVRGYLgrflfsgDDAFKPVGV- 432
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 559 grypneLSGGQRQRIAIARAMALDPDVIVCDEAVSALDVlvqdQVLRLLND-LQAEKGlSYLFITHDLAVVRQIADEVVV 637
Cdd:COG0488 433 ------LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI----ETLEALEEaLDDFPG-TVLLVSHDRYFLDRVATRILE 501
|
....*....
gi 2545376782 638 MQHGKLVEH 646
Cdd:COG0488 502 FEDGGVREY 510
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-661 |
1.10e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 115.01 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKST---VANMVLHLLKP--TSGKVFYEGRDTstFKsKDLLGFRRHVQPVFQ--NP 511
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTllrVFNRLIELYPEarVSGEVYLDGQDI--FK-MDVIELRRRVQMVFQipNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 512 YgsldPMYSIFRSIEEPLRIHKI-GDKKWRANRVKELLDMVEMPASVMGRY---PNELSGGQRQRIAIARAMALDPDVIV 587
Cdd:PRK14247 94 I----PNLSIFENVALGLKLNRLvKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 588 CDEAVSALDVLVQDQVLRLLndLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQKQYT 661
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
420-645 |
1.37e-28 |
|
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: 113.47 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprKKemfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTstfksKDLLG 499
Cdd:cd03268 1 LKTNDLTKTYG---KK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-----QKNIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVqpvfqnpyGSL--DPMYSIFRSIEEPLRIHKIGdKKWRANRVKELLDMVEMPASVmGRYPNELSGGQRQRIAIAR 577
Cdd:cd03268 70 ALRRI--------GALieAPGFYPNLTARENLRLLARL-LGIRKKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 578 AMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKLVE 645
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
429-653 |
2.79e-28 |
|
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: 119.80 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 429 FKLPRKKEMfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVF 508
Cdd:TIGR02204 345 FAYPARPDQ-PALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAEL---RARMALVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 509 QNP------------YGSLDpmysifrSIEEPLRIHKigdkkwRANRVKELLDmvEMP---ASVMGRYPNELSGGQRQRI 573
Cdd:TIGR02204 421 QDPvlfaasvmenirYGRPD-------ATDEEVEAAA------RAAHAHEFIS--ALPegyDTYLGERGVTLSGGQRQRI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 574 AIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKglSYLFITHDLAVVrQIADEVVVMQHGKLVEHATTDEVF 653
Cdd:TIGR02204 486 AIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGR--TTLIIAHRLATV-LKADRIVVMDQGRIVAQGTHAELI 562
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
416-652 |
3.67e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.98 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKEFklPRkkemFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTsTFKS- 494
Cdd:COG3845 2 MPPALELRGITKRF--GG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 495 KDLLgfRRHVQPVFQNPygSLDPMYSIFRSI---EEPLRIHKIGDKKWRAnRVKELldmvempasvMGRY-----PN--- 563
Cdd:COG3845 75 RDAI--ALGIGMVHQHF--MLVPNLTVAENIvlgLEPTKGGRLDRKAARA-RIREL----------SERYgldvdPDakv 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 564 -ELSGGQRQRIAIARAMALDPDVIVCDEAVSaldVLVQ---DQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQ 639
Cdd:COG3845 140 eDLSVGEQQRVEILKALYRGARILILDEPTA---VLTPqeaDELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLR 215
|
250
....*....|...
gi 2545376782 640 HGKLVEHATTDEV 652
Cdd:COG3845 216 RGKVVGTVDTAET 228
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
420-654 |
3.98e-28 |
|
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: 120.23 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKLPRKkemfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlg 499
Cdd:TIGR01193 474 IVINDVSYSYGYGSN-----ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL-- 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 fRRHVQPVFQNPYgsldpmysIFR-SIEEPLRI-HKIG---DKKWRANRVKELLDMVE-MPASVMGRYPNE---LSGGQR 570
Cdd:TIGR01193 547 -RQFINYLPQEPY--------IFSgSILENLLLgAKENvsqDEIWAACEIAEIKDDIEnMPLGYQTELSEEgssISGGQK 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 571 QRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQaEKGLsyLFITHDLAVVRQiADEVVVMQHGKLVEHATTD 650
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ-DKTI--IFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHD 693
|
....
gi 2545376782 651 EVFD 654
Cdd:TIGR01193 694 ELLD 697
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
420-644 |
1.71e-27 |
|
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: 111.27 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKLPRKKEMFK---------------AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFY 484
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPGLIgslkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 485 EGRDTSTFKSKdllgFRRHVQPVF---QNPYGSLDPMYSiFRSIEeplRIHKIGDKKWRaNRVKELLDMVEMpASVMGRY 561
Cdd:cd03267 81 AGLVPWKRRKK----FLRRIGVVFgqkTQLWWDLPVIDS-FYLLA---AIYDLPPARFK-KRLDELSELLDL-EELLDTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 562 PNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHG 641
Cdd:cd03267 151 VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
...
gi 2545376782 642 KLV 644
Cdd:cd03267 231 RLL 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
417-641 |
3.65e-27 |
|
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: 110.22 E-value: 3.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 417 EHIITVDHLTKEF--------KLPrkkemfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFY---- 484
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqggkRLP-------VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 485 EGRDTSTFKSKDLLGFRRH----------VQP-VfqnpyGSLDpmysifrSIEEPLRIHKIGDKKWRAnRVKELLDMVEM 553
Cdd:COG4778 75 GWVDLAQASPREILALRRRtigyvsqflrVIPrV-----SALD-------VVAEPLLERGVDREEARA-RARELLARLNL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 554 PASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIAD 633
Cdd:COG4778 142 PERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVAD 220
|
....*...
gi 2545376782 634 EVVVMQHG 641
Cdd:COG4778 221 RVVDVTPF 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
441-641 |
3.74e-27 |
|
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: 110.25 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTstfkskDLLGFRRHVqpVFQNpYgSLDPMYS 520
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI------TEPGPDRMV--VFQN-Y-SLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 521 IFRSIEEPL-RIHKIGDKKWRANRVKELLDMVEMPASVmGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVL- 598
Cdd:TIGR01184 71 VRENIALAVdRVLPDLSKSERRAIVEEHIALVGLTEAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALt 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2545376782 599 ---VQDQVLRLLNdlqaEKGLSYLFITHDLAVVRQIADEVVVMQHG 641
Cdd:TIGR01184 150 rgnLQEELMQIWE----EHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-380 |
5.48e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 110.88 E-value: 5.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 17 GPLLEVKDlaIDFT-TDTGKPvhAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEIAga 95
Cdd:PRK13635 3 EEIIRVEH--ISFRyPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE----AGTITVGGMVLS-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 96 KQSEFDKLRgtKMGLVPQDPmsnlnpvwrigtqvkealkannmdvahekrsalakalagdevevkgndDETFLGAKelpe 175
Cdd:PRK13635 73 EETVWDVRR--QVGMVFQNP------------------------------------------------DNQFVGAT---- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 176 lmteakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagVADDQAWYLAKKYVTGSTMDDRI 255
Cdd:PRK13635 99 ---------------------------------------------------------VQDDVAFGLENIGVPREEMVERV 121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 256 AGLLSEAGLPDAATRArqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFIT 335
Cdd:PRK13635 122 DQALRQVGMEDFLNRE---PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSIT 198
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 336 HDLGLAAeRAQHIVVMYKGQVVESGPSLEVLQHPQH--------PYTKRLVAA 380
Cdd:PRK13635 199 HDLDEAA-QADRVIVMNKGEILEEGTPEEIFKSGHMlqeigldvPFSVKLKEL 250
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
441-643 |
5.79e-27 |
|
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: 107.69 E-value: 5.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFkskDLLGFRRHVQPVFQNpygsldpmys 520
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW---DPNELGDHVGYLPQD---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 521 ifrsieeplrihkigdkkwranrvKELLDmvempASVMGrypNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQ 600
Cdd:cd03246 85 ------------------------DELFS-----GSIAE---NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2545376782 601 DQVLRLLNDLQAeKGLSYLFITHDLAVVRQiADEVVVMQHGKL 643
Cdd:cd03246 133 RALNQAIAALKA-AGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
439-655 |
7.73e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.60 E-value: 7.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRD-TSTFKSKDLLGFRRHVQPVFQNPYGSLdp 517
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKDIKQIRKKVGLVFQFPESQL-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 518 mysifrsIEEPLRI------HKIGDKKWRANRV-KELLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDE 590
Cdd:PRK13649 99 -------FEETVLKdvafgpQNFGVSQEEAEALaREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 591 AVSALDVLVQDQVLRLLNDLQaEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDH 655
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
441-651 |
8.50e-27 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 116.20 E-value: 8.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDtstfkskdllgfRRHVQP-VFQNPYGSLDPMY 519
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIP------------REEIPReVLANSVAMVDQDI 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 SIFR-SIEEPLRI--HKIGDKKW-RANRVKELLDMVempASVMGRYPNEL-------SGGQRQRIAIARAMALDPDVIVC 588
Cdd:TIGR03796 563 FLFEgTVRDNLTLwdPTIPDADLvRACKDAAIHDVI---TSRPGGYDAELaegganlSGGQRQRLEIARALVRNPSILIL 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 589 DEAVSALDVLVQDQVLRLLndlqAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDE 651
Cdd:TIGR03796 640 DEATSALDPETEKIIDDNL----RRRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEE 697
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
439-644 |
1.12e-26 |
|
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: 108.45 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNP---YGSL 515
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRNIGYVPQDVtlfYGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 516 DPMYSIFRSIEEPLRIhkigdkkWRANRVKELLDMV-------EMPASVMGRypnELSGGQRQRIAIARAMALDPDVIVC 588
Cdd:cd03245 95 RDNITLGAPLADDERI-------LRAAELAGVTDFVnkhpnglDLQIGERGR---GLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 589 DEAVSALDVLVQDQVLRLLNDLQAEKGLsyLFITHDLAVVrQIADEVVVMQHGKLV 644
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLLGDKTL--IIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
19-370 |
1.86e-26 |
|
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: 108.05 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFTtDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEEIAGAKQS 98
Cdd:cd03258 1 MIELKNVSKVFG-DTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKST----LIRCINGLERPTSGSVLVDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 99 EFDKLRgTKMGLVPQdpmsNLNPVWRigtqvkealkannmdvahekrsalakalagdevevkgnddETFLGAKELP-ELm 177
Cdd:cd03258 76 ELRKAR-RRIGMIFQ----HFNLLSS----------------------------------------RTVFENVALPlEI- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 178 teakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikAGVADDLIKAgvaddqawylakkyvtgstmddRIAG 257
Cdd:cd03258 110 --------------------------------------------AGVPKAEIEE----------------------RVLE 123
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 LLSEAGLPDaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHD 337
Cdd:cd03258 124 LLELVGLED---KADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHE 200
|
330 340 350
....*....|....*....|....*....|...
gi 2545376782 338 LGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQ 370
Cdd:cd03258 201 MEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-351 |
1.90e-26 |
|
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: 107.56 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIDFTTDtGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGakqse 99
Cdd:cd03293 1 LEVRNVSKTYGGG-GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTS----GEVLVDGEPVTG----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 fdklRGTKMGLVPQDPmsnlnpvwrigtqvkealkannmdvahekrsalakALagdevevkgnddetflgakeLPelmte 179
Cdd:cd03293 71 ----PGPDRGYVFQQD-----------------------------------AL--------------------LP----- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 180 akkalteagvsgeafdkavarftnewvpgsetrWRVADDLIKAGvaddLIKAGVADDQAwylakkyvtgstmDDRIAGLL 259
Cdd:cd03293 87 ---------------------------------WLTVLDNVALG----LELQGVPKAEA-------------RERAEELL 116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 260 SEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLG 339
Cdd:cd03293 117 ELVGLSGFENA---YPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDID 193
|
330
....*....|..
gi 2545376782 340 LAAERAQHIVVM 351
Cdd:cd03293 194 EAVFLADRVVVL 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
21-355 |
2.24e-26 |
|
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: 107.17 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 21 EVKDLAidFTTDTGKPVhAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEIAGAKQSEF 100
Cdd:cd03225 1 ELKNLS--FSYPDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT----SGEVLVDGKDLTKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 101 DKlrgtKMGLVPQDPmsnlnpvwrigtqvkealkannmdvahekrsalakalagdevevkgnddetflgakelpelmtea 180
Cdd:cd03225 74 RR----KVGLVFQNP----------------------------------------------------------------- 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 181 kkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvADDLIKAGVADDQAWYLAKKYVTGSTMDDRIAGLLS 260
Cdd:cd03225 85 --------------------------------------------DDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALE 120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 261 EAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGL 340
Cdd:cd03225 121 LVGLEGLRDR---SPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDL 196
|
330
....*....|....*
gi 2545376782 341 AAERAQHIVVMYKGQ 355
Cdd:cd03225 197 LLELADRVIVLEDGK 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
439-639 |
2.65e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.49 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDllgFRRHVQPVFQNPYGSLDPM 518
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI---YRQQVSYCAQTPTLFGDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 519 YS--IFrsieePLRIHKigdKKWRANRVKELLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALD 596
Cdd:PRK10247 98 YDnlIF-----PWQIRN---QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2545376782 597 VLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQiADEVVVMQ 639
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQ 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
439-638 |
2.71e-26 |
|
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: 113.54 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPYgsldpM 518
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQIAWVPQHPF-----L 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 519 YSifRSIEEPLRIHKIG---DKKWRANRVKELLDMV----EMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEA 591
Cdd:TIGR02857 408 FA--GTIAENIRLARPDasdAEIREALERAGLDEFVaalpQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545376782 592 VSALDVLVQDQVLRLLNDLQaeKGLSYLFITHDLAVVRQiADEVVVM 638
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
39-373 |
3.91e-26 |
|
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: 114.16 E-value: 3.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 39 AVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEIAGAKQSEfdkLRGtKMGLVPQDPmsn 118
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT----SGRILIDGIDLRQIDPAS---LRR-QIGVVLQDV--- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 119 lnpvwRI--GTqVKEalkanNMdvahekrsALAKALAGDEvevkgnddetflgakelpelmtEAKKALTEAGvsgeafdk 196
Cdd:COG2274 559 -----FLfsGT-IRE-----NI--------TLGDPDATDE----------------------EIIEAARLAG-------- 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 197 avarftnewvpgsetrwrvaddlikagvADDLIKAgvaddqawyLAKKYVTgstmddriagLLSEAGLPdaatrarqfph 276
Cdd:COG2274 590 ----------------------------LHDFIEA---------LPMGYDT----------VVGEGGSN----------- 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 eFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLhmLTDSLGTAVLFITHDLGLAAeRAQHIVVMYKGQV 356
Cdd:COG2274 612 -LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL--RRLLKGRTVIIIAHRLSTIR-LADRIIVLDKGRI 687
|
330
....*....|....*..
gi 2545376782 357 VESGPSLEVLQHPQHPY 373
Cdd:COG2274 688 VEDGTHEELLARKGLYA 704
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
419-670 |
3.95e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.04 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFKlprkkeMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDtSTFKSKDLL 498
Cdd:COG4152 1 MLELKGLTKRFG------DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP-LDPEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 GF----RrhvqpvfqnpygSLDP-MysifrSIEEPL----RIHKIGDKKWRAnRVKELLDMVEMPAsvmgrYPN----EL 565
Cdd:COG4152 74 GYlpeeR------------GLYPkM-----KVGEQLvylaRLKGLSKAEAKR-RADEWLERLGLGD-----RANkkveEL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 566 SGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVE 645
Cdd:COG4152 131 SKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVL 209
|
250 260 270
....*....|....*....|....*....|....*.
gi 2545376782 646 HATTDEVfdhpQKQYTR-----------DLLDAIPG 670
Cdd:COG4152 210 SGSVDEI----RRQFGRntlrleadgdaGWLRALPG 241
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
443-643 |
4.77e-26 |
|
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: 106.79 E-value: 4.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPygsldpmySIF 522
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL---HSKVSLVGQEP--------VLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 523 -RSIEEPL-------RIHKIGDKKWRANRVKELLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSA 594
Cdd:cd03248 101 aRSLQDNIayglqscSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2545376782 595 LDVLVQDQVLRLLNDLQAEKglSYLFITHDLAVVRQiADEVVVMQHGKL 643
Cdd:cd03248 181 LDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-369 |
5.49e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 107.10 E-value: 5.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTtdtGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPgtghVVNGSIKLDGEEIAGAKQ 97
Cdd:COG1121 5 PAIELENLTVSYG---GRPV--LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP----PTSGTVRLFGKPPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 98 sefdklrgtKMGLVPQdpmsnlnpvwrigtqvkealkannmdvahekrsalakalagdevevKGNDDETFlgakelPelm 177
Cdd:COG1121 76 ---------RIGYVPQ----------------------------------------------RAEVDWDF------P--- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 178 teakkalteagVSGEAFdkaVA----RFTNEWVPGSETRWRVADDLIKagvaddliKAGVADdqawyLAKKyvtgstmdd 253
Cdd:COG1121 92 -----------ITVRDV---VLmgryGRRGLFRRPSRADREAVDEALE--------RVGLED-----LADR--------- 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 254 RIAGLlseaglpdaatrarqfphefSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLF 333
Cdd:COG1121 136 PIGEL--------------------SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILV 194
|
330 340 350
....*....|....*....|....*....|....*.
gi 2545376782 334 ITHDLGLAAERAQHIVVMyKGQVVESGPSLEVLQHP 369
Cdd:COG1121 195 VTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPE 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
417-657 |
5.89e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 107.04 E-value: 5.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 417 EHIITVDHLTKEFKlprKKemfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFkskd 496
Cdd:COG1137 1 MMTLEAENLVKSYG---KR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 497 llgfrrhvqpvfqnpygsldPMY--------------SIFR--SIEEPLR----IHKIgDKKWRANRVKELLDM--VEMP 554
Cdd:COG1137 71 --------------------PMHkrarlgigylpqeaSIFRklTVEDNILavleLRKL-SKKEREERLEELLEEfgITHL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 555 ASVMGRYpneLSGGQRQRIAIARAMALDPDVIVCDEAVSALD---VL-VQDQVLRLlndlqAEKGLSYLfIT-HDlavVR 629
Cdd:COG1137 130 RKSKAYS---LSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVAdIQKIIRHL-----KERGIGVL-ITdHN---VR 197
|
250 260 270
....*....|....*....|....*....|.
gi 2545376782 630 ---QIADEVVVMQHGKLVEHATTDEVFDHPQ 657
Cdd:COG1137 198 etlGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
440-653 |
6.48e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.01 E-value: 6.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStFKSKDLLGFRRHVQPVFQNPYGSLDPMy 519
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLRESVGMVFQDPDNQLFSA- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 SIFRSIEEPLRIHKIGDKKWRaNRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLV 599
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVR-KRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 600 QDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVF 653
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
442-671 |
7.00e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 107.54 E-value: 7.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 442 DDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLGFRRHVQPVFQNpyGSLDPMYSI 521
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS--GALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 522 FRSIEEPLRIHKIGDKKWRANRVKELLDMVEM--PASVMgryPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLV 599
Cdd:PRK11831 102 FDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLrgAAKLM---PSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 600 QDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQKQyTRDLLDAIPGG 671
Cdd:PRK11831 179 MGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR-VRQFLDGIADG 249
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
432-644 |
1.03e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 112.51 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 432 PRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLGFRR-HVQPVFQN 510
Cdd:PRK10535 15 PSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRReHFGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 511 PYgsLDPMYSIFRSIEEPlRIHKIGDKKWRANRVKELLDMVEMPASVmGRYPNELSGGQRQRIAIARAMALDPDVIVCDE 590
Cdd:PRK10535 95 YH--LLSHLTAAQNVEVP-AVYAGLERKQRLLRAQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 591 AVSALDVLVQDQVLRLLNDLQaEKGLSYLFITHDLAVVRQiADEVVVMQHGKLV 644
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
445-643 |
1.06e-25 |
|
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: 105.33 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 445 SFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTfkskdLLGFRRHVQPVFQ--NPYGSLDPMYSIF 522
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG-----LAPYQRPVSMLFQenNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 523 RSIEEPLRIHKIGDKKwranrvkelldMVEMPASV-----MGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDV 597
Cdd:TIGR01277 93 LGLHPGLKLNAEQQEK-----------VVDAAQQVgiadyLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2545376782 598 LVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKL 643
Cdd:TIGR01277 162 LLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
254-652 |
1.40e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.89 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 254 RIAGLLSEAGL---PDAATrarqfpHEFSGGMRQRALIAIGLACRPDLLIADEPTSALdvTVQ--KRILDHLHMLTDSlG 328
Cdd:COG3845 121 RIRELSERYGLdvdPDAKV------EDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-G 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 329 TAVLFITHDLGLAAERAQHIVVMYKGQVVESGPslevlqhpqhpytkrlvaaaPSLASQRIISAKERGEDADALLDHHIA 408
Cdd:COG3845 192 KSIIFITHKLREVMAIADRVTVLRRGKVVGTVD--------------------TAETSEEELAELMVGREVLLRVEKAPA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 409 --GESTLEksehiitVDHLTkeFKLPRKKEmfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEG 486
Cdd:COG3845 252 epGEVVLE-------VENLS--VRDDRGVP---ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 487 RDTSTFKSKDL--LGFR-----RHVQ------PVFQNpygsldpmySIFRSIEEPlRIHKIGDKKWRA--NRVKELLDM- 550
Cdd:COG3845 320 EDITGLSPRERrrLGVAyipedRLGRglvpdmSVAEN---------LILGRYRRP-PFSRGGFLDRKAirAFAEELIEEf 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 551 ------VEMPASvmgrypnELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHD 624
Cdd:COG3845 390 dvrtpgPDTPAR-------SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISED 461
|
410 420
....*....|....*....|....*...
gi 2545376782 625 LAVVRQIADEVVVMQHGKLVEHATTDEV 652
Cdd:COG3845 462 LDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
420-646 |
1.57e-25 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 104.97 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFklpRKKemfKAVDDVSFSVKRGTTlAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKdllg 499
Cdd:cd03264 1 LQLENLTKRY---GKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNPygSLDPMYSIFRSIEEPLRIHKIGDKKWRAnRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAM 579
Cdd:cd03264 70 LRRRIGYLPQEF--GVYPNFTVREFLDYIAWLKGIPSKEVKA-RVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKglSYLFITHDLAVVRQIADEVVVMQHGKLVEH 646
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-378 |
1.63e-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: 106.57 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDTGkPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAKQ 97
Cdd:cd03294 19 KLLAKGKSKEEILKKTG-QTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTS----GKVLIDGQDIAAMSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 98 SEFDKLRGTKMGLVPQdpmsnlnpvwrigtqvKEALKANnmdvahekRSALAKALAGdeVEVKGnddetflgakelpelm 177
Cdd:cd03294 94 KELRELRRKKISMVFQ----------------SFALLPH--------RTVLENVAFG--LEVQG---------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 178 teakkalteagvsgeafdkavarftnewVPGSETRWRVADDLIKAGVADDlikagvaddqawylakkyvtgstmddriag 257
Cdd:cd03294 132 ----------------------------VPRAEREERAAEALELVGLEGW------------------------------ 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 llseaglpdaatrARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHD 337
Cdd:cd03294 154 -------------EHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHD 220
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2545376782 338 LGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLV 378
Cdd:cd03294 221 LDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-380 |
3.81e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 105.26 E-value: 3.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFTTDTG----KPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAG 94
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS----GELLIDDHPLHF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 95 AKQSefdkLRGTKMGLVPQDPMSNLNPVWRIGTQVKEALKANNMDVAHEKRSALAKALagdevevkgnddetflgakelp 174
Cdd:PRK15112 80 GDYS----YRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETL---------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 175 elmteakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmddR 254
Cdd:PRK15112 134 -------------------------------------------------------------------------------R 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 255 IAGLLseaglPDAATrarQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFI 334
Cdd:PRK15112 135 QVGLL-----PDHAS---YYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYV 206
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2545376782 335 THDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAA 380
Cdd:PRK15112 207 TQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
420-645 |
4.04e-25 |
|
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: 104.15 E-value: 4.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKLPRKKEM----------------FKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVF 483
Cdd:cd03220 1 IELENVSKSYPTYKGGSSslkklgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 484 YEGRDTStfkskdLLGFRrhvqpvfqnpyGSLDPMYSIFRSIEEPLRIHKIgDKKWRANRVKELLDMVEMPASV---MGR 560
Cdd:cd03220 81 VRGRVSS------LLGLG-----------GGFNPELTGRENIYLNGRLLGL-SRKEIDEKIDEIIEFSELGDFIdlpVKT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 561 YpnelSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQaEKGLSYLFITHDLAVVRQIADEVVVMQH 640
Cdd:cd03220 143 Y----SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEK 217
|
....*
gi 2545376782 641 GKLVE 645
Cdd:cd03220 218 GKIRF 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
416-663 |
4.57e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.86 E-value: 4.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKEFKlprKKemfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHL--LKP---TSGKVFYEGRDTS 490
Cdd:PRK14239 2 TEPILQVSDLSVYYN---KK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 491 TFKSkDLLGFRRHVQPVFQ--NPYgsldPMySIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVMGRYPNE---L 565
Cdd:PRK14239 76 SPRT-DTVDLRKEIGMVFQqpNPF----PM-SIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSalgL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 566 SGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQaeKGLSYLFITHDLAVVRQIADEVVVMQHGKLVE 645
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQASRISDRTGFFLDGDLIE 227
|
250
....*....|....*...
gi 2545376782 646 HATTDEVFDHPQKQYTRD 663
Cdd:PRK14239 228 YNDTKQMFMNPKHKETED 245
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
440-660 |
4.89e-25 |
|
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: 104.29 E-value: 4.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDL----LGF----RRhvqpVFqnp 511
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlgIGYvpegRR----IF--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 512 yGSLdpmysifrSIEEPLRI--HKIGDKKWRANRVKELLDM----VEMpasvMGRYPNELSGGQRQRIAIARAMALDPDV 585
Cdd:COG0410 91 -PSL--------TVEENLLLgaYARRDRAEVRADLERVYELfprlKER----RRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 586 IVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHP--QKQY 660
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPevREAY 233
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
420-656 |
6.04e-25 |
|
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: 103.78 E-value: 6.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprKKemfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFkskdllg 499
Cdd:cd03218 1 LRAENLSKRYG---KR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 frrhvqpvfqnpygsldPMY--------------SIFR--SIEEPLR----IHKIgDKKWRANRVKELLDMVEMpASVMG 559
Cdd:cd03218 68 -----------------PMHkrarlgigylpqeaSIFRklTVEENILavleIRGL-SKKEREEKLEELLEEFHI-THLRK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 560 RYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALD-VLVQDqVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVM 638
Cdd:cd03218 129 SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpIAVQD-IQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYII 206
|
250
....*....|....*...
gi 2545376782 639 QHGKLVEHATTDEVFDHP 656
Cdd:cd03218 207 YEGKVLAEGTPEEIAANE 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
419-653 |
6.87e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.79 E-value: 6.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTkeFKLPRKKEMfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRdtsTFKSKDLL 498
Cdd:PRK13642 4 ILEVENLV--FKYEKESDV-NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 GFRRHVQPVFQNPYGSLdpmysIFRSIEEPLRI---HKIGDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAI 575
Cdd:PRK13642 78 NLRRKIGMVFQNPDNQF-----VGATVEDDVAFgmeNQGIPREEMIKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 576 ARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDEVF 653
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
440-656 |
2.13e-24 |
|
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: 101.80 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPY---GSLd 516
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---RSRISIIPQDPVlfsGTI- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 517 pmysifRSIEEPLRIHkiGDKK-WRA-------NRVKELLDMVEMPASVMGrypNELSGGQRQRIAIARAMALDPDVIVC 588
Cdd:cd03244 95 ------RSNLDPFGEY--SDEElWQAlervglkEFVESLPGGLDTVVEEGG---ENLSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 589 DEAVSALDV----LVQdQVLRllndlQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEhattdevFDHP 656
Cdd:cd03244 164 DEATASVDPetdaLIQ-KTIR-----EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVE-------FDSP 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-362 |
2.17e-24 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 102.13 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 12 MQKEHGPLLEVKDLAIDFTTDTGkPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEE 91
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTGAG-ELTILKGISLEVEAGESVAIVGASGSGKST----LLGLLAGLDRPTSGTVRLAGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 92 IAGAKQSEFDKLRGTKMGLVPQD--PMSNLNpvwrigtqvkeALKaNNMdvahekrsalakalagdevevkgnddetflg 169
Cdd:COG4181 76 LFALDEDARARLRARHVGFVFQSfqLLPTLT-----------ALE-NVM------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 170 akeLPelmteakkaLTEAGVsGEAFDKAVArftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgs 249
Cdd:COG4181 113 ---LP---------LELAGR-RDARARARA-------------------------------------------------- 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 250 tmddriagLLSEAGLpdaATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGT 329
Cdd:COG4181 130 --------LLERVGL---GHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGT 198
|
330 340 350
....*....|....*....|....*....|...
gi 2545376782 330 AVLFITHDLGLAAeRAQHIVVMYKGQVVESGPS 362
Cdd:COG4181 199 TLVLVTHDPALAA-RCDRVLRLRAGRLVEDTAA 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
439-653 |
2.23e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 103.66 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKV-FYEGRDTSTFKSKDLLGFRRHVQPVFQNPYGSLDP 517
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 518 MySIFRSIeePLRIHKIGDKKWRANRVK-ELLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALD 596
Cdd:PRK13643 100 E-TVLKDV--AFGPQNFGIPKEKAEKIAaEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 597 VLVQDQVLRLLNDLQaEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVF 653
Cdd:PRK13643 177 PKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
420-668 |
3.65e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.08 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFklpRKKemfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSK---- 495
Cdd:COG4604 2 IEIKNVSKRY---GGK---VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRelak 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 496 ------------------DLLGFRRHvqpvfqnPY--GSL---DpmysiFRSIEEPLrihkigdkkwranrvkELLDMVE 552
Cdd:COG4604 76 rlailrqenhinsrltvrELVAFGRF-------PYskGRLtaeD-----REIIDEAI----------------AYLDLED 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 553 MpasvMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIA 632
Cdd:COG4604 128 L----ADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYA 203
|
250 260 270
....*....|....*....|....*....|....*.
gi 2545376782 633 DEVVVMQHGKLVEHATTDEVFdhpqkqyTRDLLDAI 668
Cdd:COG4604 204 DHIVAMKDGRVVAQGTPEEII-------TPEVLSDI 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
440-650 |
4.37e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.09 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTfkskdlLGFRRHVqpVFQNPygSLDPMY 519
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG------PGAERGV--VFQNE--GLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 SIFRSIEEPLRIHKIGdKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLV 599
Cdd:PRK11248 86 NVQDNVAFGLQLAGVE-KMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 600 QDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQ--HGKLVEHATTD 650
Cdd:PRK11248 164 REQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVERLPLN 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
420-644 |
4.60e-24 |
|
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: 100.43 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlpRKKemfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTsTFKSKDLLG 499
Cdd:cd03269 1 LEVENVTKRFG--RVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 F---------RRHVQPVFqNPYGSLDPM--YSIFRSIEEPLRIHKIGDKKWRanRVKelldmvempasvmgrypnELSGG 568
Cdd:cd03269 74 YlpeerglypKMKVIDQL-VYLAQLKGLkkEEARRRIDEWLERLELSEYANK--RVE------------------ELSKG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 569 QRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:cd03269 133 NQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-368 |
5.21e-24 |
|
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: 106.77 E-value: 5.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 17 GPLLEVKDLaiDFTTDTGKPvhAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAK 96
Cdd:COG4988 334 PPSIELEDV--SFSYPGGRP--ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS----GSILINGVDLSDLD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 97 QSEfdkLRGtKMGLVPQdpmsnlNPVWRIGTqVKEALkannmdvahekrsALAKALAGDEvevkgnddetflgakelpel 176
Cdd:COG4988 406 PAS---WRR-QIAWVPQ------NPYLFAGT-IRENL-------------RLGRPDASDE-------------------- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 177 mtEAKKALTEAGvsgeafdkavarftnewvpgsetrwrvaddlikagvADDLIKAgvaddqawylakkyvtgstMDDRIA 256
Cdd:COG4988 442 --ELEAALEAAG------------------------------------LDEFVAA-------------------LPDGLD 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 257 GLLSEAGLPdaatrarqfpheFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLtdSLGTAVLFITH 336
Cdd:COG4988 465 TPLGEGGRG------------LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITH 530
|
330 340 350
....*....|....*....|....*....|..
gi 2545376782 337 DLGLAAeRAQHIVVMYKGQVVESGPSLEVLQH 368
Cdd:COG4988 531 RLALLA-QADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
438-656 |
5.22e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 104.15 E-value: 5.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 438 FKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDllgfrRHVQPVFQNpYgSLDP 517
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----RDIAMVFQN-Y-ALYP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 518 MYSIFRSIEEPLRIHKIGdKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALD- 596
Cdd:PRK11650 90 HMSVRENMAYGLKIRGMP-KAEIEERVAEAARILEL-EPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDa 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 597 -VLVQdqvLRL-LNDLQAEKGLSYLFITHDlavvrQI-----ADEVVVMQHGKLVEHATTDEVFDHP 656
Cdd:PRK11650 168 kLRVQ---MRLeIQRLHRRLKTTSLYVTHD-----QVeamtlADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
417-644 |
6.09e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.12 E-value: 6.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 417 EHIITVDHLTKefklpRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTvanMVLHL---LKPTSGKVFYEGRDTSTFK 493
Cdd:PRK13647 2 DNIIEVEDLHF-----RYKDGTKALKGLSLSIPEGSKTALLGPNGAGKST---LLLHLngiYLPQRGRVKVMGREVNAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 494 SKDLlgfRRHVQPVFQnpygslDPMYSIFRS-IEEPLRIHKIG---DKKWRANRVKELLDMVEMPAsVMGRYPNELSGGQ 569
Cdd:PRK13647 74 EKWV---RSKVGLVFQ------DPDDQVFSStVWDDVAFGPVNmglDKDEVERRVEEALKAVRMWD-FRDKPPYHLSYGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 570 RQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
252-380 |
1.05e-23 |
|
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: 100.45 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 252 DDRIAGLLSEAGLPDAATRARqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAV 331
Cdd:cd03295 111 RERADELLALVGLDPAEFADR-YPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTI 189
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2545376782 332 LFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAA 380
Cdd:cd03295 190 VFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
441-661 |
1.35e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 100.69 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLK-----PTSGKVFYEGRDTSTFKSkDLLGFRRHVQPVFQ--NPYg 513
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDV-DPIEVRREVGMVFQypNPF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 514 sldPMYSIFRSIEEPLRIHK-IGDKKWRANRVKELLDMVEMPASVMGR---YPNELSGGQRQRIAIARAMALDPDVIVCD 589
Cdd:PRK14267 98 ---PHLTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 590 EAVSALDVLVQDQVLRLLNDLQAEkgLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQKQYT 661
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
439-644 |
1.73e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 99.18 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLGFRRHVQPVFQNPYGSLDpm 518
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 519 YSIFRSIEEPLRIHKIGDKKWRaNRVKELLDMVEMPASVMGrYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVL 598
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIR-RRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2545376782 599 VQDQVLRLLNDLQaEKGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:PRK10908 172 LSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-643 |
3.15e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.86 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTdtgkpVHAVRDANFTVYPGQWVAIVGESGSGKSTsAMAVL-GLLP-GTghvVNGSIKLDGEEI--A 93
Cdd:PRK13549 4 YLLEMKNITKTFGG-----VKALDNVSLKVRAGEIVSLCGENGAGKST-LMKVLsGVYPhGT---YEGEIIFEGEELqaS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 94 GAKQSEfdklrgtKMGLVpqdpmsnlnpvwrIGTQ----VKEALKANNMdvahekrsalakalagdevevkgnddetFLG 169
Cdd:PRK13549 75 NIRDTE-------RAGIA-------------IIHQelalVKELSVLENI----------------------------FLG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 170 akelpelmteakkalteagvsgeafdkavarftNEWVPGsetrwrvaddlikagvaddlikaGVADDQAWYLakkyvtgs 249
Cdd:PRK13549 107 ---------------------------------NEITPG-----------------------GIMDYDAMYL-------- 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 250 tmddRIAGLLSEAGLP-DAATRARqfphEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlG 328
Cdd:PRK13549 123 ----RAQKLLAQLKLDiNPATPVG----NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-G 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 329 TAVLFITHDLGLAAERAQHIVVMYKGQVVESGPslevlqhpqhpytkrlvaaAPSLASQRIIsAKERGEDADALLDH--H 406
Cdd:PRK13549 194 IACIYISHKLNEVKAISDTICVIRDGRHIGTRP-------------------AAGMTEDDII-TMMVGRELTALYPRepH 253
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 407 IAGESTLEkSEHIiTVDHLTKefklPRKKEmfkaVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLK-PTSGKVFYE 485
Cdd:PRK13549 254 TIGEVILE-VRNL-TAWDPVN----PHIKR----VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFID 323
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 486 GRDTSTFKSKDLLGF---------RRH----VQPVFQNPYGSLDPMYSIFRSIEEPLRIHKIGDKKWRAnRVKElldmve 552
Cdd:PRK13549 324 GKPVKIRNPQQAIAQgiamvpedrKRDgivpVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRL-KVKT------ 396
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 553 mpASVMGRYPNeLSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIA 632
Cdd:PRK13549 397 --ASPELAIAR-LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLS 472
|
650
....*....|.
gi 2545376782 633 DEVVVMQHGKL 643
Cdd:PRK13549 473 DRVLVMHEGKL 483
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
17-379 |
3.82e-23 |
|
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: 104.08 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 17 GPLLEVKDLAidFTTDtGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPgtghVVNGSIKLDGEEIAGAK 96
Cdd:COG4987 331 GPSLELEDVS--FRYP-GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD----PQSGSITLGGVDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 97 QSEfdkLRGTkMGLVPQDP-------MSNLnpvwrigtqvkealkannmdvahekrsALAKALAGDEvevkgnddetflg 169
Cdd:COG4987 404 EDD---LRRR-IAVVPQRPhlfdttlRENL---------------------------RLARPDATDE------------- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 170 akelpelmtEAKKALTEAGVsgeafdkavarftnewvpgsetrwrvaddlikagvaDDLIKAgvaddqawylakkyvtgs 249
Cdd:COG4987 440 ---------ELWAALERVGL------------------------------------GDWLAA------------------ 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 250 tMDDRIAGLLSEAGLPdaatrarqfpheFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDslGT 329
Cdd:COG4987 457 -LPDGLDTWLGEGGRR------------LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GR 521
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2545376782 330 AVLFITHDLgLAAERAQHIVVMYKGQVVESGPSLEVLQhpQHPYTKRLVA 379
Cdd:COG4987 522 TVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLA--QNGRYRQLYQ 568
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
420-645 |
4.26e-23 |
|
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: 96.61 E-value: 4.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTkeFKLPRKKEmfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKskDLLg 499
Cdd:cd03247 1 LSINNVS--FSYPEQEQ--QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE--KAL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 fRRHVQPVFQNPYgsldpmysIFrsieeplrihkigDKKWRANrvkelldmvempasvMGRypnELSGGQRQRIAIARAM 579
Cdd:cd03247 74 -SSLISVLNQRPY--------LF-------------DTTLRNN---------------LGR---RFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLndLQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVE 645
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIM 176
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
276-360 |
4.48e-23 |
|
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: 96.74 E-value: 4.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 276 HEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQ 355
Cdd:cd03214 96 NELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
....*
gi 2545376782 356 VVESG 360
Cdd:cd03214 176 IVAQG 180
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-376 |
4.48e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 98.53 E-value: 4.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFttdtGKpVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIaGAKQS 98
Cdd:COG1126 1 MIEIENLHKSF----GD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDS----GTITVDGEDL-TDSKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 99 EFDKLRgTKMGLVPQDPmsNLNPvwrigtqvkealkannmdvaHekRSAL---AKALagdeVEVKGnddetflgakelpe 175
Cdd:COG1126 71 DINKLR-RKVGMVFQQF--NLFP--------------------H--LTVLenvTLAP----IKVKK-------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 176 lMTEAkkalteagvsgEAFDKAVArftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmddri 255
Cdd:COG1126 108 -MSKA-----------EAEERAME-------------------------------------------------------- 119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 256 agLLSEAGLPDaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFIT 335
Cdd:COG1126 120 --LLERVGLAD---KADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVT 193
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2545376782 336 HDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKR 376
Cdd:COG1126 194 HEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
439-643 |
6.13e-23 |
|
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: 96.35 E-value: 6.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfkskdllgfrrhvqpvfqnpygsldpm 518
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT---------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 519 ysiFRSIEEPLRiHKIG----DkkwranRVKELLdMVEMPAS---VMGRYpneLSGGQRQRIAIARAMALDPDVIVCDEA 591
Cdd:cd03215 66 ---RRSPRDAIR-AGIAyvpeD------RKREGL-VLDLSVAeniALSSL---LSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 592 VSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKL 643
Cdd:cd03215 132 TRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
441-670 |
6.65e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 99.01 E-value: 6.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSG-----KVFYEGRdtSTFKSKDLLGFRRHVQPVFQ--NPYg 513
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGR--SIFNYRDVLEFRRRVGMLFQrpNPF- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 514 sldPMySIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVMGRY---PNELSGGQRQRIAIARAMALDPDVIVCDE 590
Cdd:PRK14271 114 ---PM-SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 591 AVSALDVLVQDQVLRLLNDLqAEKgLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQKQYTRDLLDAIPG 670
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSL-ADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSG 267
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
418-624 |
6.73e-23 |
|
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: 97.16 E-value: 6.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 418 HIITVDHLTKEFklpRKKEMFkavDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDtstfKSKDL 497
Cdd:COG4133 1 MMLEAENLSCRR---GERLLF---SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP----IRDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 498 LGFRRHVQPVFQNP--YGSLdpmysifrSIEEPLRIH-KIGDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIA 574
Cdd:COG4133 71 EDYRRRLAYLGHADglKPEL--------TVRENLRFWaALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2545376782 575 IARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDlQAEKGLSYLFITHD 624
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
254-401 |
8.36e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 100.26 E-value: 8.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 254 RIAGLLSEAGLPDaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLF 333
Cdd:PRK11153 120 RVTELLELVGLSD---KADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 334 ITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLV----------------AAAPSLASQRIISAKERGE 397
Cdd:PRK11153 197 ITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIqstlhldlpedylarlQAEPTTGSGPLLRLEFTGE 276
|
....
gi 2545376782 398 DADA 401
Cdd:PRK11153 277 SVDA 280
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
441-652 |
9.73e-23 |
|
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: 103.28 E-value: 9.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFkskDLLGFRRHVQPVFQNPYgsldpMYS 520
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIA---DPAWLRRQMGVVLQENV-----LFS 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 521 ifRSIEEPLRIHKIG---DKKWRANRVKELLDMV-EMPA---SVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVS 593
Cdd:TIGR01846 545 --RSIRDNIALCNPGapfEHVIHAAKLAGAHDFIsELPQgynTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATS 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 594 ALDVLVQDQVLRLLNDLQaeKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDEV 652
Cdd:TIGR01846 623 ALDYESEALIMRNMREIC--RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEEL 678
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
441-653 |
9.95e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.16 E-value: 9.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDL---LGFRRHVQPVfqnPYG-SLD 516
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLarrLALLPQHHLT---PEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 517 PMYSIFRSIEEPL------RIHKIGDKKWRANRVKELLDmvempasvmgRYPNELSGGQRQRIAIARAMALDPDVIVCDE 590
Cdd:PRK11231 95 ELVAYGRSPWLSLwgrlsaEDNARVNQAMEQTRINHLAD----------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 591 AVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVF 653
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-663 |
9.98e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.19 E-value: 9.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANmVLHLLKPTSGKVFYEGR----DTSTFKSK-DLLGFRRHVQPVFQNPyg 513
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGRveffNQNIYERRvNLNRLRRQVSMVHPKP-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 514 SLDPMySIFRSIEEPLRIhkIGdkkWRANRvkELLDMVEMP---ASVMGRYPN-------ELSGGQRQRIAIARAMALDP 583
Cdd:PRK14258 98 NLFPM-SVYDNVAYGVKI--VG---WRPKL--EIDDIVESAlkdADLWDEIKHkihksalDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 584 DVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQH-----GKLVEHATTDEVFDHPQK 658
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHD 249
|
....*
gi 2545376782 659 QYTRD 663
Cdd:PRK14258 250 SRTRE 254
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
40-306 |
1.05e-22 |
|
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: 94.64 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 40 VRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEIagakQSEFDKLRGTKMGLVPQDPmsNL 119
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT----EGTILLDGQDL----TDDERKSLRKEIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 120 NPVWRIGTQVKEALkannmdvahekrsalakalagdevevkgnddetflgakELPELMTEAkkalteagvsgeafdkava 199
Cdd:pfam00005 71 FPRLTVRENLRLGL--------------------------------------LLKGLSKRE------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 200 rftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstMDDRIAGLLSEAGLPD-AATRARQFPHEF 278
Cdd:pfam00005 94 ---------------------------------------------------KDARAEEALEKLGLGDlADRPVGERPGTL 122
|
250 260
....*....|....*....|....*...
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTS 306
Cdd:pfam00005 123 SGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-368 |
1.10e-22 |
|
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: 98.27 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAidFT-TDTGKPvhAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLL-PGTGHV-VNGSIKLDGEEIagak 96
Cdd:TIGR04520 1 IEVENVS--FSyPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlPTSGKVtVDGLDTLDEENL---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 97 qsefDKLRgTKMGLVPQDPMSNLnpvwrIGTQVKEalkannmDVAhekrsalakalagdevevkgnddetFlGakelPEl 176
Cdd:TIGR04520 73 ----WEIR-KKVGMVFQNPDNQF-----VGATVED-------DVA-------------------------F-G----LE- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 177 mteakkalteagvsgeafdkavarftNEWVPGSEtrwrvaddlikagvaddlikagvaddqawylakkyvtgstMDDRIA 256
Cdd:TIGR04520 105 --------------------------NLGVPREE----------------------------------------MRKRVD 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 257 GLLSEAGLPDAATRArqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITH 336
Cdd:TIGR04520 119 EALKLVGMEDFRDRE---PHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITH 195
|
330 340 350
....*....|....*....|....*....|..
gi 2545376782 337 DLGLAAErAQHIVVMYKGQVVESGPSLEVLQH 368
Cdd:TIGR04520 196 DMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
441-653 |
1.38e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.53 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTvanmvlhLLK-------PTSGKVFYEGRDTSTFKSKDLLGfRRHVQPvfQNPyg 513
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKST-------LLRalsgelsPDSGEVRLNGRPLADWSPAELAR-RRAVLP--QHS-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 514 sldpmysifrSIEEPLRIHKI---GDKKWRANRVKElldmVEMPASVM---------GRYPNELSGGQRQRIAIARAMA- 580
Cdd:PRK13548 86 ----------SLSFPFTVEEVvamGRAPHGLSRAED----DALVAAALaqvdlahlaGRDYPQLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 581 -----LDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVF 653
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
445-651 |
1.64e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.57 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 445 SFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRD-TSTFKSkdllgfRRHVQPVFQNpyGSLDPMYSIFR 523
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhTTTPPS------RRPVSMLFQE--NNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 524 SIEepLRIHKiGDKKWRANRVKelldmVEMPASVMG------RYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDV 597
Cdd:PRK10771 91 NIG--LGLNP-GLKLNAAQREK-----LHAIARQMGiedllaRLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 598 LVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDE 651
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
441-626 |
2.64e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 95.63 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKP---TSGKVFYEGRDTSTFKSKdllgfRRHVQPVFQNPYgsLDP 517
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE-----QRRIGILFQDDL--LFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 518 MYSIFRSIEEPLRiHKIGdKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDV 597
Cdd:COG4136 90 HLSVGENLAFALP-PTIG-RAQRRARVEQALEEAGL-AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
170 180
....*....|....*....|....*....
gi 2545376782 598 LVQDQVLRLLNDLQAEKGLSYLFITHDLA 626
Cdd:COG4136 167 ALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
283-652 |
2.83e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 100.90 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 283 RQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDsLGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPS 362
Cdd:PRK15439 146 RQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKT 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 363 LEvlqhpqhpytkrlvaaapsLASQRIISAKERGEDADALLDhhiAGESTLEKSEH---------IITVDHLTKE-FKlp 432
Cdd:PRK15439 225 AD-------------------LSTDDIIQAITPAAREKSLSA---SQKLWLELPGNrrqqaagapVLTVEDLTGEgFR-- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 433 rkkemfkavdDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLL--GF-----RRHVQ 505
Cdd:PRK15439 281 ----------NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLarGLvylpeDRQSS 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 506 ------PVFQNPYGSLDPMYSIFrsiEEPLRIHKIGDKKWRANRVKelLDMVEMPASVmgrypneLSGGQRQRIAIARAM 579
Cdd:PRK15439 351 glyldaPLAWNVCALTHNRRGFW---IKPARENAVLERYRRALNIK--FNHAEQAART-------LSGGNQQKVLIAKCL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEV 652
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
438-663 |
3.30e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.77 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 438 FKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMV--LHLLKPT---SGKVFYEGRDTSTfKSKDLLGFRRHVQPVFQNPY 512
Cdd:PRK14243 23 FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 513 gsldPM-YSIFRSIEEPLRIHKI-GDKKW---RANRVKELLDMVEMPASVMGRypnELSGGQRQRIAIARAMALDPDVIV 587
Cdd:PRK14243 102 ----PFpKSIYDNIAYGARINGYkGDMDElveRSLRQAALWDEVKDKLKQSGL---SLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 588 CDEAVSALDVLVQDQVLRLLNDLQAEkgLSYLFITHDLAVVRQIADEVVVM---------QHGKLVEHATTDEVFDHPQK 658
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQ 252
|
....*
gi 2545376782 659 QYTRD 663
Cdd:PRK14243 253 QATRD 257
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
441-655 |
3.32e-22 |
|
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: 100.89 E-value: 3.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDtstFKSKDLLGFRRHV----QPVFQNPyGSLD 516
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGAD---LKQWDRETFGKHIgylpQDVELFP-GTVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 517 PMYSIFRSIEEPLRIHKIGdkkwRANRVKELLDMVEMP-ASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSAL 595
Cdd:TIGR01842 410 ENIARFGENADPEKIIEAA----KLAGVHELILRLPDGyDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 596 DVLVQDQVLRLLNDLQAeKGLSYLFITHDLAVVrQIADEVVVMQHGKLVEHATTDEVFDH 655
Cdd:TIGR01842 486 DEEGEQALANAIKALKA-RGITVVVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
442-651 |
4.25e-22 |
|
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: 101.05 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 442 DDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNP---------- 511
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RAAIGIVPQDTvlfndtiayn 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 512 --YGSLDPmysifrSIEEplrihkIgdkkWRANRVKELLDMVE-MP---ASVMGrypnE----LSGGQRQRIAIARAMAL 581
Cdd:COG5265 452 iaYGRPDA------SEEE------V----EAAARAAQIHDFIEsLPdgyDTRVG----ErglkLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 582 DPDVIVCDEAVSALDVLVQDQVLRLLNdlQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDE 651
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALR--EVARGRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAE 578
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
34-361 |
4.29e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 95.12 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 34 GKPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEEIAGAKQSEFDKLRgTKMGLVPQ 113
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR-RRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 114 DpmsnlnpvWRIgtqvkealkannmdvahekrsalakalagdevevkgnddetflgakeLPelmteakkalteagvsgea 193
Cdd:COG2884 87 D--------FRL-----------------------------------------------LP------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 194 fDKAVarFTNewvpgsetrwrVADDLIKAGVADDLIKAgvaddqawylakkyvtgstmddRIAGLLSEAGLPDaatRARQ 273
Cdd:COG2884 93 -DRTV--YEN-----------VALPLRVTGKSRKEIRR----------------------RVREVLDLVGLSD---KAKA 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 274 FPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDsLGTAVLFITHDLGLAAERAQHIVVMYK 353
Cdd:COG2884 134 LPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELED 212
|
....*...
gi 2545376782 354 GQVVESGP 361
Cdd:COG2884 213 GRLVRDEA 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
400-653 |
5.60e-22 |
|
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: 100.21 E-value: 5.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 400 DALLDHHIAGESTLE--KSEHIITVDHLTkeFKLPRKKEMfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKP 477
Cdd:COG4618 309 NELLAAVPAEPERMPlpRPKGRLSVENLT--VVPPGSKRP--ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 478 TSGKVFYEGRDTSTFkSKDLLGfrRHV----QPV--F-----QN--PYGSLDPmysifRSIEEPLR---IHkigdkkwra 541
Cdd:COG4618 385 TAGSVRLDGADLSQW-DREELG--RHIgylpQDVelFdgtiaENiaRFGDADP-----EKVVAAAKlagVH--------- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 542 nrvkellDMV-EMP---ASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGlS 617
Cdd:COG4618 448 -------EMIlRLPdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGA-T 519
|
250 260 270
....*....|....*....|....*....|....*.
gi 2545376782 618 YLFITHDLAVVrQIADEVVVMQHGKLVEHATTDEVF 653
Cdd:COG4618 520 VVVITHRPSLL-AAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-380 |
8.79e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.52 E-value: 8.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDTGKPVHA----VRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIA 93
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLSGKHQhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQ----GNVSWRGEPLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 94 GAKQSEFDKLRGTkMGLVPQDPMSNLNPVWRIGTQVKEALKannmdvaHekrsalakalagdevevkgnddetflgakel 173
Cdd:PRK10419 78 KLNRAQRKAFRRD-IQMVFQDSISAVNPRKTVREIIREPLR-------H------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 174 pelMTEAKKALTEAgvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmdd 253
Cdd:PRK10419 119 ---LLSLDKAERLA------------------------------------------------------------------ 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 254 RIAGLLSEAGLPDAAtrARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLF 333
Cdd:PRK10419 130 RASEMLRAVDLDDSV--LDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLF 207
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2545376782 334 ITHDLGLAAERAQHIVVMYKGQVVESGPSLEvLQHPQHPYTKRLVAA 380
Cdd:PRK10419 208 ITHDLRLVERFCQRVMVMDNGQIVETQPVGD-KLTFSSPAGRVLQNA 253
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-360 |
1.19e-21 |
|
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: 93.75 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 21 EVKDLAIDFTtdtGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEIAgakqsef 100
Cdd:cd03235 1 EVEDLTVSYG---GHPV--LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT----SGSIRVFGKPLE------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 101 dkLRGTKMGLVPQdpmsnlnpvwrigtqvkealkannmdvaheKRSAlakalagdevevkgndDETFlgakelPelmtea 180
Cdd:cd03235 65 --KERKRIGYVPQ------------------------------RRSI----------------DRDF------P------ 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 181 kkalteagVSGEAFdkaVA----RFTNEWVPGSETRWRVADDLIKAGVADDLIkagvaddqawylakkyvtgstmDDRIA 256
Cdd:cd03235 85 --------ISVRDV---VLmglyGHKGLFRRLSKADKAKVDEALERVGLSELA----------------------DRQIG 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 257 gllseaglpdaatrarqfphEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDsLGTAVLFITH 336
Cdd:cd03235 132 --------------------ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTH 190
|
330 340
....*....|....*....|....
gi 2545376782 337 DLGLAAERAQHIVVMyKGQVVESG 360
Cdd:cd03235 191 DLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
436-648 |
1.35e-21 |
|
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: 93.25 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 436 EMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPY--- 512
Cdd:cd03369 19 DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL---RSSLTIIPQDPTlfs 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 513 ----GSLDP--MYSIfRSIEEPLRIHKIGdkkwranrvkelldmvempasvmgrypNELSGGQRQRIAIARAMALDPDVI 586
Cdd:cd03369 96 gtirSNLDPfdEYSD-EEIYGALRVSEGG---------------------------LNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 587 VCDEAVSALDV----LVQDQVLRLLNDlqaekgLSYLFITHDLavvRQIA--DEVVVMQHGKLVEHAT 648
Cdd:cd03369 148 VLDEATASIDYatdaLIQKTIREEFTN------STILTIAHRL---RTIIdyDKILVMDAGEVKEYDH 206
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
253-378 |
1.42e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 96.75 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 DRIAGLLSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQK---RILDHLHmltDSLGT 329
Cdd:COG1118 112 ARVEELLELVQLEGLADR---YPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKelrRWLRRLH---DELGG 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2545376782 330 AVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLV 378
Cdd:COG1118 186 TTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
17-378 |
2.08e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 96.32 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 17 GPLLEVKDLAIDFTTdtgkpVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAG-- 94
Cdd:COG3842 3 MPALELENVSKRYGD-----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDS----GRILLDGRDVTGlp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 95 AKQsefdklRGtkMGLVPQDPmsnlnpvwrigtqvkeALKANnmdvahekrsalakalagdevevkgnddetflgakelp 174
Cdd:COG3842 74 PEK------RN--VGMVFQDY----------------ALFPH-------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 175 elMTeakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagVADDQAWYLAKKYVTGSTMDDR 254
Cdd:COG3842 92 --LT------------------------------------------------------VAENVAFGLRMRGVPKAEIRAR 115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 255 IAGLLSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFI 334
Cdd:COG3842 116 VAELLELVGLEGLADR---YPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYV 192
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2545376782 335 THDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLV 378
Cdd:COG3842 193 THDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFI 236
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
254-356 |
2.81e-21 |
|
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: 91.31 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 254 RIAGLLSEAGLPDAATrARQFpHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLF 333
Cdd:cd03230 74 RIGYLPEEPSLYENLT-VREN-LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILL 150
|
90 100
....*....|....*....|...
gi 2545376782 334 ITHDLGLAAERAQHIVVMYKGQV 356
Cdd:cd03230 151 SSHILEEAERLCDRVAILNNGRI 173
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
233-412 |
5.05e-21 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 95.10 E-value: 5.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 233 VADDQAWYLAKKYVTGSTMDDRIAGLLSEAGLPDAAtraRQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTV 312
Cdd:TIGR03265 93 VADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSE---RKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 313 QKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSLASQRIISA 392
Cdd:TIGR03265 170 REHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPGTRGGGS 249
|
170 180
....*....|....*....|
gi 2545376782 393 KERGEDADALLDHHIAGEST 412
Cdd:TIGR03265 250 RARVGGLTLACAPGLAQPGA 269
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
254-623 |
5.20e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 98.27 E-value: 5.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 254 RIAGLLSEAGLPDAATR-ARQFphefSGGMRQRaliaIGLACR----PDLLIADEPTSALDVTVQKRILDhlhmLTDSL- 327
Cdd:NF033858 116 RIDELLRATGLAPFADRpAGKL----SGGMKQK----LGLCCAlihdPDLLILDEPTTGVDPLSRRQFWE----LIDRIr 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 328 ----GTAVLFIThdlglA----AERAQHIVVMYKGQVVESGPSLEVLQHpqhpytkrlvAAAPSLasqriisakergEDA 399
Cdd:NF033858 184 aerpGMSVLVAT-----AymeeAERFDWLVAMDAGRVLATGTPAELLAR----------TGADTL------------EAA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 400 -DALL------DHH---IAGESTLEKSEHIITVDHLTKEFKlprkkeMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVAN 469
Cdd:NF033858 237 fIALLpeekrrGHQpvvIPPRPADDDDEPAIEARGLTMRFG------DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 470 MVLHLLKPTSGKVFYEGR-----DTSTfkskdllgfRRHVQPVFQ--NPYGSLdpmysifrSIEEPLRIH----KIGDKK 538
Cdd:NF033858 311 MLTGLLPASEGEAWLFGQpvdagDIAT---------RRRVGYMSQafSLYGEL--------TVRQNLELHarlfHLPAAE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 539 WRAnRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSy 618
Cdd:NF033858 374 IAA-RVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT- 450
|
....*.
gi 2545376782 619 LFI-TH 623
Cdd:NF033858 451 IFIsTH 456
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
20-365 |
7.11e-21 |
|
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: 92.25 E-value: 7.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIDFTTDTgkpvHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEIAGAKQSE 99
Cdd:cd03256 1 IEVENLSKTYPNGK----KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT----SGSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 FDKLRGtKMGLVPQDPmsNLnpvwrIGTQvkealkannmdvahekrSALAKALAGdevevkgnddetFLGAKELpelmte 179
Cdd:cd03256 73 LRQLRR-QIGMIFQQF--NL-----IERL-----------------SVLENVLSG------------RLGRRST------ 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 180 akkalteagvsgeafdkavarftnewvpgsetrWRVADDLikagvaddlikagvaddqaWYLAKKYvtgstmddRIAGLL 259
Cdd:cd03256 110 ---------------------------------WRSLFGL-------------------FPKEEKQ--------RALAAL 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 260 SEAGLPD-AATRARQFphefSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDL 338
Cdd:cd03256 130 ERVGLLDkAYQRADQL----SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQV 205
|
330 340
....*....|....*....|....*..
gi 2545376782 339 GLAAERAQHIVVMYKGQVVESGPSLEV 365
Cdd:cd03256 206 DLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
251-651 |
7.15e-21 |
|
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: 96.43 E-value: 7.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 251 MDDRIAGLLSEAGLpDAATRARQFpHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTA 330
Cdd:TIGR02633 117 MYLRAKNLLRELQL-DADNVTRPV-GDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 331 VLFITHDLGLAAERAQHIVVMYKGQvvesgpslevlqhpqHPYTKrlvaAAPSLASQRIIsAKERGEDADALLDH--HIA 408
Cdd:TIGR02633 194 CVYISHKLNEVKAVCDTICVIRDGQ---------------HVATK----DMSTMSEDDII-TMMVGREITSLYPHepHEI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 409 GESTLEkSEHIiTVDHLTKefklPRKKEmfkaVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPT-SGKVFYEGR 487
Cdd:TIGR02633 254 GDVILE-ARNL-TCWDVIN----PHRKR----VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGK 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 488 DTSTFKSKDLLGFRRHVQPVFQNPYGSLDPM-------YSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVMGR 560
Cdd:TIGR02633 324 PVDIRNPAQAIRAGIAMVPEDRKRHGIVPILgvgknitLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 561 ypneLSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQH 640
Cdd:TIGR02633 404 ----LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVLGLSDRVLVIGE 478
|
410
....*....|....*
gi 2545376782 641 GKL----VEHATTDE 651
Cdd:TIGR02633 479 GKLkgdfVNHALTQE 493
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-360 |
1.17e-20 |
|
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: 90.66 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIDFttdtgKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAKQSE 99
Cdd:cd03259 1 LELKGLSKTY-----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDS----GEILIDGRDVTGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 fdklRGTkmGLVPQDPmsNLNPvwrigtqvkealkannmdvaHekrsalakalagdevevkgnddetflgakelpelMTe 179
Cdd:cd03259 72 ----RNI--GMVFQDY--ALFP--------------------H----------------------------------LT- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 180 akkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagVADDQAWYLAKKYVTGSTMDDRIAGLL 259
Cdd:cd03259 89 -----------------------------------------------------VAENIAFGLKLRGVPKAEIRARVRELL 115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 260 SEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLG 339
Cdd:cd03259 116 ELVGLEGLLNR---YPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQE 192
|
330 340
....*....|....*....|.
gi 2545376782 340 LAAERAQHIVVMYKGQVVESG 360
Cdd:cd03259 193 EALALADRIAVMNEGRIVQVG 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
443-660 |
1.39e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.94 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRdtstfKSKDLLGFRRHVQPVFQNpYgSLDPMYSIF 522
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-----RMNDVPPAERGVGMVFQS-Y-ALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 523 RSIEEPLRIHKIgDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQ 602
Cdd:PRK11000 94 ENMSFGLKLAGA-KKEEINQRVNQVAEVLQL-AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 603 VLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQKQY 660
Cdd:PRK11000 172 MRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRF 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
419-651 |
1.60e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 91.69 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFK--LPRKKemfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSkd 496
Cdd:COG1101 1 MLELKNLSKTFNpgTVNEK---RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 497 llgFRR--HVQPVFQNPY----GSLdpmysifrSIEEPLRIH---------KIGDKKWRANRVKELLDMVEM-----PAS 556
Cdd:COG1101 76 ---YKRakYIGRVFQDPMmgtaPSM--------TIEENLALAyrrgkrrglRRGLTKKRRELFRELLATLGLglenrLDT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 557 VMGrypnELSGGQRQriAIARAMAL--DPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDL--AVvrQIA 632
Cdd:COG1101 145 KVG----LLSGGQRQ--ALSLLMATltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMeqAL--DYG 216
|
250
....*....|....*....
gi 2545376782 633 DEVVVMQHGKLVEHATTDE 651
Cdd:COG1101 217 NRLIMMHEGRIILDVSGEE 235
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
250-373 |
1.74e-20 |
|
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: 90.86 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 250 TMDDRIAGLLSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGT 329
Cdd:cd03296 112 EIRAKVHELLKLVQLDWLADR---YPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHV 188
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2545376782 330 AVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPY 373
Cdd:cd03296 189 TTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
44-358 |
2.10e-20 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 90.49 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 44 NFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEEIAGAKQSEFDKLRGTKMGLVPQdpMSNLNPVW 123
Cdd:TIGR02211 25 SLSIGKGEIVAIVGSSGSGKST----LLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQ--FHHLLPDF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 124 RIGTQVKEALKANNMDVAHEKRSALAkalagdevevkgnddetflgakelpelmteakkalteagvsgeafdkavarftn 203
Cdd:TIGR02211 99 TALENVAMPLLIGKKSVKEAKERAYE------------------------------------------------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 204 ewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmddriagLLSEAGLPDaatRARQFPHEFSGGMR 283
Cdd:TIGR02211 125 ------------------------------------------------------MLEKVGLEH---RINHRPSELSGGER 147
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 284 QRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLaAERAQHIVVMYKGQVVE 358
Cdd:TIGR02211 148 QRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLEL-AKKLDRVLEMKDGQLFN 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
440-625 |
2.28e-20 |
|
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: 95.12 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPYgsldpmy 519
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRVSVCAQDAH------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 sIF-RSIEEPLRIHK---IGDKKWRANRVKELLDMVE-MP---ASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEA 591
Cdd:TIGR02868 420 -LFdTTVRENLRLARpdaTDEELWAALERVGLADWLRaLPdglDTVLGEGGARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....
gi 2545376782 592 VSALDVLVQDQVLRLLndLQAEKGLSYLFITHDL 625
Cdd:TIGR02868 499 TEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
440-652 |
3.35e-20 |
|
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: 89.89 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLgfRRHVQPVfqnPYGSldpmy 519
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA--RAGIAYV---PQGR----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 SIFR--SIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDV 597
Cdd:TIGR03410 85 EIFPrlTVEENLLTGLAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 598 LVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEV 652
Cdd:TIGR03410 165 SIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
441-653 |
3.55e-20 |
|
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: 90.53 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYegrdtstfkskdLLGFRR-------------HVQPV 507
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVR------------LFGERRggedvwelrkrigLVSPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 508 FQNP---------------YGSLDpmysIFRSIEEPLRihkigdkkwraNRVKELLDMVEMpASVMGRYPNELSGGQRQR 572
Cdd:COG1119 87 LQLRfprdetvldvvlsgfFDSIG----LYREPTDEQR-----------ERARELLELLGL-AHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 573 IAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEV 652
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
.
gi 2545376782 653 F 653
Cdd:COG1119 231 L 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-366 |
4.02e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.82 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDTgKPvhAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIagaKQ 97
Cdd:PRK13632 6 VMIKVENVSFSYPNSE-NN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQS----GEIKIDGITI---SK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 98 SEFDKLRgTKMGLVPQDPmsnlnpvwrigtqvkealkannmdvahekrsalakalagdevevkgndDETFLGAKelpelm 177
Cdd:PRK13632 76 ENLKEIR-KKIGIIFQNP------------------------------------------------DNQFIGAT------ 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 178 teakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagVADDQAWYLAKKYVTGSTMDDRIAG 257
Cdd:PRK13632 101 -------------------------------------------------------VEDDIAFGLENKKVPPKKMKDIIDD 125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 LLSEAGLPDAATRArqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHD 337
Cdd:PRK13632 126 LAKKVGMEDYLDKE---PQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHD 202
|
330 340
....*....|....*....|....*....
gi 2545376782 338 LGlAAERAQHIVVMYKGQVVESGPSLEVL 366
Cdd:PRK13632 203 MD-EAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-380 |
4.36e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.46 E-value: 4.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDlaIDFTTDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEEIAGAKQSE 99
Cdd:COG1132 340 IEFEN--VSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKST----LVNLLLRFYDPTSGRILIDGVDIRDLTLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 fdkLRGtKMGLVPQDPM--SnlnpvwriGTqVKEALkannmdvahekrsALAKALAGDEvevkgnddetflgakelpelm 177
Cdd:COG1132 412 ---LRR-QIGVVPQDTFlfS--------GT-IRENI-------------RYGRPDATDE--------------------- 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 178 tEAKKALTEAGvsgeafdkavarftnewvpgsetrwrvADDLIKAgvaddlikagvaddqawyLAKKYVTgstmddriag 257
Cdd:COG1132 445 -EVEEAAKAAQ---------------------------AHEFIEA------------------LPDGYDT---------- 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 LLSEAGlpdaatrarqfpHEFSGGMRQRalIAI--GLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDslGTAVLFIT 335
Cdd:COG1132 469 VVGERG------------VNLSGGQRQR--IAIarALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIA 532
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2545376782 336 HDLGlAAERAQHIVVMYKGQVVESGPSLEVLQhpQHPYTKRLVAA 380
Cdd:COG1132 533 HRLS-TIRNADRILVLDDGRIVEQGTHEELLA--RGGLYARLYRL 574
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
444-651 |
4.98e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.53 E-value: 4.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 444 VSFSVKRGTTLAIVGESGSGKSTVANMVLHLLkPTSGKVFYEGRDtstFKSKDLLGFRRHVQPVFQNP---YGSL----- 515
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIE---LRELDPESWRKHLSWVGQNPqlpHGTLrdnvl 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 516 --DPMYSifrsiEEplRIHKIGDKKWRANRVKELLDMVEMPAS-VMGRypneLSGGQRQRIAIARAMALDPDVIVCDEAV 592
Cdd:PRK11174 445 lgNPDAS-----DE--QLQQALENAWVSEFLPLLPQGLDTPIGdQAAG----LSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 593 SALDVLVQDQVLRLLNdlQAEKGLSYLFITHDLAVVRQIaDEVVVMQHGKLVEHATTDE 651
Cdd:PRK11174 514 ASLDAHSEQLVMQALN--AASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAE 569
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
440-656 |
8.50e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 89.28 E-value: 8.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLgfRRHVQPVFQNpygsldpmY 519
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA--RMGVVRTFQH--------V 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 SIFRSIE--EPLRI--HK-------IGDKKWRANRVKE---------------LLDMVEMPASvmgrypnELSGGQRQRI 573
Cdd:PRK11300 90 RLFREMTviENLLVaqHQqlktglfSGLLKTPAFRRAEsealdraatwlervgLLEHANRQAG-------NLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 574 AIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVF 653
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
...
gi 2545376782 654 DHP 656
Cdd:PRK11300 243 NNP 245
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
416-647 |
8.73e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 88.68 E-value: 8.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKefKLPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSK 495
Cdd:PRK10584 3 AENIVEVHHLKK--SVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 496 DLLGFR-RHVQPVFQNPYgsLDPMYSIFRSIEEPLRIHKIGDKKWRaNRVKELLDMVEMpASVMGRYPNELSGGQRQRIA 574
Cdd:PRK10584 81 ARAKLRaKHVGFVFQSFM--LIPTLNALENVELPALLRGESSRQSR-NGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 575 IARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLavvrQIA---DEVVVMQHGKLVEHA 647
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDL----QLAarcDRRLRLVNGQLQEEA 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-356 |
1.04e-19 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 87.95 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIDFTtdtGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIagakqSE 99
Cdd:COG4619 1 LELEGLSFRVG---GKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTS----GEIYLDGKPL-----SA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 FD--KLRgTKMGLVPQDPmsnlnpvwrigtqvkealkannmdvahekrsalakalagdevevkgnddetflgakelpelm 177
Cdd:COG4619 67 MPppEWR-RQVAYVPQEP-------------------------------------------------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 178 teakkalteagvsgeafdkavarftnEWVPGSetrwrvaddlikagVADDLikagvadDQAWYLAKKYVTgstmDDRIAG 257
Cdd:COG4619 84 --------------------------ALWGGT--------------VRDNL-------PFPFQLRERKFD----RERALE 112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 LLSEAGLPDAATRARqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHD 337
Cdd:COG4619 113 LLERLGLPPDILDKP--VERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHD 190
|
330
....*....|....*....
gi 2545376782 338 LGLAAERAQHIVVMYKGQV 356
Cdd:COG4619 191 PEQIERVADRVLTLEAGRL 209
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
432-642 |
1.21e-19 |
|
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: 87.52 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 432 PRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRdtstfkskdlLGFrrhvqpVFQNP 511
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS----------IAY------VSQEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 512 YgsldpmysIFR-SIEEPLRIHKIGDKKWrANRVKE----LLDMVEMPA---SVMGRYPNELSGGQRQRIAIARAMALDP 583
Cdd:cd03250 76 W--------IQNgTIRENILFGKPFDEER-YEKVIKacalEPDLEILPDgdlTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545376782 584 DVIVCDEAVSALDVLVQDQVLR--LLNDLQAEKglSYLFITHDLAVVRQiADEVVVMQHGK 642
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
251-362 |
2.02e-19 |
|
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: 87.62 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 251 MDDRIAGLLSEAGLPDAATRaRQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlgTA 330
Cdd:cd03260 116 LDERVEEALRKAALWDEVKD-RLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YT 192
|
90 100 110
....*....|....*....|....*....|..
gi 2545376782 331 VLFITHDLGLAAERAQHIVVMYKGQVVESGPS 362
Cdd:cd03260 193 IVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
440-648 |
2.09e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 92.47 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTT--------------LAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQ 505
Cdd:PRK10790 342 DIDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 506 PVFQNPYGSLDPMY---SIFRSIEEplrihkigDKKWRANRVKELLDMV-EMPA---SVMGRYPNELSGGQRQRIAIARA 578
Cdd:PRK10790 419 MVQQDPVVLADTFLanvTLGRDISE--------EQVWQALETVQLAELArSLPDglyTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 579 MALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLsyLFITHDLAVVRQiADEVVVMQHGKLVEHAT 648
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL--VVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
456-653 |
2.59e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.53 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 456 IVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStFKSKDLLGFRRHVQPVFQNPYGSLdpMYS-IFRSIEEPLRIHKI 534
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPEQQI--FYTdIDSDIAFSLRNLGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 535 GDKKWrANRVKELLDMVEmpASVMGRYPNE-LSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAE 613
Cdd:PRK13638 109 PEAEI-TRRVDEALTLVD--AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2545376782 614 kGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVF 653
Cdd:PRK13638 186 -GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
29-367 |
4.01e-19 |
|
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: 86.90 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 29 FTTDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEEIAGAKQSEFDKlrgtKM 108
Cdd:cd03253 8 FAYDPGRPV--LKDVSFTIPAGKKVAIVGPSGSGKST----ILRLLFRFYDVSSGSILIDGQDIREVTLDSLRR----AI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 109 GLVPQDpmsnlNPVWrigtqvkealkanNMDVAHEKRSalakalagdevevkGNDDETflgakelPELMTEAKKAlteag 188
Cdd:cd03253 78 GVVPQD-----TVLF-------------NDTIGYNIRY--------------GRPDAT-------DEEVIEAAKA----- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 189 vsgeafdkavarftnewvpgsetrwrvaddlikAGVADDLIKagvaddqawyLAKKYVTgstmddrIAGllsEAGLpdaa 268
Cdd:cd03253 114 ---------------------------------AQIHDKIMR----------FPDGYDT-------IVG---ERGL---- 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 269 trarqfphEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDslGTAVLFITHDLGLAAErAQHI 348
Cdd:cd03253 137 --------KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKI 205
|
330
....*....|....*....
gi 2545376782 349 VVMYKGQVVESGPSLEVLQ 367
Cdd:cd03253 206 IVLKDGRIVERGTHEELLA 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
276-355 |
4.04e-19 |
|
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: 84.60 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 276 HEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKGQ 355
Cdd:cd00267 79 PQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
440-638 |
4.74e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.36 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYegrdtstfkskdllgfRRHVQPVFQNPYGSLDPMY 519
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRR----------------AGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 SIfrSIEE-----------PLRIHKIGDKKwranRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVC 588
Cdd:NF040873 71 PL--TVRDlvamgrwarrgLWRRLTRDDRA----AVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2545376782 589 DEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQiADEVVVM 638
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
233-378 |
1.16e-18 |
|
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: 87.55 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 233 VADDQAWYLAKKYVTGSTMDDRIAGLLSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTV 312
Cdd:TIGR01187 59 VEENVAFGLKMRKVPRAEIKPRVLEALRLVQLEEFADR---KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKL 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 313 QKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLV 378
Cdd:TIGR01187 136 RDQMQLELKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
273-369 |
1.21e-18 |
|
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: 87.85 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 273 QFPHEFSGGMRQRalIAIG--LACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVV 350
Cdd:COG4148 129 RRPATLSGGERQR--VAIGraLLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVL 206
|
90
....*....|....*....
gi 2545376782 351 MYKGQVVESGPSLEVLQHP 369
Cdd:COG4148 207 LEQGRVVASGPLAEVLSRP 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-645 |
1.23e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTtdtgkPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEEiagakq 97
Cdd:PRK09700 4 PYISMAGIGKSFG-----PVHALKSVNLTVYPGEIHALLGENGAGKST----LMKVLSGIHEPTKGTITINNIN------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 98 seFDKLrgtkmglvpqDPmsnlnpvwRIGTQvkealkaNNMDVAHEKRSALakalagDEVEVKGNddeTFLGakELPelm 177
Cdd:PRK09700 69 --YNKL----------DH--------KLAAQ-------LGIGIIYQELSVI------DELTVLEN---LYIG--RHL--- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 178 teAKKALteaGVSgeafdkavarftneWVPGSETRWRVADDLIKAGVADDLikagvaddqawylakkyvtgstmDDRIAG 257
Cdd:PRK09700 108 --TKKVC---GVN--------------IIDWREMRVRAAMMLLRVGLKVDL-----------------------DEKVAN 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 LlseaglpdaatrarqfphefSGGMRQRALIAIGLACRPDLLIADEPTSALdvtVQKRIlDHLHMLTDSL---GTAVLFI 334
Cdd:PRK09700 146 L--------------------SISHKQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEV-DYLFLIMNQLrkeGTAIVYI 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 335 THDLGLAAERAQHIVVMYKGQVVESGPSLEVlqhpqhpYTKRLVaaapslasqRIISAKErgedadaLLDHHIAGESTLE 414
Cdd:PRK09700 202 SHKLAEIRRICDRYTVMKDGSSVCSGMVSDV-------SNDDIV---------RLMVGRE-------LQNRFNAMKENVS 258
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 415 KSEH--IITVDHLTkefklpRKKemFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTf 492
Cdd:PRK09700 259 NLAHetVFEVRNVT------SRD--RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP- 329
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 493 kSKDLLGFRRHVQPVFQNPYGS-LDPMYSIFR--SIEEPLRIHKIG---------DKKWRANRVKELLdmvEMPASVMGR 560
Cdd:PRK09700 330 -RSPLDAVKKGMAYITESRRDNgFFPNFSIAQnmAISRSLKDGGYKgamglfhevDEQRTAENQRELL---ALKCHSVNQ 405
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 561 YPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQH 640
Cdd:PRK09700 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCE 484
|
....*
gi 2545376782 641 GKLVE 645
Cdd:PRK09700 485 GRLTQ 489
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
258-376 |
1.38e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.96 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 LLSEAGLpdaATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLfITHD 337
Cdd:PRK11264 128 LLAKVGL---AGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHE 203
|
90 100 110
....*....|....*....|....*....|....*....
gi 2545376782 338 LGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKR 376
Cdd:PRK11264 204 MSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
279-355 |
1.54e-18 |
|
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: 83.78 E-value: 1.54e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQ 355
Cdd:cd03229 102 SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
233-373 |
1.75e-18 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 85.24 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 233 VADDQAWYLAKKYVTGSTMDDRIAGLLSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTV 312
Cdd:TIGR00968 89 VRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDR---YPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKV 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545376782 313 QKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPY 373
Cdd:TIGR00968 166 RKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPF 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
233-370 |
1.75e-18 |
|
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: 84.98 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 233 VADDQAWYLAKKYVTGSTMDDRIAGLLSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTV 312
Cdd:cd03300 89 VFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 313 QKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQ 370
Cdd:cd03300 166 RKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
258-372 |
2.17e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 85.14 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 LLSEAGLpdaATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHD 337
Cdd:PRK09493 120 LLAKVGL---AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHE 195
|
90 100 110
....*....|....*....|....*....|....*
gi 2545376782 338 LGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHP 372
Cdd:PRK09493 196 IGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
441-643 |
2.49e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPYGSLDpmYS 520
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA---SRRVASVPQDTSLSFE--FD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 521 IFRSIE-----EPLRIHKIGDKKWRAnrVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSAL 595
Cdd:PRK09536 94 VRQVVEmgrtpHRSRFDTWTETDRAA--VERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2545376782 596 DVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKL 643
Cdd:PRK09536 171 DINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-370 |
5.96e-18 |
|
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: 83.64 E-value: 5.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIDFttdtgKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAKQSE 99
Cdd:cd03219 1 LEVRGLTKRF-----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTS----GSVLFDGEDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 FdklrgTKMGLVP--QDP-----MSnlnpvwrigtqVKEalkanNMDVAHEKRSALAKALAGDevevkgnddetflgAKE 172
Cdd:cd03219 72 I-----ARLGIGRtfQIPrlfpeLT-----------VLE-----NVMVAAQARTGSGLLLARA--------------RRE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 173 LPELMTEAKKALTEAGVSGEAfdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmd 252
Cdd:cd03219 117 EREARERAEELLERVGLADLA----------------------------------------------------------- 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 DRIAGLLSeaglpdaatrarqfphefsGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVL 332
Cdd:cd03219 138 DRPAGELS-------------------YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVL 197
|
330 340 350
....*....|....*....|....*....|....*...
gi 2545376782 333 FITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQ 370
Cdd:cd03219 198 LVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
441-645 |
7.30e-18 |
|
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: 82.19 E-value: 7.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHL--LKPTSGKVFYEGRDTsTFKSKD---LLGfrrhvqpvfqnpygsl 515
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDI-TDLPPEeraRLG---------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 516 dpmysIFRSIEEPLRIHKIgdkkwranRVKELLdmvempasvmgRYPNE-LSGGQRQRIAIARAMALDPDVIVCDEAVSA 594
Cdd:cd03217 79 -----IFLAFQYPPEIPGV--------KNADFL-----------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 595 LDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQI-ADEVVVMQHGKLVE 645
Cdd:cd03217 135 LDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
259-380 |
7.50e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.38 E-value: 7.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 LSEAGLPDAAT-RARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLgtAVLFITHD 337
Cdd:PRK14271 144 LTEVGLWDAVKdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHN 221
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2545376782 338 LGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAA 380
Cdd:PRK14271 222 LAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAG 264
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
378-651 |
8.94e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.19 E-value: 8.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 378 VAAAPSLASQRIISAKERGEDADALLDHHIAGESTLEKSEHIITVDHLTkeFKLPRKKEmfKAVDDVSFSVKRGTTLAIV 457
Cdd:PRK11160 297 VAGAFQHLGQVIASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVS--FTYPDQPQ--PVLKGLSLQIKAGEKVALL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 458 GESGSGKSTVanmvLHLL----KPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPYgsldpmysIFR-SIEEPLRI- 531
Cdd:PRK11160 373 GRTGCGKSTL----LQLLtrawDPQQGEILLNGQPIADYSEAAL---RQAISVVSQRVH--------LFSaTLRDNLLLa 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 532 -HKIGDKKWRA--NRV--KELLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRL 606
Cdd:PRK11160 438 aPNASDEALIEvlQQVglEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILEL 517
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2545376782 607 LNDLQAEKGLsyLFITHDLAVVRQIaDEVVVMQHGKLVEHATTDE 651
Cdd:PRK11160 518 LAEHAQNKTV--LMITHRLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
439-657 |
9.41e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 9.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTF----KSKDLLGFRRHVQPVFQNpygs 514
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhaRARRGIGYLPQEASIFRR---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 515 ldpmYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSA 594
Cdd:PRK10895 93 ----LSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 595 LDVLVQDQVLRLLNDLQaEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQ 657
Cdd:PRK10895 168 VDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
275-370 |
9.97e-18 |
|
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: 82.77 E-value: 9.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 275 PHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKG 354
Cdd:cd03299 127 PETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNG 206
|
90
....*....|....*.
gi 2545376782 355 QVVESGPSLEVLQHPQ 370
Cdd:cd03299 207 KLIQVGKPEEVFKKPK 222
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
442-670 |
1.47e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.11 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 442 DDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPYGSLD----P 517
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV---ARRIGLLAQNATTPGDitvqE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 518 MYSIFRSIEEPLRihkigdKKWRanrvKELLDMVE--MPAS----VMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEA 591
Cdd:PRK10253 101 LVARGRYPHQPLF------TRWR----KEDEEAVTkaMQATgithLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 592 VSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATtdevfdhPQKQYTRDLLDAIPG 670
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA-------PKEIVTAELIERIYG 242
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
251-381 |
1.70e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.58 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 251 MDDRIAGLLSEAGLPD-AATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLgt 329
Cdd:PRK14267 122 LDERVEWALKKAALWDeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY-- 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 330 AVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAA 381
Cdd:PRK14267 200 TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGA 251
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
382-656 |
1.85e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 86.30 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 382 PSLASQRIISAKERGEDA----DALLDHHIA---GESTLEKSEHIITVDhlTKEFKLPRKKEMfkAVDDVSFSVKRGTTL 454
Cdd:PRK10789 269 PMLALAWMFNIVERGSAAysriRAMLAEAPVvkdGSEPVPEGRGELDVN--IRQFTYPQTDHP--ALENVNFTLKPGQML 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 455 AIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKskdLLGFRRHVQPVFQNPYGSLDPMYSIF---------RSI 525
Cdd:PRK10789 345 GICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ---LDSWRSRLAVVSQTPFLFSDTVANNIalgrpdatqQEI 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 526 EEPLRIHKIGDkkwranrvkellDMVEMPASvmgrYPNE-------LSGGQRQRIAIARAMALDPDVIVCDEAVSALDVL 598
Cdd:PRK10789 422 EHVARLASVHD------------DILRLPQG----YDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGR 485
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 599 VQDQVLRLLNdlQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDEVFDHP 656
Cdd:PRK10789 486 TEHQILHNLR--QWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
239-367 |
2.20e-17 |
|
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: 82.21 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 239 WYLAKKY-VTGSTMDDRIAGLLSEAGLPD-AATRArqfpHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRI 316
Cdd:COG4555 96 RYFAELYgLFDEELKKRIEELIELLGLEEfLDRRV----GELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLL 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2545376782 317 LDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQ 367
Cdd:COG4555 172 REILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
420-653 |
2.24e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.62 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLG 499
Cdd:PRK15056 7 IVVNDVTVTWR-----NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVfqnpygslDPMYSIFrsIEEPLRIHKIGDKKW--RAN-----RVKELLDMVEMpASVMGRYPNELSGGQRQR 572
Cdd:PRK15056 82 YVPQSEEV--------DWSFPVL--VEDVVMMGRYGHMGWlrRAKkrdrqIVTAALARVDM-VEFRHRQIGELSGGQKKR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 573 IAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADeVVVMQHGKLVEHATTDEV 652
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETT 228
|
.
gi 2545376782 653 F 653
Cdd:PRK15056 229 F 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
450-657 |
2.56e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.77 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 450 RGTTlAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGR---DTStfKSKDLLGFRRHVQPVFQNpyGSLDPMYSIfrsiE 526
Cdd:PRK11144 24 QGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAE--KGICLPPEKRRIGYVFQD--ARLFPHYKV----R 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 527 EPLRIhkiGDKKWRA---NRVKELLDMvempASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQV 603
Cdd:PRK11144 95 GNLRY---GMAKSMVaqfDKIVALLGI----EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 604 LRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHPQ 657
Cdd:PRK11144 168 LPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
38-356 |
2.58e-17 |
|
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: 81.04 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 38 HAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAKQsEFDKLRgTKMGLVPQDpmS 117
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDS----GTIIIDGLKLTDDKK-NINELR-QKVGMVFQQ--F 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 118 NLNPvwrigtqvkealkanNMDVahekrsalakalagdevevkgnddetflgakelpelmteaKKALTEAgvsgeafdka 197
Cdd:cd03262 86 NLFP---------------HLTV----------------------------------------LENITLA---------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 198 varftnewvpgsetrwrvaddlikagvaddLIKA-GVADDQAWYLAKKyvtgstmddriagLLSEAGLPDaatRARQFPH 276
Cdd:cd03262 101 ------------------------------PIKVkGMSKAEAEERALE-------------LLEKVGLAD---KADAYPA 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKGQV 356
Cdd:cd03262 135 QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
20-355 |
4.05e-17 |
|
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: 79.35 E-value: 4.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDlaIDFTTDtGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEIAGAKQSE 99
Cdd:cd03228 1 IEFKN--VSFSYP-GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT----SGEILIDGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 fdkLRGtKMGLVPQDPmsnlnpvwrigtqvkealkannmdvahekrsalakalagdevevkgnddetFLgakelpelmte 179
Cdd:cd03228 74 ---LRK-NIAYVPQDP---------------------------------------------------FL----------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 180 akkalteagvsgeaFDkavarftnewvpGSetrwrVADDLikagvaddlikagvaddqawylakkyvtgstmddriagll 259
Cdd:cd03228 88 --------------FS------------GT-----IRENI---------------------------------------- 96
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 260 seaglpdaatrarqfpheFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDslGTAVLFITHDLG 339
Cdd:cd03228 97 ------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLS 156
|
330
....*....|....*.
gi 2545376782 340 LaAERAQHIVVMYKGQ 355
Cdd:cd03228 157 T-IRDADRIIVLDDGR 171
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-367 |
5.56e-17 |
|
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: 80.56 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLaidfttDTG-KPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPgtghVVNGSIKLDGEEIAGAKQS 98
Cdd:cd03224 1 LEVENL------NAGyGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP----PRSGSIRFDGRDITGLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 99 EFDKlRGtkMGLVPQDPM--SNLNpvwrigtqVKEalkanNMDVAhekrsalAKALAGDEVEvkgnddetflgakelpel 176
Cdd:cd03224 71 ERAR-AG--IGYVPEGRRifPELT--------VEE-----NLLLG-------AYARRRAKRK------------------ 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 177 mteakkalteagvsgEAFDKAVARFtnewvPGSETRWrvaddlikagvaddlikagvaddqawylakkyvtgstmdDRIA 256
Cdd:cd03224 110 ---------------ARLERVYELF-----PRLKERR---------------------------------------KQLA 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 257 GLLSeaglpdaatrarqfphefsGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITH 336
Cdd:cd03224 131 GTLS-------------------GGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQ 190
|
330 340 350
....*....|....*....|....*....|.
gi 2545376782 337 DLGLAAERAQHIVVMYKGQVVESGPSLEVLQ 367
Cdd:cd03224 191 NARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
420-623 |
6.14e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 78.73 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTkeFKLPRKKemfKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFkskdllg 499
Cdd:cd03223 1 IELENLS--LATPDGR---VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLF------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 frrhvqpVFQNPY---GSLdpmysifrsieeplrihkigdkkwranrvKELLdmvempasvmgRYP--NELSGGQRQRIA 574
Cdd:cd03223 69 -------LPQRPYlplGTL-----------------------------REQL-----------IYPwdDVLSGGEQQRLA 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2545376782 575 IARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNdlqaEKGLSYLFITH 623
Cdd:cd03223 102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
436-658 |
7.78e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.08 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 436 EMFKavdDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEgrDTSTFKSKDLLGFRRHVQPVFQNP---- 511
Cdd:PTZ00265 399 EIYK---DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSKIGVVSQDPllfs 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 512 --------YG--SLDPMYSIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPAS------------------------- 556
Cdd:PTZ00265 474 nsiknnikYSlySLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTtdsneliemrknyqtikdsevvdvs 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 557 ------------------VMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSY 618
Cdd:PTZ00265 554 kkvlihdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2545376782 619 LFITHDLAVVRqIADEVVVMQHGKLVEHATTDEVFDHPQK 658
Cdd:PTZ00265 634 IIIAHRLSTIR-YANTIFVLSNRERGSTVDVDIIGEDPTK 672
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
417-644 |
8.34e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.68 E-value: 8.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 417 EHIITVDHLTKEFKLPRkkemfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKD 496
Cdd:PRK09700 3 TPYISMAGIGKSFGPVH------ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 497 llgfrrhvqpVFQNPYGSLDPMYSIFR--SIEEPLRIHKIGDKK--------WRANRVK--ELLDMVEMPASVMGRYPNe 564
Cdd:PRK09700 77 ----------AAQLGIGIIYQELSVIDelTVLENLYIGRHLTKKvcgvniidWREMRVRaaMMLLRVGLKVDLDEKVAN- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 565 LSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:PRK09700 146 LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-357 |
1.15e-16 |
|
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: 79.22 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 21 EVKDLAIDFttdtGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAgakqsef 100
Cdd:cd03226 1 RIENISFSY----KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESS----GSILLNGKPIK------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 101 DKLRGTKMGLVPQDPmsnlnpvwriGTQvkealkannmdvahekrsalakaLAGDEVEvkgndDETFLGAKELPELMTEA 180
Cdd:cd03226 66 AKERRKSIGYVMQDV----------DYQ-----------------------LFTDSVR-----EELLLGLKELDAGNEQA 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 181 KKALTEAGVSGeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstMDDRiaglls 260
Cdd:cd03226 108 ETVLKDLDLYA-----------------------------------------------------------LKER------ 122
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 261 eaglpdaatrarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGL 340
Cdd:cd03226 123 -------------HPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEF 188
|
330
....*....|....*..
gi 2545376782 341 AAERAQHIVVMYKGQVV 357
Cdd:cd03226 189 LAKVCDRVLLLANGAIV 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
272-395 |
1.33e-16 |
|
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: 81.70 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 272 RQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVM 351
Cdd:TIGR02142 126 GRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVL 205
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2545376782 352 YKGQVVESGPSLEVLQHPQHPYTKRLVAAapSLASQRIISAKER 395
Cdd:TIGR02142 206 EDGRVAAAGPIAEVWASPDLPWLAREDQG--SLIEGVVAEHDQH 247
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
420-643 |
1.37e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.11 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprKKEMFKAVDdvsFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYegrdtstfKSKDLLG 499
Cdd:PRK11247 13 LLLNAVSKRYG---ERTVLNQLD---LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA--------GTAPLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 FRRHVQPVFQNpyGSLDPMYSIFRSIEEPLRihkiGDkkWRAnRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAM 579
Cdd:PRK11247 79 AREDTRLMFQD--ARLLPWKKVIDNVGLGLK----GQ--WRD-AALQALAAVGL-ADRANEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKL 643
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
406-640 |
1.44e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.23 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 406 HIAGESTLEKSEHIITVdhlTKEFKLPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYE 485
Cdd:COG2401 14 TKVYSSVLDLSERVAIV---LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 486 grdtstfkskdllgfrrhvqpVFQNPYGSldpmysifrsiEEPL--RIHKIGDKKwranRVKELLDMVEM-PASVMGRYP 562
Cdd:COG2401 91 ---------------------VPDNQFGR-----------EASLidAIGRKGDFK----DAVELLNAVGLsDAVLWLRRF 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 563 NELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQH 640
Cdd:COG2401 135 KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
251-394 |
1.45e-16 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 80.91 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 251 MDDRIAGLLSEAGLpDAATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTA 330
Cdd:COG1125 111 IRARVDELLELVGL-DPEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKT 189
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 331 VLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSLASQRIISAKE 394
Cdd:COG1125 190 IVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGADRGLRRLSLLRVED 253
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
397-623 |
2.51e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 397 EDADALLDHHIAGESTLEKSE-HIITVDHLTkeFKLPRKKEMfkaVDDVSFSVKRGTTLAIVGESGSGKSTvanmvlhLL 475
Cdd:COG4178 339 EEALEAADALPEAASRIETSEdGALALEDLT--LRTPDGRPL---LEDLSLSLKPGERLLITGPSGSGKST-------LL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 476 KPTSGK-VFYEGRdtstfkskdlLGFRRHVQPVF--QNPY---GSLDPM--YsifrsieePLRIHKIGDKkwranRVKEL 547
Cdd:COG4178 407 RAIAGLwPYGSGR----------IARPAGARVLFlpQRPYlplGTLREAllY--------PATAEAFSDA-----ELREA 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 548 LDMVEMPA-----SVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLndLQAEKGLSYLFIT 622
Cdd:COG4178 464 LEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVG 541
|
.
gi 2545376782 623 H 623
Cdd:COG4178 542 H 542
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
420-646 |
2.61e-16 |
|
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: 77.59 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKLPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANmVL---HLLKPTSGKVFYEGRDTSTFKSKD 496
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLN-ALagrRTGLGVSGEVLINGRPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 497 LLGFrrhvqpVFQNP--YGSLdpmysifrSIEEPLRIHkigdkkwranrvkelldmvempASVMGrypneLSGGQRQRIA 574
Cdd:cd03213 83 IIGY------VPQDDilHPTL--------TVRETLMFA----------------------AKLRG-----LSGGERKRVS 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 575 IARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDL-AVVRQIADEVVVMQHGKLVEH 646
Cdd:cd03213 122 IALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYF 193
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
253-381 |
3.84e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.86 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 DRIAGLLSEAGLPDAATRarQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVL 332
Cdd:PRK10619 130 ERAVKYLAKVGIDERAQG--KYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMV 206
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2545376782 333 FITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAA 381
Cdd:PRK10619 207 VVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLKGS 255
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
277-637 |
3.89e-16 |
|
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: 82.14 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYkGQ- 355
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY-GEp 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 356 ----VVesgpslevlqhpQHPYTKRlVAaapslasqriISAKERG----EDA---DALLDHHIAGESTLEKSEHIITVDH 424
Cdd:COG1245 290 gvygVV------------SKPKSVR-VG----------INQYLDGylpeENVrirDEPIEFEVHAPRREKEEETLVEYPD 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 425 LTK---EFKLprkkemfkAVDdvSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVF---------------YEG 486
Cdd:COG1245 347 LTKsygGFSL--------EVE--GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkisykpqyispdYDG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 487 RdtstfkSKDLLgfRRHVQPVFQNpygsldpmySIFRS-IEEPLRIHKIgdkkwranrvkelldmvempasvMGRYPNEL 565
Cdd:COG1245 417 T------VEEFL--RSANTDDFGS---------SYYKTeIIKPLGLEKL-----------------------LDKNVKDL 456
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 566 SGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVV 637
Cdd:COG1245 457 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
424-644 |
4.02e-16 |
|
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: 78.08 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 424 HLTKEFKLPRKKEMF----KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMV---LHLLKPTSGKVFYEGRDtstfKSKD 496
Cdd:cd03234 2 RVLPWWDVGLKAKNWnkyaRILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQP----RKPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 497 LlgFRRHVQPVFQNPYgsLDPMYSIFRSIE--EPLRIHKIGDKKWRANRVKELLDMVEMPASVMGRYPNELSGGQRQRIA 574
Cdd:cd03234 78 Q--FQKCVAYVRQDDI--LLPGLTVRETLTytAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 575 IARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
259-367 |
4.25e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.66 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 LSEAGLpdAATRARQFPhEFSGGMRQRALIAIGLA------CRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVL 332
Cdd:PRK13548 119 LAQVDL--AHLAGRDYP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVI 195
|
90 100 110
....*....|....*....|....*....|....*
gi 2545376782 333 FITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQ 367
Cdd:PRK13548 196 VVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
440-652 |
5.46e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.68 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTL-------------AIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKdllGFRRHVQP 506
Cdd:PRK10575 13 ALRNVSFRVPGRTLLhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK---AFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 507 VFQNpygsLDPMYSIfrSIEEplrIHKIGDKKWRA----------NRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIA 576
Cdd:PRK10575 90 LPQQ----LPAAEGM--TVRE---LVAIGRYPWHGalgrfgaadrEKVEEAISLVGL-KPLAHRLVDSLSGGERQRAWIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 577 RAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEV 652
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
39-370 |
5.50e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.91 E-value: 5.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 39 AVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEI-AGAKQSEFDKLRgTKMGLVPQDPMS 117
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPT----SGTVTIGERVItAGKKNKKLKPLR-KKVGIVFQFPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 118 NLnpvwrigtqvkealkannmdvahekrsalakalagdevevkgnddetflgakelpelmteakkalteagvsgeaFDKA 197
Cdd:PRK13634 97 QL--------------------------------------------------------------------------FEET 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 198 VARftnewvpgsetrwrvaddlikaGVADDLIKAGVADDQAWYLAKKyvtgstmddriagLLSEAGLP-DAATRArqfPH 276
Cdd:PRK13634 103 VEK----------------------DICFGPMNFGVSEEDAKQKARE-------------MIELVGLPeELLARS---PF 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQV 356
Cdd:PRK13634 145 ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
330
....*....|....
gi 2545376782 357 VESGPSLEVLQHPQ 370
Cdd:PRK13634 225 FLQGTPREIFADPD 238
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
253-370 |
6.43e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 77.75 E-value: 6.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 DRIAGLLSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVL 332
Cdd:COG4161 120 EKAMKLLARLRLTDKADR---FPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVI 196
|
90 100 110
....*....|....*....|....*....|....*...
gi 2545376782 333 fITHDLGLAAERAQHIVVMYKGQVVESGpSLEVLQHPQ 370
Cdd:COG4161 197 -VTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQPQ 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
250-369 |
6.57e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.69 E-value: 6.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 250 TMDDRIAGLLSEAGLPDAATRArqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGT 329
Cdd:PRK13652 113 TVAHRVSSALHMLGLEELRDRV---PHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGM 189
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2545376782 330 AVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHP 369
Cdd:PRK13652 190 TVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-399 |
9.09e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.49 E-value: 9.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 13 QKEHGPLLEVKDLAIDFTTDtgkpvHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEEI 92
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQ-----HAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLAGFEQPTAGQIMLDGVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 93 AgakqsefdklrgtkmgLVP--QDPMsnlnpvwrigtqvkealkanNMdvahekrsalakalagdevevkgnddeTFLGA 170
Cdd:PRK11607 84 S----------------HVPpyQRPI--------------------NM---------------------------MFQSY 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 171 KELPELMTEAKKALteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikaGVADDQawyLAKKYVTgst 250
Cdd:PRK11607 101 ALFPHMTVEQNIAF-----------------------------------------------GLKQDK---LPKAEIA--- 127
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 251 mdDRIAGLLSEAGLPDAATRArqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTA 330
Cdd:PRK11607 128 --SRVNEMLGLVHMQEFAKRK---PHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVT 202
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 331 VLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLVAAAPSLASqriiSAKERGEDA 399
Cdd:PRK11607 203 CVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEG----VLKERQEDG 267
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
420-642 |
9.25e-16 |
|
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: 74.79 E-value: 9.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprKKEMFKavdDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVfyegrdtstfkskdllg 499
Cdd:cd03221 1 IELENLSKTYG---GKLLLK---DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 500 frrhvqpvfqnpygsldpmysifrsieeplrihkigdkKWranrvkelldmveMPASVMGRYPnELSGGQRQRIAIARAM 579
Cdd:cd03221 58 --------------------------------------TW-------------GSTVKIGYFE-QLSGGEKMRLALAKLL 85
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQvlrLLNDLQAEKGlSYLFITHDLAVVRQIADEVVVMQHGK 642
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEA---LEEALKEYPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-367 |
1.04e-15 |
|
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: 77.19 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 21 EVKDlaIDFTTDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEEIagaKQSEF 100
Cdd:cd03249 2 EFKN--VSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLERFYDPTSGEILLDGVDI---RDLNL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 101 DKLRGtKMGLVPQDPMsnlnpvwRIGTQVKEALKAnnmdvahekrsalakalagdevevkGNDDETflgakelpelMTEA 180
Cdd:cd03249 73 RWLRS-QIGLVSQEPV-------LFDGTIAENIRY-------------------------GKPDAT----------DEEV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 181 KKALTEAGvsgeafdkavarftnewvpgsetrwrvADDLIKAgvaddlikagvaddqawyLAKKYVTgstmddriagLLS 260
Cdd:cd03249 110 EEAAKKAN---------------------------IHDFIMS------------------LPDGYDT----------LVG 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 261 EAGLpdaatrarqfphEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRI---LDHLHMltdslGTAVLFITHD 337
Cdd:cd03249 135 ERGS------------QLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVqeaLDRAMK-----GRTTIVIAHR 197
|
330 340 350
....*....|....*....|....*....|
gi 2545376782 338 LgLAAERAQHIVVMYKGQVVESGPSLEVLQ 367
Cdd:cd03249 198 L-STIRNADLIAVLQNGQVVEQGTHDELMA 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
233-370 |
1.05e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.87 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 233 VADDQAWYLAKKYVTGSTMDDRIAGLLSEAGLPDaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTV 312
Cdd:PRK13648 101 VKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLE---RADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 313 QKRILDHLHMLTDSLGTAVLFITHDLGLAAErAQHIVVMYKGQVVESGPSLEVLQHPQ 370
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
271-360 |
1.17e-15 |
|
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: 76.18 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 271 ARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVV 350
Cdd:cd03297 125 LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVV 204
|
90
....*....|
gi 2545376782 351 MYKGQVVESG 360
Cdd:cd03297 205 MEDGRLQYIG 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
276-357 |
1.20e-15 |
|
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: 74.77 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 276 HEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKGQ 355
Cdd:cd03216 81 YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
..
gi 2545376782 356 VV 357
Cdd:cd03216 160 VV 161
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
441-651 |
1.33e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 78.72 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGrdtSTFKSKDLLGFRR-HVQPVFQNpygsLDPMY 519
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG---VPVPARARLARARiGVVPQFDN----LDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 SIFRSIEEPLRIHKIGDKKWRAnRVKELLDMVEMPASVMGRYpNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLV 599
Cdd:PRK13536 130 TVRENLLVFGRYFGMSTREIEA-VIPSLLEFARLESKADARV-SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 600 QDQVLRLLNDLQAeKGLSYLFITHDLAVVRQIADEVVVMQHG-KLVE---HATTDE 651
Cdd:PRK13536 208 RHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEgrpHALIDE 262
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
441-655 |
1.44e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.92 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLgfRRHVQPVFQNpygsLDPMYS 520
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQ--RVGVVPQFDN----LDPDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 521 IFRSIEEPLRIHKIGDKKWRAnRVKELLDMVEMPASVMGRYpNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQ 600
Cdd:PRK13537 97 VRENLLVFGRYFGLSAAAARA-LVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 601 DQVLRLLNDLQAeKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDH 655
Cdd:PRK13537 175 HLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
224-376 |
1.83e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.59 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 224 VADDLIKA-----GVADDQAWYLAKKyvtgstmddriagLLSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDL 298
Cdd:PRK11124 99 VQQNLIEApcrvlGLSKDQALARAEK-------------LLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQV 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 299 LIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLfITHDLGLAAERAQHIVVMYKGQVVESGPSlevlQHPQHPYTKR 376
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGHIVEQGDA----SCFTQPQTEA 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-365 |
2.29e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLaidfTTDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPgtghVVNGSIKLDGEEIAGAKQ 97
Cdd:COG3845 256 VVLEVENL----SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP----PASGSIRLDGEDITGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 98 SEFdklRGTKMGLVPQDPMSNlnpvwrigtqvkealkannmdvahekrsalakALAGDevevkgnddetflgakelpelM 177
Cdd:COG3845 328 RER---RRLGVAYIPEDRLGR--------------------------------GLVPD---------------------M 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 178 TeakkaLTEAGVSGEAFDKAVARFTneWVpgsetRWRVADDLikagvADDLIKAgvaddqawylakkyvtgstMDDRIAG 257
Cdd:COG3845 352 S-----VAENLILGRYRRPPFSRGG--FL-----DRKAIRAF-----AEELIEE-------------------FDVRTPG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 llseaglPDAATRArqfpheFSGGMRQRALIAIGLACRPDLLIADEPTSALDV----TVQKRILDhlhmLTDSlGTAVLF 333
Cdd:COG3845 396 -------PDTPARS------LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaieFIHQRLLE----LRDA-GAAVLL 457
|
330 340 350
....*....|....*....|....*....|....*
gi 2545376782 334 ITHDLG--LA-AERaqhIVVMYKGQVVESGPSLEV 365
Cdd:COG3845 458 ISEDLDeiLAlSDR---IAVMYEGRIVGEVPAAEA 489
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
439-657 |
2.52e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.18 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTvanmvlhLLK-------PTSGKVFYEGRdtstfkskdllgfrrhvQPVFQNP 511
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKST-------LLKilsgnyqPDAGSILIDGQ-----------------EMRFAST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 512 YGSLDPMYSIFR---------SIEEPLRI----HKIG--DKKWRANRVKELLDMVEM---PASVMGRypneLSGGQRQRI 573
Cdd:PRK11288 74 TAALAAGVAIIYqelhlvpemTVAENLYLgqlpHKGGivNRRLLNYEAREQLEHLGVdidPDTPLKY----LSIGQRQMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 574 AIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVF 653
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQV 228
|
....
gi 2545376782 654 DHPQ 657
Cdd:PRK11288 229 DRDQ 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
208-370 |
3.10e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.76 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 208 GSETRWRVADdliKAGVA-----DDLIKAGVADDQAWYLAKKYVTGSTMDDRIAGLLSEAGLPDAATRArqfPHEFSGGM 282
Cdd:PRK13640 75 TAKTVWDIRE---KVGIVfqnpdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSE---PANLSGGQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 283 RQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGlAAERAQHIVVMYKGQVVESGPS 362
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSP 227
|
....*...
gi 2545376782 363 LEVLQHPQ 370
Cdd:PRK13640 228 VEIFSKVE 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-358 |
3.12e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.05 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDtGKPVHAVRDANFTVYPGQWVAIVGESGSGKST--SAMAvlGLLPGTGhvvnGSIKLDGEEIAGA 95
Cdd:COG4525 2 SMLTVRHVSVRYPGG-GQPQPALQDVSLTIESGEFVVALGASGCGKTTllNLIA--GFLAPSS----GEITLDGVPVTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 96 kqsefdklrGTKMGLVPQdpmsnlnpvwrigtqvKEALkannmdvahekrsalakalagdevevkgnddetflgakeLPe 175
Cdd:COG4525 75 ---------GADRGVVFQ----------------KDAL---------------------------------------LP- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 176 lmteakkalteagvsgeafdkavarftnewvpgsetrWR-VADDlikagVADDLIKAGVADDQAwylakkyvtgstmdDR 254
Cdd:COG4525 90 -------------------------------------WLnVLDN-----VAFGLRLRGVPKAER--------------RA 113
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 255 IAG-LLSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLF 333
Cdd:COG4525 114 RAEeLLALVGLADFARR---RIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFL 190
|
330 340
....*....|....*....|....*..
gi 2545376782 334 ITHDLGLAAERAQHIVVM--YKGQVVE 358
Cdd:COG4525 191 ITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
416-650 |
3.38e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.82 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKEFklprkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVanM-VLHLLKPT---SGKVFYEG----- 486
Cdd:PRK13549 2 MEYLLEMKNITKTF------GGVKALDNVSLKVRAGEIVSLCGENGAGKSTL--MkVLSGVYPHgtyEGEIIFEGeelqa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 487 ---RDTStfkskdllgfRRHVQPVFQNPygSLDPMYSIFRSI---EEPLRIHKIGDKKWRAnRVKELLDMVEMPASVMGR 560
Cdd:PRK13549 74 sniRDTE----------RAGIAIIHQEL--ALVKELSVLENIflgNEITPGGIMDYDAMYL-RAQKLLAQLKLDINPATP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 561 YPNeLSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAeKGLSYLFITHDLAVVRQIADEVVVMQH 640
Cdd:PRK13549 141 VGN-LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTICVIRD 218
|
250
....*....|
gi 2545376782 641 GKlveHATTD 650
Cdd:PRK13549 219 GR---HIGTR 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-351 |
3.49e-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: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTDT--GKPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEE---- 91
Cdd:COG4778 3 TLLEVENLSKTFTLHLqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKST----LLKCIYGNYLPDSGSILVRHDGgwvd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 92 IAGAKQSEFDKLRGTKMGLVPQdpmsnlnpvwrigtqvkealkannmdvahekrsalakalagdevevkgnddetFLgaK 171
Cdd:COG4778 79 LAQASPREILALRRRTIGYVSQ-----------------------------------------------------FL--R 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 172 ELPelmteakkalteagvsgeafdkavarftnewvpgsetrwRV-ADDLikagVADDLIKAGVADDQAwylakkyvtgst 250
Cdd:COG4778 104 VIP---------------------------------------RVsALDV----VAEPLLERGVDREEA------------ 128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 251 mDDRIAGLLSEAGLPDAATRArqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTA 330
Cdd:COG4778 129 -RARARELLARLNLPERLWDL--PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTA 204
|
330 340
....*....|....*....|.
gi 2545376782 331 VLFITHDLGLAAERAQHIVVM 351
Cdd:COG4778 205 IIGIFHDEEVREAVADRVVDV 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
271-367 |
4.94e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.50 E-value: 4.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 271 ARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDV--TVQkrILDHLHMLTDSLGTAVLFITHDLGLAAERAQHI 348
Cdd:COG4604 129 ADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhSVQ--MMKLLRRLADELGKTVVIVLHDINFASCYADHI 206
|
90
....*....|....*....
gi 2545376782 349 VVMYKGQVVESGPSLEVLQ 367
Cdd:COG4604 207 VAMKDGRVVAQGTPEEIIT 225
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
420-655 |
5.81e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 75.62 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKLPR--------------KKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYE 485
Cdd:PRK13546 5 VNIKNVTKEYRIYRtnkermkdalipkhKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 486 GrDTSTFKSKDLLGfrrhvqpvfqnpyGSLDPMYSI-FRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPAsvmgrypNE 564
Cdd:PRK13546 85 G-EVSVIAISAGLS-------------GQLTGIENIeFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPV-------KK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 565 LSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQaEKGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:PRK13546 144 YSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
250
....*....|.
gi 2545376782 645 EHATTDEVFDH 655
Cdd:PRK13546 223 DYGELDDVLPK 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
236-414 |
5.81e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.92 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 236 DQAWYLAK-KYVTGSTMDDRIAGLLSEAGLPDAATRARQfphEFSGGMRQRALIAIGLACRPDLLIADEPTSALD-VTVQ 313
Cdd:COG4152 90 EQLVYLARlKGLSKAEAKRRADEWLERLGLGDRANKKVE---ELSKGNQQKVQLIAALLHDPELLILDEPFSGLDpVNVE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 314 KrILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVL-QHPQHPYTKRLVAAAPSLASQ-RIIS 391
Cdd:COG4152 167 L-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRrQFGRNTLRLEADGDAGWLRALpGVTV 244
|
170 180
....*....|....*....|...
gi 2545376782 392 AKERGEDADALLDHHIAGESTLE 414
Cdd:COG4152 245 VEEDGDGAELKLEDGADAQELLR 267
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
246-360 |
6.22e-15 |
|
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: 74.33 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 246 VTGSTMDDRIAGLLSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTD 325
Cdd:cd03265 103 VPGAERRERIDELLDFVGLLEAADR---LVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKE 179
|
90 100 110
....*....|....*....|....*....|....*
gi 2545376782 326 SLGTAVLFITHDLGLAAERAQHIVVMYKGQVVESG 360
Cdd:cd03265 180 EFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
424-655 |
7.49e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 78.01 E-value: 7.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 424 HLTKEFKLPRK-----KEMFK---------AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGrdt 489
Cdd:PRK13545 9 HVTKKYKMYNKpfdklKDLFFrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 490 stfkSKDLLGFRrhvqpvfqnpyGSLDPMYSIFRSIEepLRIHKIGDKKwraNRVKELLDMVEMPASVmGRYPNE----L 565
Cdd:PRK13545 86 ----SAALIAIS-----------SGLNGQLTGIENIE--LKGLMMGLTK---EKIKEIIPEIIEFADI-GKFIYQpvktY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 566 SGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQaEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVE 645
Cdd:PRK13545 145 SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFK-EQGKTIFFISHSLSQVKSFCTKALWLHYGQVKE 223
|
250
....*....|
gi 2545376782 646 HATTDEVFDH 655
Cdd:PRK13545 224 YGDIKEVVDH 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
250-351 |
7.59e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.42 E-value: 7.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 250 TMDDR--IAGLLSEAGLPDAATRARQfphEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSl 327
Cdd:NF040873 93 TRDDRaaVDDALERVGLADLAGRQLG---ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHAR- 168
|
90 100
....*....|....*....|....
gi 2545376782 328 GTAVLFITHDLGLAAeRAQHIVVM 351
Cdd:NF040873 169 GATVVVVTHDLELVR-RADPCVLL 191
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
233-375 |
7.70e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 7.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 233 VADDQAWYLAKKYVTGSTMDDRIAGLLSEAGLPDaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTV 312
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLEN---YAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 313 QKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTK 375
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
277-378 |
7.70e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.95 E-value: 7.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLgtAVLFITHDLGLAAERAQHIVVMYKGQV 356
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQI 223
|
90 100
....*....|....*....|..
gi 2545376782 357 VESGPSLEVLQHPQHPYTKRLV 378
Cdd:PRK14247 224 VEWGPTREVFTNPRHELTEKYV 245
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
39-351 |
8.28e-15 |
|
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: 77.71 E-value: 8.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 39 AVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAKQsefDKLRGTkMGLVPQDPmsn 118
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE----GSIAVNGVPLADADA---DSWRDQ-IAWVPQHP--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 119 lnpvwrigtQVKEALKANNMdvahekrsALAKALAGDEvevkgnddetflgakelpelmtEAKKALTEAGvsgeafdkav 198
Cdd:TIGR02857 406 ---------FLFAGTIAENI--------RLARPDASDA----------------------EIREALERAG---------- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 199 arftnewvpgsetrwrvaddlikagvADDLIKAgvaddqawylakkyvtgstmddRIAGLLSEAGlpdaatrarQFPHEF 278
Cdd:TIGR02857 437 --------------------------LDEFVAA----------------------LPQGLDTPIG---------EGGAGL 459
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDslGTAVLFITHDLGLaAERAQHIVVM 351
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLAL-AALADRIVVL 529
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-370 |
8.99e-15 |
|
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: 74.25 E-value: 8.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLaidfttDTG-KPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAK 96
Cdd:COG0410 2 PMLEVENL------HAGyGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRS----GSIRFDGEDITGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 97 QSEFDKlRGtkMGLVPQD-----PMSnlnpvwrigtqVKEALKannmdvahekrsaLAKALAGDEVEVKGNDDETFlgak 171
Cdd:COG0410 72 PHRIAR-LG--IGYVPEGrrifpSLT-----------VEENLL-------------LGAYARRDRAEVRADLERVY---- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 172 EL-PELmteakkalteagvsgeafdkavarftnewvpgsETRWRvaddlikagvaddlikagvaddqawylakkyvtgst 250
Cdd:COG0410 121 ELfPRL---------------------------------KERRR------------------------------------ 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 251 mddRIAGLLSeaglpdaatrarqfphefsGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTA 330
Cdd:COG0410 132 ---QRAGTLS-------------------GGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVT 188
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2545376782 331 VLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQ 370
Cdd:COG0410 189 ILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
34-364 |
1.37e-14 |
|
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: 73.31 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 34 GKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIagakQSEFDKLRGtKMGLVPQ 113
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS----GTAYINGYSI----RTDRKAARQ-SLGYCPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 114 DpmsnlnpvwrigtqvkealkannmDVahekrsalakalagdevevkgnddetflgakeLPELMTeakkalteagvsgea 193
Cdd:cd03263 83 F------------------------DA--------------------------------LFDELT--------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 194 fdkavarftnewvpgsetrwrvaddlikagVADDLikagvaddqaWYLAK-KYVTGSTMDDRIAGLLSEAGLPDAATRar 272
Cdd:cd03263 92 ------------------------------VREHL----------RFYARlKGLPKSEIKEEVELLLRVLGLTDKANK-- 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 273 qFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDslGTAVLFITHDLGLAAERAQHIVVMY 352
Cdd:cd03263 130 -RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMS 206
|
330
....*....|..
gi 2545376782 353 KGQVVESGPSLE 364
Cdd:cd03263 207 DGKLRCIGSPQE 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
443-662 |
1.49e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.76 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVL---------HLLKPT----------------------------------- 478
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhHIVFKNehtndmtneqdyqgdeeqnvgmknvnefsltkegg 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 479 ----------SGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPYgsLDPMySIFRSIEEPLRIHKIGDKKwRANRVKELL 548
Cdd:PTZ00265 1266 sgedstvfknSGKILLDGVDICDYNLKDL---RNLFSIVSQEPM--LFNM-SIYENIKFGKEDATREDVK-RACKFAAID 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 549 DMVE-MPASV---MGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHD 624
Cdd:PTZ00265 1339 EFIEsLPNKYdtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR 1418
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2545376782 625 LAVVRQiADEVVVMQH----GKLVE-HATTDEVF---DHPQKQYTR 662
Cdd:PTZ00265 1419 IASIKR-SDKIVVFNNpdrtGSFVQaHGTHEELLsvqDGVYKKYVK 1463
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
443-645 |
1.98e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.52 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVL-H-LLKPTSGKVFYEGRDTSTFKSKDllgfRRH--VQPVFQNP------- 511
Cdd:CHL00131 25 GLNLSINKGEIHAIMGPNGSGKSTLSKVIAgHpAYKILEGDILFKGESILDLEPEE----RAHlgIFLAFQYPieipgvs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 512 --------YGSldpmYSIFRSIEE--PLRIHKIgdkkwranrVKELLDMVEMPASVMGRYPNE-LSGGQRQRIAIARAMA 580
Cdd:CHL00131 101 nadflrlaYNS----KRKFQGLPEldPLEFLEI---------INEKLKLVGMDPSFLSRNVNEgFSGGEKKRNEILQMAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 581 LDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIA-DEVVVMQHGKLVE 645
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIK 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
277-637 |
1.99e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLACRPDLLIADEPTSALDV----TVQKRILDhlhmLTDslGTAVLFITHDLGLAAERAQHIVVMY 352
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIrqrlNVARLIRE----LAE--GKYVLVVEHDLAVLDYLADNVHIAY 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 353 kGQ-----VVesgpslevlqhpQHPYTKRlvaaapslasqriisakergEDADALLDHHIAGESTLEKSEHIITVDH-LT 426
Cdd:PRK13409 286 -GEpgaygVV------------SKPKGVR--------------------VGINEYLKGYLPEENMRIRPEPIEFEERpPR 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 427 KEFKLPRKKE---MFKAVDDVSFSVKRGT-----TLAIVGESGSGKSTVANMVLHLLKPTSGKVF--------------- 483
Cdd:PRK13409 333 DESERETLVEypdLTKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpelkisykpqyikpd 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 484 YEGRdtstfkSKDLLgfrRHVQPVFQNPYgsldpmysiFRS-IEEPLRIHKIgdkkwranrvkelldmvempasvMGRYP 562
Cdd:PRK13409 413 YDGT------VEDLL---RSITDDLGSSY---------YKSeIIKPLQLERL-----------------------LDKNV 451
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 563 NELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVV 637
Cdd:PRK13409 452 KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-362 |
2.02e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.97 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFTTDTGkpVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLpgtgHVVNGSIKLDGEEIAGAKQS 98
Cdd:PRK13642 4 ILEVENLVFKYEKESD--VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLF----EEFEGKVKIDGELLTAENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 99 EFDKlrgtKMGLVPQDPmsnlnpvwrigtqvkealkannmdvahekrsalakalagdevevkgndDETFLGAKelpelmt 178
Cdd:PRK13642 78 NLRR----KIGMVFQNP------------------------------------------------DNQFVGAT------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 179 eakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagVADDQAWYLAKKYVTGSTMDDRIAGL 258
Cdd:PRK13642 99 ------------------------------------------------------VEDDVAFGMENQGIPREEMIKRVDEA 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 LSEAGLPDAATRArqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDL 338
Cdd:PRK13642 125 LLAVNMLDFKTRE---PARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDL 201
|
330 340
....*....|....*....|....*
gi 2545376782 339 GLAAErAQHIVVMYKGQVV-ESGPS 362
Cdd:PRK13642 202 DEAAS-SDRILVMKAGEIIkEAAPS 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-356 |
2.41e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.00 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFTTDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEIAgaKQS 98
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYT--LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE----SGQIIIDGDLLT--EEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 99 EFDKLRgtKMGLVPQDPmsnlnpvwrigtqvkealkannmdvahekrsalakalagdevevkgndDETFLGAKelpelmt 178
Cdd:PRK13650 76 VWDIRH--KIGMVFQNP------------------------------------------------DNQFVGAT------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 179 eakkalteagvsgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagVADDQAWYLAKKYVTGSTMDDRIAGL 258
Cdd:PRK13650 99 ------------------------------------------------------VEDDVAFGLENKGIPHEEMKERVNEA 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 LSEAGLPDAATRArqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDL 338
Cdd:PRK13650 125 LELVGMQDFKERE---PARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDL 201
|
330
....*....|....*...
gi 2545376782 339 GLAAeRAQHIVVMYKGQV 356
Cdd:PRK13650 202 DEVA-LSDRVLVMKNGQV 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
277-360 |
2.82e-14 |
|
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: 72.40 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDsLGTAVLFITHDLGLAAERAQHIVVMYKGQV 356
Cdd:cd03266 136 GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
....
gi 2545376782 357 VESG 360
Cdd:cd03266 215 VYEG 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
31-365 |
2.92e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.58 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 31 TDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSA--MAVLgLLPGTGHV-VNGSIKLDGEEIAGAKQsefdklrgtK 107
Cdd:PRK13633 17 NEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAkhMNAL-LIPSEGKVyVDGLDTSDEENLWDIRN---------K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 108 MGLVPQDPMSNLnpvwrIGTQVKEalkannmDVAhekrsalakalagdevevkgnddetfLGakelPElmteakkaltea 187
Cdd:PRK13633 87 AGMVFQNPDNQI-----VATIVEE-------DVA--------------------------FG----PE------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 188 gvsgeafdkavarftNEWVPGSETRWRVADDLIKAGVaddlikagvaddqawYLAKKYVtgstmddriagllseaglpda 267
Cdd:PRK13633 113 ---------------NLGIPPEEIRERVDESLKKVGM---------------YEYRRHA--------------------- 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 268 atrarqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAErAQH 347
Cdd:PRK13633 142 -------PHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADR 213
|
330
....*....|....*...
gi 2545376782 348 IVVMYKGQVVESGPSLEV 365
Cdd:PRK13633 214 IIVMDSGKVVMEGTPKEI 231
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
245-357 |
4.70e-14 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 71.97 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 245 YVTGSTMDDRIAGLLSEAGLPDaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLT 324
Cdd:TIGR02982 112 NLSYQEARERARAMLEAVGLGD---HLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLA 188
|
90 100 110
....*....|....*....|....*....|....*.
gi 2545376782 325 DSLGTAVLFITHD---LGLaaerAQHIVVMYKGQVV 357
Cdd:TIGR02982 189 KEQGCTILMVTHDnriLDV----ADRILQMEDGKLL 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
27-367 |
4.94e-14 |
|
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: 71.87 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 27 IDFTTDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIagaKQSEFDKLRgT 106
Cdd:cd03254 8 VNFSYDEKKPV--LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQK----GQILIDGIDI---RDISRKSLR-S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 107 KMGLVPQDPmsnlnpvWRIGTQVKEALKANNMDvahekrsalakalagdevevkgNDDEtflgakelpelmtEAKKALTE 186
Cdd:cd03254 78 MIGVVLQDT-------FLFSGTIMENIRLGRPN----------------------ATDE-------------EVIEAAKE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 187 AGvsgeafdkavarftnewvpgsetrwrvADDLIKagvaddlikagvaddqawYLAKKYVTgstmddriagLLSEAGlpd 266
Cdd:cd03254 116 AG---------------------------AHDFIM------------------KLPNGYDT----------VLGENG--- 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 267 aatrarqfpHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDslGTAVLFITHDLGlAAERAQ 346
Cdd:cd03254 138 ---------GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNAD 205
|
330 340
....*....|....*....|.
gi 2545376782 347 HIVVMYKGQVVESGPSLEVLQ 367
Cdd:cd03254 206 KILVLDDGKIIEEGTHDELLA 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
271-365 |
5.98e-14 |
|
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: 71.73 E-value: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 271 ARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVV 350
Cdd:TIGR01184 108 ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVM 187
|
90
....*....|....*
gi 2545376782 351 MYKGQVVESGPSLEV 365
Cdd:TIGR01184 188 LTNGPAANIGQILEV 202
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
277-367 |
6.21e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 72.35 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKGQV 356
Cdd:PRK11231 138 DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
90
....*....|.
gi 2545376782 357 VESGPSLEVLQ 367
Cdd:PRK11231 217 MAQGTPEEVMT 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
439-657 |
6.57e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.07 E-value: 6.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfrrhvqpvfqnpygSLDPM 518
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKL----------------YLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 519 YSIfrSIEEPLRIH---KIGDKKWRANRVKelldmvempASVMGRYP-NELSGGQRQRIAIARAMALDPDVIVCDEAVSA 594
Cdd:PRK09544 82 LPL--TVNRFLRLRpgtKKEDILPALKRVQ---------AGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 595 LDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHgKLVEHATTDEVFDHPQ 657
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHPE 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
247-369 |
7.32e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.58 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 247 TGSTMDDRIAGLLSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDS 326
Cdd:PRK10851 109 NAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEE 185
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2545376782 327 LGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHP 369
Cdd:PRK10851 186 LKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
441-641 |
9.00e-14 |
|
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: 70.82 E-value: 9.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLGFRRHvqPVfqnPYGSLDPmYS 520
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRY--SV---AYAAQKP-WL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 521 IFRSIEEPLRIHKIGDKKwranRVKELLDMVEMPASV----------MGRYPNELSGGQRQRIAIARAMALDPDVIVCDE 590
Cdd:cd03290 91 LNATVEENITFGSPFNKQ----RYKAVTDACSLQPDIdllpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 591 AVSALDVLVQDQVLR--LLNDLQAEKgLSYLFITHDLAVVRQiADEVVVMQHG 641
Cdd:cd03290 167 PFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-370 |
9.66e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.03 E-value: 9.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFTTDTgkpvHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEIAGAKQS 98
Cdd:PRK13639 1 ILETRDLKYSYPDGT----EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPT----SGEVLIKGEPIKYDKKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 99 EFdKLRgTKMGLVPQDPMSNLnpvwrIGTQVKEalkannmDVAHekrSALAKALAGDEVEvkgnddetflgakelpelmT 178
Cdd:PRK13639 73 LL-EVR-KTVGIVFQNPDDQL-----FAPTVEE-------DVAF---GPLNLGLSKEEVE-------------------K 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 179 EAKKALTEAGVSGeaFDKAVarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmddriagl 258
Cdd:PRK13639 117 RVKEALKAVGMEG--FENKP------------------------------------------------------------ 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 lseaglpdaatrarqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDL 338
Cdd:PRK13639 135 ----------------PHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDV 197
|
330 340 350
....*....|....*....|....*....|..
gi 2545376782 339 GLAAERAQHIVVMYKGQVVESGPSLEVLQHPQ 370
Cdd:PRK13639 198 DLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-369 |
1.22e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFTTDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIagakqS 98
Cdd:TIGR00958 478 LIEFQDVSFSYPNRPDVPV--LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG----GQVLLDGVPL-----V 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 99 EFD-KLRGTKMGLVPQDPMsnlnpVWRigtqvkealkannmdvahekRSALAKALAGdevevkgnddetfLGAKELPELM 177
Cdd:TIGR00958 547 QYDhHYLHRQVALVGQEPV-----LFS--------------------GSVRENIAYG-------------LTDTPDEEIM 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 178 TEAKKALteagvsgeafdkavarftnewvpgsetrwrvaddlikagvADDLIkagvaddqawylakkyvtgSTMDDRIAG 257
Cdd:TIGR00958 589 AAAKAAN----------------------------------------AHDFI-------------------MEFPNGYDT 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 LLSEAGlpdaatrarqfpHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRildhLHMLTDSLGTAVLFITHD 337
Cdd:TIGR00958 610 EVGEKG------------SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL----LQESRSRASRTVLLIAHR 673
|
330 340 350
....*....|....*....|....*....|..
gi 2545376782 338 LGLaAERAQHIVVMYKGQVVESGPSLEVLQHP 369
Cdd:TIGR00958 674 LST-VERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
436-637 |
1.23e-13 |
|
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: 71.29 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 436 EMFKAVDDVSFSVKRGT-----TLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStFKSKdllgfrrHVQPVFQn 510
Cdd:cd03237 5 TMKKTLGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQ-------YIKADYE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 511 pyGSLDPM-YSIFRSIEEplrihkigDKKWRANRVKELldMVEmpaSVMGRYPNELSGGQRQRIAIARAMALDPDVIVCD 589
Cdd:cd03237 76 --GTVRDLlSSITKDFYT--------HPYFKTEIAKPL--QIE---QILDREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2545376782 590 EAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVV 637
Cdd:cd03237 141 EPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
252-412 |
1.55e-13 |
|
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: 71.65 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 252 DDRIAGLLSEAGLPDAATR-ARQFphefSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTA 330
Cdd:TIGR01188 102 EERAEELLELFELGEAADRpVGTY----SGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRALKEE-GVT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 331 VLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVlqhpQHPYTKRLVAAAPSLASQRiisAKERGEDADALLDHHIAGE 410
Cdd:TIGR01188 177 ILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL----KRRLGKDTLESRPRDIQSL---KVEVSMLIAELGETGLGLL 249
|
..
gi 2545376782 411 ST 412
Cdd:TIGR01188 250 AV 251
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-378 |
1.92e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 70.84 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 9 MLAMQKEHGPLLEVKDLAIDFTTDtgkpvHAVRDANFTVYPGQWVAIVGESGSGKSTsamavlgLL----------PGTG 78
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDK-----QALKDINLDIPENKVTALIGPSGCGKST-------LLrclnrmndliPGAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 79 hvVNGSIKLDGEEIAgAKQSEFDKLRgTKMGLVPQDPmsnlNP----VWRigtqvkealkanNmdVA-----HEKRSala 149
Cdd:COG1117 69 --VEGEILLDGEDIY-DPDVDVVELR-RRVGMVFQKP----NPfpksIYD------------N--VAyglrlHGIKS--- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 150 KALAGDEVEvkgnddetflgakelpelmteakKALTEAGVsgeafdkavarftnewvpgsetrWrvaDDlikagVADDLi 229
Cdd:COG1117 124 KSELDEIVE-----------------------ESLRKAAL-----------------------W---DE-----VKDRL- 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 230 kagvaDDQAwylakkyvtgstmddriagllseAGLpdaatrarqfphefSGGMRQRALIAIGLACRPDLLIADEPTSALD 309
Cdd:COG1117 149 -----KKSA-----------------------LGL--------------SGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 310 VTVQKRILDHLHMLTDSLgtAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRLV 378
Cdd:COG1117 187 PISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
219-366 |
1.94e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.66 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 219 LIKAGVADDLI----KAGVADDQAWYLAKKYVtgstmddRIAGLlSEAGLPDAatrarqfPHEFSGGMRQRALIAIGLAC 294
Cdd:PRK13651 118 LFEQTIEKDIIfgpvSMGVSKEEAKKRAAKYI-------ELVGL-DESYLQRS-------PFELSGGQKRRVALAGILAM 182
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 295 RPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVL 366
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
279-366 |
2.91e-13 |
|
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: 69.82 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDslGTAVLFITHDLGlAAERAQHIVVMYKGQVVE 358
Cdd:cd03252 140 SGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVE 216
|
....*...
gi 2545376782 359 SGPSLEVL 366
Cdd:cd03252 217 QGSHDELL 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
226-363 |
3.18e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 226 DDLIKAGVADDQAWYLAKKYVTGSTMDDRIAGLLSEAGLPDAATRArqfPHEFSGGMRQRALIAIGLACRPDLLIADEPT 305
Cdd:PRK13647 90 DQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKP---PYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 306 SALDVTVQK---RILDHLHmltdSLGTAVLFITHDLGLAAERAQHIVVMYKGQVV-ESGPSL 363
Cdd:PRK13647 167 AYLDPRGQEtlmEILDRLH----NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLaEGDKSL 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
419-662 |
3.39e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFklprkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLL---KPTSGKVFYEGRDTSTFK-- 493
Cdd:PRK09984 4 IIRVEKLAKTF------NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 494 SKDLLGFRRHVQPVFQNpYGSLDPMysifrSIEEPLRIHKIGDKK-WRA----------NRVKELLDMVEMPASVMGRYp 562
Cdd:PRK09984 78 ARDIRKSRANTGYIFQQ-FNLVNRL-----SVLENVLIGALGSTPfWRTcfswftreqkQRALQALTRVGMVHFAHQRV- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 563 NELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGK 642
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
250 260
....*....|....*....|....
gi 2545376782 643 LV----EHATTDEVFDHPQKQYTR 662
Cdd:PRK09984 231 VFydgsSQQFDNERFDHLYRSINR 254
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
279-367 |
4.21e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.82 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVE 358
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
....*....
gi 2545376782 359 SGPSLEVLQ 367
Cdd:PRK10575 229 QGTPAELMR 237
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
439-652 |
4.89e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.74 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANmVLHLLKPT---SGKVFYEGrDTSTFKS-KDllgfRRHVQPVFQNPYGS 514
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMK-VLSGVYPHgsyEGEILFDG-EVCRFKDiRD----SEALGIVIIHQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 515 LDPMYSIFRSI---EEPLRiHKIGDkkWRA--NRVKELLDMV---EMPASVMGrypnELSGGQRQRIAIARAMALDPDVI 586
Cdd:NF040905 89 LIPYLSIAENIflgNERAK-RGVID--WNEtnRRARELLAKVgldESPDTLVT----DIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 587 VCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKLVE--HATTDEV 652
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIEtlDCRADEV 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
252-350 |
5.57e-13 |
|
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: 68.27 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 252 DDRIAGLLSEAGLPDaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAV 331
Cdd:COG4133 109 REAIDEALEAVGLAG---LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAV 184
|
90
....*....|....*....
gi 2545376782 332 LFITHDLgLAAERAQHIVV 350
Cdd:COG4133 185 LLTTHQP-LELAAARVLDL 202
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
20-114 |
5.75e-13 |
|
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: 67.63 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDlaIDFTT-DTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAKQS 98
Cdd:cd03246 1 LEVEN--VSFRYpGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTS----GRVRLDGADISQWDPN 72
|
90
....*....|....*.
gi 2545376782 99 EFdklrGTKMGLVPQD 114
Cdd:cd03246 73 EL----GDHVGYLPQD 84
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
253-373 |
7.31e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.29 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 DRIAGLLseaGLPDAATRarqFPHEFSGGMRQRalIAIG--LACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTA 330
Cdd:PRK11144 110 DKIVALL---GIEPLLDR---YPGSLSGGEKQR--VAIGraLLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIP 181
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2545376782 331 VLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQ-HPY 373
Cdd:PRK11144 182 ILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRPW 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
419-650 |
7.70e-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: 71.39 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 419 IITVDHLTKEFklprkkEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANmVLHLLKPT---SGKVFYEGRDTSTFKSK 495
Cdd:TIGR02633 1 LLEMKGIVKTF------GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHgtwDGEIYWSGSPLKASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 496 DLLgfRRHVQPVFQNPygSLDPMYSIFRSIeepLRIHKIGDKKWRAN------RVKELLDMVEMPASVMGRYPNELSGGQ 569
Cdd:TIGR02633 74 DTE--RAGIVIIHQEL--TLVPELSVAENI---FLGNEITLPGGRMAynamylRAKNLLRELQLDADNVTRPVGDYGGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 570 RQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAeKGLSYLFITHDLAVVRQIADEVVVMQHGKLVehATT 649
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHV--ATK 223
|
.
gi 2545376782 650 D 650
Cdd:TIGR02633 224 D 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
246-357 |
8.34e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.36 E-value: 8.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 246 VTGSTMDD---RIAGLLSEAGLPDaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILdHLHM 322
Cdd:PRK10908 106 IAGASGDDirrRVSAALDKVGLLD---KAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL-RLFE 181
|
90 100 110
....*....|....*....|....*....|....*
gi 2545376782 323 LTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVV 357
Cdd:PRK10908 182 EFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
212-356 |
8.53e-13 |
|
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: 67.07 E-value: 8.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 212 RWRVADDLIKAGVADDLIKAGVAddqawylakkYVTGstmdDRIA-GLLSEAGLPDAATrarqFPHEFSGGMRQRALIAI 290
Cdd:cd03215 56 EITLDGKPVTRRSPRDAIRAGIA----------YVPE----DRKReGLVLDLSVAENIA----LSSLLSGGNQQKVVLAR 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 291 GLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKGQV 356
Cdd:cd03215 118 WLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-338 |
8.99e-13 |
|
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: 71.24 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 17 GPLLEVKDLAidFTTDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAK 96
Cdd:TIGR02868 332 KPTLELRDLS--AGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ----GEVTLDGVPVSSLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 97 QSEFDKLrgtkMGLVPQDPMSnlnpvwrIGTQVKEALkannmdvahekrsALAKALAGDEvevkgnddetflgakelpel 176
Cdd:TIGR02868 404 QDEVRRR----VSVCAQDAHL-------FDTTVRENL-------------RLARPDATDE-------------------- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 177 mtEAKKALTeagvsgeafdkavarftnewvpgsetrwrvaddliKAGVADDLikagvaddqawylakkyvtgstmDDRIA 256
Cdd:TIGR02868 440 --ELWAALE-----------------------------------RVGLADWL-----------------------RALPD 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 257 GLLSEAGlPDAATrarqfpheFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDslGTAVLFITH 336
Cdd:TIGR02868 460 GLDTVLG-EGGAR--------LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITH 528
|
..
gi 2545376782 337 DL 338
Cdd:TIGR02868 529 HL 530
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
422-643 |
9.32e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.25 E-value: 9.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 422 VDHLTKEFKlprKKEMFkavDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLGFR 501
Cdd:COG0488 1 LENLSKSFG---GRPLL---DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 502 RHvqPVFQNPYGSLDPMYSIFRSIEE-----------PLRIHKIGDKK-----WRA-NRVKELLDMVEMPASVMGRYPNE 564
Cdd:COG0488 75 DL--TVLDTVLDGDAELRALEAELEEleaklaepdedLERLAELQEEFealggWEAeARAEEILSGLGFPEEDLDRPVSE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 565 LSGGQRQRIAIARAMALDPDVIVCDEAVSALDVlvqDQVLRLLNDLQAEKGlSYLFITHDLAVVRQIADEVVVMQHGKL 643
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDL---ESIEWLEEFLKNYPG-TVLVVSHDRYFLDRVATRILELDRGKL 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
444-662 |
1.55e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.16 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 444 VSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPYgsldpMYS-IF 522
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL---RRVLSIIPQSPV-----LFSgTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 523 RSIEEPLRIHKIGDkKWRANRVKELLDMVE-----MPASVMGRYPNeLSGGQRQRIAIARAMALDPDVIVCDEAVSALDV 597
Cdd:PLN03232 1327 RFNIDPFSEHNDAD-LWEALERAHIKDVIDrnpfgLDAEVSEGGEN-FSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 598 LVQDQVLRLLNdlQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDEVFDHPQKQYTR 662
Cdd:PLN03232 1405 RTDSLIQRTIR--EEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFR 1466
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
251-636 |
1.58e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.75 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 251 MDDRIAGLLSEAGL-PDAATRarqfphEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVqkriLDHLHMLTDSLGT 329
Cdd:PRK11147 135 LENRINEVLAQLGLdPDAALS------SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 330 AVLFITHDLGLAAERAQHIVVMYKGQVVeSGPS--------------LEVLQHPQhpYTKRL----------VAAAPSLA 385
Cdd:PRK11147 205 SIIFISHDRSFIRNMATRIVDLDRGKLV-SYPGnydqyllekeealrVEELQNAE--FDRKLaqeevwirqgIKARRTRN 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 386 SQRIISAK----ERGEDADALLDHHIAGESTLEKSEHIITVDHLtkEFKLPRKkemfKAVDDVSFSVKRGTTLAIVGESG 461
Cdd:PRK11147 282 EGRVRALKalrrERSERREVMGTAKMQVEEASRSGKIVFEMENV--NYQIDGK----QLVKDFSAQVQRGDKIALIGPNG 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 462 SGKSTVANMVLHLLKPTSGKVfyegrdtstfkskdllgfrrHVQPVFQNPY-----GSLDPMYSIFRSIEEplrihkiGD 536
Cdd:PRK11147 356 CGKTTLLKLMLGQLQADSGRI--------------------HCGTKLEVAYfdqhrAELDPEKTVMDNLAE-------GK 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 537 KKWRANRVKE-----LLDMVEMPASVMgrYP-NELSGGQRQRIAIARaMALDP-DVIVCDEAVSALDVlvqdQVLRLLND 609
Cdd:PRK11147 409 QEVMVNGRPRhvlgyLQDFLFHPKRAM--TPvKALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDV----ETLELLEE 481
|
410 420
....*....|....*....|....*..
gi 2545376782 610 LQAEKGLSYLFITHDlavvRQIADEVV 636
Cdd:PRK11147 482 LLDSYQGTVLLVSHD----RQFVDNTV 504
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
240-360 |
1.86e-12 |
|
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: 66.83 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 240 YLAK-KYVTGSTMDDRIAGLLSEAGLPDAATRArqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILD 318
Cdd:cd03264 95 YIAWlKGIPSKEVKARVDEVLELVNLGDRAKKK---IGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRN 171
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2545376782 319 HLHMLtdSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVESG 360
Cdd:cd03264 172 LLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
258-356 |
2.21e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.15 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 258 LLSEAGLpdaATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHD 337
Cdd:PRK11629 129 MLAAVGL---EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD 205
|
90
....*....|....*....
gi 2545376782 338 LGLaAERAQHIVVMYKGQV 356
Cdd:PRK11629 206 LQL-AKRMSRQLEMRDGRL 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
251-366 |
2.46e-12 |
|
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: 67.42 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 251 MDDRIAGLLSEAGLpdAATRARQFpHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTA 330
Cdd:COG1119 119 QRERARELLELLGL--AHLADRPF-GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPT 195
|
90 100 110
....*....|....*....|....*....|....*.
gi 2545376782 331 VLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVL 366
Cdd:COG1119 196 LVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
228-356 |
2.99e-12 |
|
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: 66.28 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 228 LIKAGVADDQAWYLAKKYVTGSTMDDRIAGLLSEAGLPDaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSA 307
Cdd:cd03292 90 LPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSH---KHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2545376782 308 LDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKGQV 356
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
440-645 |
3.01e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.62 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfkSKDLLGFRRHVQPVFQNPYgsldpmy 519
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYRKLFSAVFTDFH------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 sifrsieepLRIHKIGDKKWRAN--RVKELLDMVEMPASVM---GRYPN-ELSGGQRQRIAIARAMALDPDVIVCDEAvs 593
Cdd:PRK10522 408 ---------LFDQLLGPEGKPANpaLVEKWLERLKMAHKLEledGRISNlKLSKGQKKRLALLLALAEERDILLLDEW-- 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 594 ALDvlvQDQVLR------LLNDLQaEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVE 645
Cdd:PRK10522 477 AAD---QDPHFRrefyqvLLPLLQ-EMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
253-358 |
3.08e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.73 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 DRIAGLLSEAGLpdaATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVL 332
Cdd:PRK10584 125 NGAKALLEQLGL---GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLI 201
|
90 100
....*....|....*....|....*.
gi 2545376782 333 FITHDLGLAAeRAQHIVVMYKGQVVE 358
Cdd:PRK10584 202 LVTHDLQLAA-RCDRRLRLVNGQLQE 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
449-638 |
3.19e-12 |
|
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: 69.43 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 449 KRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVfyeGRDTST------FKSKDLlgfrrhvQPVFQNPY-GSLdpmysi 521
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSWdevlkrFRGTEL-------QDYFKKLAnGEI------ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 522 fRSIEEPLRIHKIG--------------DKKWRANRVKELLDMvempASVMGRYPNELSGGQRQRIAIARAMALDPDVIV 587
Cdd:COG1245 161 -KVAHKPQYVDLIPkvfkgtvrellekvDERGKLDELAEKLGL----ENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2545376782 588 CDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVM 638
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
443-652 |
4.36e-12 |
|
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: 67.19 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDT----------STFKSKDLLGfrrhvqpVFQNPY 512
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISfssqfswimpGTIKENIIFG-------VSYDEY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 513 GsldpmysiFRSIEEPLRIHkigdkkwranrvKELLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAV 592
Cdd:cd03291 128 R--------YKSVVKACQLE------------EDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545376782 593 SALDVLVQDQVL-RLLNDLQAEKglSYLFITHDLAVVRqIADEVVVMQHGKLVEHATTDEV 652
Cdd:cd03291 188 GYLDVFTEKEIFeSCVCKLMANK--TRILVTSKMEHLK-KADKILILHEGSSYFYGTFSEL 245
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
441-623 |
4.36e-12 |
|
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: 69.39 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANmVLHLLKPTSGKVFYEGRDTSTFKskdllgfrrhvqpVFQNPYGSLdpmyS 520
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLTKPAKGKLFY-------------VPQRPYMTL----G 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 521 IFR-SIEEPLRIHKIGDKKWRANRVKELLDMV--------EMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEA 591
Cdd:TIGR00954 530 TLRdQIIYPDSSEDMKRRGLSDKDLEQILDNVqlthilerEGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 2545376782 592 VSALDVLVQDQVLRLLNdlqaEKGLSYLFITH 623
Cdd:TIGR00954 610 TSAVSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
430-651 |
4.40e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.31 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 430 KLPRKKEMFKAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKP---TSGKVFYEGRDTSTFKSKDLLGFRRHVQP 506
Cdd:TIGR00955 30 CFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 507 VFqnpyGSL----DPMYSIFrsieepLRIHKIGDKKWRANRVKELLDMVEM----------PASVMGrypneLSGGQRQR 572
Cdd:TIGR00955 110 FI----PTLtvreHLMFQAH------LRMPRRVTKKEKRERVDEVLQALGLrkcantrigvPGRVKG-----LSGGERKR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 573 IAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHD-LAVVRQIADEVVVMQHGKLVEHATTDE 651
Cdd:TIGR00955 175 LAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
444-652 |
4.42e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.49 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 444 VSFSVKRGTTLAIVGESGSGKSTVANMVLHLLkPTSGKVFYEGRDTSTFKSKDLLGFR----RHVQPVFQNP---YGSLD 516
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRaylsQQQTPPFAMPvfqYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 517 -----PMYSIFRSIEEPLRIHKIGDKkwranrvkelldmvempasvMGRYPNELSGGQRQRIAIARAM-----ALDPD-- 584
Cdd:PRK03695 94 qpdktRTEAVASALNEVAEALGLDDK--------------------LGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgq 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 585 VIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEV 652
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
275-365 |
4.95e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 66.99 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 275 PHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKG 354
Cdd:PRK13637 142 PFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKG 221
|
90
....*....|.
gi 2545376782 355 QVVESGPSLEV 365
Cdd:PRK13637 222 KCELQGTPREV 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
252-360 |
6.24e-12 |
|
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: 65.32 E-value: 6.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 252 DDRIAGLLSEAGLPDAATR-ARQFphefSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTA 330
Cdd:cd03268 104 KKRIDEVLDVVGLKDSAKKkVKGF----SLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GIT 178
|
90 100 110
....*....|....*....|....*....|
gi 2545376782 331 VLFITHDLGLAAERAQHIVVMYKGQVVESG 360
Cdd:cd03268 179 VLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
252-366 |
7.52e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.16 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 252 DDRIAGLLSEAGLPDAAtraRQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAV 331
Cdd:PRK10253 121 EEAVTKAMQATGITHLA---DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTL 197
|
90 100 110
....*....|....*....|....*....|....*
gi 2545376782 332 LFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVL 366
Cdd:PRK10253 198 AAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
448-638 |
7.91e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 448 VKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKvfYEGRDT-----STFKSKDLLG-FRR----HVQPVFQNPYGSLDP 517
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEPSwdevlKRFRGTELQNyFKKlyngEIKVVHKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 518 MYsiFR-SIEEPLRihKIgDKKWRANRVKELLDMvempASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALD 596
Cdd:PRK13409 174 KV--FKgKVRELLK--KV-DERGKLDEVVERLGL----ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2545376782 597 VLVQDQVLRLLNDLQAEKglSYLFITHDLAVVRQIADEVVVM 638
Cdd:PRK13409 245 IRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIA 284
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
277-370 |
8.37e-12 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 65.26 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGlAAERAQHIVVMYKGQV 356
Cdd:TIGR03771 113 ELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELAGA-GTAILMTTHDLA-QAMATCDRVVLLNGRV 190
|
90
....*....|....
gi 2545376782 357 VESGPSLEvLQHPQ 370
Cdd:TIGR03771 191 IADGTPQQ-LQDPA 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
254-434 |
8.71e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.57 E-value: 8.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 254 RIAGLLSEAGLPDaaTRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLF 333
Cdd:PRK13645 129 KVPELLKLVQLPE--DYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIM 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 334 ITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHpQHPYTKrlVAAAPSLASQRIISAKERGEDadaLLDHHIAgestl 413
Cdd:PRK13645 207 VTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN-QELLTK--IEIDPPKLYQLMYKLKNKGID---LLNKNIR----- 275
|
170 180
....*....|....*....|.
gi 2545376782 414 eksehiiTVDHLTKEFKLPRK 434
Cdd:PRK13645 276 -------TIEEFAKELAKVLK 289
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
271-378 |
1.20e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.89 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 271 ARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVV 350
Cdd:PRK09452 138 AQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVV 217
|
90 100
....*....|....*....|....*...
gi 2545376782 351 MYKGQVVESGPSLEVLQHPQHPYTKRLV 378
Cdd:PRK09452 218 MRDGRIEQDGTPREIYEEPKNLFVARFI 245
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
439-678 |
1.23e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 66.68 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVAnMVLHLLKPTSGKVFYEGRDTSTFKS--KDLLGFRRHVQPVFQNPYGSLD 516
Cdd:NF000106 27 KAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*TWCANRRalRRTIG*HRPVR*GRRESFSGRE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 517 PMYSIFRSIEEPLRihkigDKKWRANRVKELLDMVEmpasVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALD 596
Cdd:NF000106 106 NLYMIGR*LDLSRK-----DARARADELLERFSLTE----AAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 597 VLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVfdhPQKQYTRDL---------LDA 667
Cdd:NF000106 177 PRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL---KTKVGGRTLqirpahaaeLDR 252
|
250
....*....|.
gi 2545376782 668 IPGGKLQLGLD 678
Cdd:NF000106 253 MVGAIAQAGLD 263
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
277-366 |
1.34e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.79 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFItHDLGLAAERAQHIVVMYKGQV 356
Cdd:PRK09536 139 SLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRV 217
|
90
....*....|
gi 2545376782 357 VESGPSLEVL 366
Cdd:PRK09536 218 RAAGPPADVL 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
277-378 |
1.47e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.07 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLgtAVLFITHDLGLAAERAQHIVVMYKGQV 356
Cdd:PRK14246 153 QLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGEL 230
|
90 100
....*....|....*....|..
gi 2545376782 357 VESGPSLEVLQHPQHPYTKRLV 378
Cdd:PRK14246 231 VEWGSSNEIFTSPKNELTEKYV 252
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
278-368 |
1.83e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 64.72 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 278 FSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKGQVV 357
Cdd:COG1134 147 YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
90
....*....|.
gi 2545376782 358 ESGPSLEVLQH 368
Cdd:COG1134 226 MDGDPEEVIAA 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
277-652 |
1.87e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLAcRPDLLIA-DEPTSALDVtvqkRILDHLHMLTDSL---GTAVLFITHDLGLAAERAQHIVVMY 352
Cdd:PRK11288 140 YLSIGQRQMVEIAKALA-RNARVIAfDEPTSSLSA----REIEQLFRVIRELraeGRVILYVSHRMEEIFALCDAITVFK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 353 KGQVVESGPSLEVLQHPQhpytkrLVAAAPSLASQRIISAKERGedadalldhhiAGESTLEksehiitVDHLtkefKLP 432
Cdd:PRK11288 215 DGRYVATFDDMAQVDRDQ------LVQAMVGREIGDIYGYRPRP-----------LGEVRLR-------LDGL----KGP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 433 RKKEmfkavdDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGrdtstfkskdllgfrrhvQPV-FQNP 511
Cdd:PRK11288 267 GLRE------PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG------------------KPIdIRSP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 512 YGSLD----------------PMYSIFRSIEEPLRIHKIG-----DKKWRANRVKELLdmvempASVMGRYPN------E 564
Cdd:PRK11288 323 RDAIRagimlcpedrkaegiiPVHSVADNINISARRHHLRagcliNNRWEAENADRFI------RSLNIKTPSreqlimN 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 565 LSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
410
....*....|...
gi 2545376782 645 -----EHATTDEV 652
Cdd:PRK11288 476 gelarEQATERQA 488
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
443-653 |
2.10e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.50 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEgrdtstfkskdllgfrRHVQPVFQNPYgsldPMYSIF 522
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE----------------RSIAYVPQQAW----IMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 523 RS------IEEPLRIHKigdkkwrANRVKEL-LDMVEMPASV---MGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAV 592
Cdd:PTZ00243 738 RGnilffdEEDAARLAD-------AVRVSQLeADLAQLGGGLeteIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545376782 593 SALDVLVQDQVLRLLNdLQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKlVEHATTDEVF 653
Cdd:PTZ00243 811 SALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGR-VEFSGSSADF 868
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
444-651 |
2.39e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.46 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 444 VSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPYgsldpMYS-IF 522
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL---RKVLGIIPQAPV-----LFSgTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 523 RSIEEPLRIHKIGDKkWRANRVKELLDMVE-----MPASVMGRYPNeLSGGQRQRIAIARAMALDPDVIVCDEAVSALDV 597
Cdd:PLN03130 1330 RFNLDPFNEHNDADL-WESLERAHLKDVIRrnslgLDAEVSEAGEN-FSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 598 ----LVQdQVLRllndlQAEKGLSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDE 651
Cdd:PLN03130 1408 rtdaLIQ-KTIR-----EEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPEN 1458
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
37-373 |
2.75e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 65.48 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 37 VHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGAKQSEfdklRGTKMglVPQDP- 115
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTS----GEILIGGRDVTDLPPKD----RNIAM--VFQSYa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 116 ----MSnlnpvwrigtqVKEalkanNMdvahekrsalakalagdevevkgnddeTFlgakelpelmteakkALTEAGVSG 191
Cdd:COG3839 86 lyphMT-----------VYE-----NI---------------------------AF---------------PLKLRKVPK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 192 EAFDKAVARftnewvpgsetrwrvaddlikagVADDLikaGVADdqawYLAKKyvtgstmddriagllseaglpdaatra 271
Cdd:COG3839 108 AEIDRRVRE-----------------------AAELL---GLED----LLDRK--------------------------- 130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 272 rqfPHEFSGGMRQRalIAIG--LACRPDLLIADEPTSALDVT--VQKRI-LDHLHmltDSLGTAVLFITHD----LGLaa 342
Cdd:COG3839 131 ---PKQLSGGQRQR--VALGraLVREPKVFLLDEPLSNLDAKlrVEMRAeIKRLH---RRLGTTTIYVTHDqveaMTL-- 200
|
330 340 350
....*....|....*....|....*....|.
gi 2545376782 343 erAQHIVVMYKGQVVESGPSLEVLQHPQHPY 373
Cdd:COG3839 201 --ADRIAVMNDGRIQQVGTPEELYDRPANLF 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-357 |
3.28e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.34 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIDFTTDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEEIAgaKQSE 99
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKST----LLNAIAGSLPPDSGSILIDGKDVT--KLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 FDklRGTKMGLVPQDPMsnlnpvwrIGT----QVKEalkanNMDVA---HEKRSaLAKALagdevevkgnddetflgake 172
Cdd:COG1101 76 YK--RAKYIGRVFQDPM--------MGTapsmTIEE-----NLALAyrrGKRRG-LRRGL-------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 173 lpelmTEAKKALteagvsgeaFDKAVARFTNewvpGSETRwrvaddlikagvaddlikagvaddqawylakkyvtgstMD 252
Cdd:COG1101 120 -----TKKRREL---------FRELLATLGL----GLENR--------------------------------------LD 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 DRIaGLLSeaglpdaatrarqfphefsGGMRQrALiAIGLAC--RPDLLIADEPTSALDVTVQKRILDhlhmLTDSL--- 327
Cdd:COG1101 144 TKV-GLLS-------------------GGQRQ-AL-SLLMATltKPKLLLLDEHTAALDPKTAALVLE----LTEKIvee 197
|
330 340 350
....*....|....*....|....*....|.
gi 2545376782 328 -GTAVLFITHDLGLAAERAQHIVVMYKGQVV 357
Cdd:COG1101 198 nNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
273-360 |
3.81e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.42 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 273 QFPHEFSGG-MRQRALIAIgLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVM 351
Cdd:PRK13646 141 QSPFQMSGGqMRKIAIVSI-LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVM 219
|
....*....
gi 2545376782 352 YKGQVVESG 360
Cdd:PRK13646 220 KEGSIVSQT 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
251-643 |
3.91e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.80 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 251 MDDRIAGLLSEAGLPdaaTRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTA 330
Cdd:PRK10762 118 MYAEADKLLARLNLR---FSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRG 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 331 VLFITHDLGLAAERAQHIVVMYKGQVVesgpslevlqhpqhpyTKRLVAaapSLASQRIIS--AKERGEDADALLDHHiA 408
Cdd:PRK10762 194 IVYISHRLKEIFEICDDVTVFRDGQFI----------------AEREVA---DLTEDSLIEmmVGRKLEDQYPRLDKA-P 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 409 GESTLEksehiitVDHLTKEfklprkkemfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRD 488
Cdd:PRK10762 254 GEVRLK-------VDNLSGP-----------GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 489 TSTFKSKDLL--GFrrhvqpvfqnPYGSLDpmysifR---------SIEEPLRI-------HKIGDKKWRANR--VKELL 548
Cdd:PRK10762 316 VVTRSPQDGLanGI----------VYISED------RkrdglvlgmSVKENMSLtalryfsRAGGSLKHADEQqaVSDFI 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 549 DMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVV 628
Cdd:PRK10762 380 RLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEV 458
|
410
....*....|....*
gi 2545376782 629 RQIADEVVVMQHGKL 643
Cdd:PRK10762 459 LGMSDRILVMHEGRI 473
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
32-121 |
3.98e-11 |
|
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: 63.28 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 32 DTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIagakqSEFD--KLRgTKMG 109
Cdd:cd03244 14 PNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSS----GSILIDGVDI-----SKIGlhDLR-SRIS 81
|
90
....*....|....*....
gi 2545376782 110 LVPQDPM-------SNLNP 121
Cdd:cd03244 82 IIPQDPVlfsgtirSNLDP 100
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
443-641 |
4.16e-11 |
|
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: 66.47 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDT----------STFKSKDLLGFRrhvqpvfqnpy 512
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISfspqtswimpGTIKDNIIFGLS----------- 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 513 gsldpmYSIFR--------SIEEPLRIHKIGDKkwranrvkelldmvempaSVMGRYPNELSGGQRQRIAIARAMALDPD 584
Cdd:TIGR01271 513 ------YDEYRytsvikacQLEEDIALFPEKDK------------------TVLGEGGITLSGGQRARISLARAVYKDAD 568
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 585 VIVCDEAVSALDVLVQDQVL-RLLNDLQAEKglSYLFITHDLAVVRQiADEVVVMQHG 641
Cdd:TIGR01271 569 LYLLDSPFTHLDVVTEKEIFeSCLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
254-377 |
5.05e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 63.24 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 254 RIAGLLSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLF 333
Cdd:COG3840 109 QVEQALERVGLAGLLDR---LPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLM 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2545376782 334 ITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQHPYTKRL 377
Cdd:COG3840 186 VTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
377-645 |
5.67e-11 |
|
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: 65.59 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 377 LVAAAPSLAS-----QRI--ISAKERGEDADALLDHHIAGESTLEKsehiITVDHLTKEFKLPRKKEMFkAVDDVSFSVK 449
Cdd:COG4615 282 LVGALPTLSRanvalRKIeeLELALAAAEPAAADAAAPPAPADFQT----LELRGVTYRYPGEDGDEGF-TLGPIDLTIR 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 450 RGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfkSKDLLGFRRHVQPVFQNPYgsldpmysIFrsiEEPL 529
Cdd:COG4615 357 RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYRQLFSAVFSDFH--------LF---DRLL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 530 RIHKIGDkkwrANRVKELLDMVEMPASVM---GRYPN-ELSGGQRQRIAIARAMALDPDVIVCDEAvsALDvlvQDQVLR 605
Cdd:COG4615 423 GLDGEAD----PARARELLERLELDHKVSvedGRFSTtDLSQGQRKRLALLVALLEDRPILVFDEW--AAD---QDPEFR 493
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2545376782 606 ------LLNDLQAeKGLSYLFITHDlavVR--QIADEVVVMQHGKLVE 645
Cdd:COG4615 494 rvfyteLLPELKA-RGKTVIAISHD---DRyfDLADRVLKMDYGKLVE 537
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
15-152 |
6.33e-11 |
|
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: 62.43 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 15 EHGPLlEVKDLAIDFTTDTGKpvhAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLpgtgHVVNGSIKLDGEEIAG 94
Cdd:cd03369 3 EHGEI-EVENLSVRYAPDLPP---VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFL----EAEEGKIEIDGIDIST 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 95 AKqseFDKLRgTKMGLVPQDPM-------SNLNPVWRIG-TQVKEALK----ANNMDVAHEKRSALAKAL 152
Cdd:cd03369 75 IP---LEDLR-SSLTIIPQDPTlfsgtirSNLDPFDEYSdEEIYGALRvsegGLNLSQGQRQLLCLARAL 140
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-360 |
7.25e-11 |
|
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: 62.63 E-value: 7.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDlaIDFTTDtGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEEIAGAKqse 99
Cdd:cd03251 1 VEFKN--VTFRYP-GDGPPVLRDISLDIPAGETVALVGPSGSGKST----LVNLIPRFYDVDSGRILIDGHDVRDYT--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 FDKLRgTKMGLVPQDpmsnlnpVWRIGTQVKEALKANNMDVAHEK-RSALAKALAGDEVEVKGNDDETFLGakelpelmt 178
Cdd:cd03251 71 LASLR-RQIGLVSQD-------VFLFNDTVAENIAYGRPGATREEvEEAARAANAHEFIMELPEGYDTVIG--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 179 eakkaltEAGVSgeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmddriagl 258
Cdd:cd03251 134 -------ERGVK-------------------------------------------------------------------- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 lseaglpdaatrarqfpheFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDslGTAVLFITHDL 338
Cdd:cd03251 139 -------------------LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRL 197
|
330 340
....*....|....*....|..
gi 2545376782 339 GlAAERAQHIVVMYKGQVVESG 360
Cdd:cd03251 198 S-TIENADRIVVLEDGKIVERG 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
439-650 |
8.27e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 8.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTStfkskdllgfrrhvqpvFQNPYGS---- 514
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-----------------FNGPKSSqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 515 ---------LDPMYSIFRSI---EEPlrIHKIGDKKWR-----ANRVKELLDMVEMPASVMGrypnELSGGQRQRIAIAR 577
Cdd:PRK10762 81 igiihqelnLIPQLTIAENIflgREF--VNRFGRIDWKkmyaeADKLLARLNLRFSSDKLVG----ELSIGEQQMVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 578 AMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKLV-EHATTD 650
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFIaEREVAD 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
219-369 |
9.38e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.72 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 219 LIKAGVADDL----IKAGVADDQAWYLAKKYVTGSTMDDriagllseaglpdaaTRARQFPHEFSGGMRQRALIAIGLAC 294
Cdd:PRK13631 129 LFKDTIEKDImfgpVALGVKKSEAKKLAKFYLNKMGLDD---------------SYLERSPFGLSGGQKRRVAIAGILAI 193
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 295 RPDLLIADEPTSALDVTVQKRILDhLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHP 369
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-368 |
1.38e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.45 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 27 IDFTTDTGKPVH--AVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEEI-AGAKQSEFDKL 103
Cdd:PRK13649 8 VSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKST----IMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 104 RgTKMGLVPQDPMSNLNPvwriGTQVKE-ALKANNMDVAHEKRSALAKalagdevevkgnddetflgakelpelmteakK 182
Cdd:PRK13649 84 R-KKVGLVFQFPESQLFE----ETVLKDvAFGPQNFGVSQEEAEALAR-------------------------------E 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 183 ALTEAGVSGEAFDKAvarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmddriagllsea 262
Cdd:PRK13649 128 KLALVGISESLFEKN----------------------------------------------------------------- 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 263 glpdaatrarqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLfITHDLGLAA 342
Cdd:PRK13649 143 ------------PFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVL-VTHLMDDVA 209
|
330 340
....*....|....*....|....*.
gi 2545376782 343 ERAQHIVVMYKGQVVESGPSLEVLQH 368
Cdd:PRK13649 210 NYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
450-632 |
1.58e-10 |
|
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: 59.69 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 450 RGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYegrdtstfkskdllgfrrhvqpvfqnpygsLDPmySIFRSIEEPL 529
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY------------------------------IDG--EDILEEVLDQ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 530 RIHKIGdkkwranrvkelldmvempasvmGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDV-----LVQDQVL 604
Cdd:smart00382 49 LLLIIV-----------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEEL 105
|
170 180
....*....|....*....|....*...
gi 2545376782 605 RLLNDLQAEKGLSYLFITHDLAVVRQIA 632
Cdd:smart00382 106 RLLLLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
34-384 |
1.62e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 62.31 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 34 GKPvhAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLL-PGTGHVVngsikldgeeIAGAKQSEFDKLRGTK--MGL 110
Cdd:PRK13644 14 GTP--ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQKGKVL----------VSGIDTGDFSKLQGIRklVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 111 VPQDPMSNLnpvwrIGTQVKEALKANnmdvahekrsalakalagdevevkgnddetflgakelPElmteakkalteagvs 190
Cdd:PRK13644 82 VFQNPETQF-----VGRTVEEDLAFG-------------------------------------PE--------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 191 geafdkavarftNEWVPGSETRWRVaddlikagvaddlikagvadDQAwylakkyvtgstmddriaglLSEAGLPDAATR 270
Cdd:PRK13644 105 ------------NLCLPPIEIRKRV--------------------DRA--------------------LAEIGLEKYRHR 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 271 ArqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGlAAERAQHIVV 350
Cdd:PRK13644 133 S---PKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIV 207
|
330 340 350
....*....|....*....|....*....|....
gi 2545376782 351 MYKGQVVESGPSLEVLQHPQhpyTKRLVAAAPSL 384
Cdd:PRK13644 208 MDRGKIVLEGEPENVLSDVS---LQTLGLTPPSL 238
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
444-654 |
1.62e-10 |
|
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: 64.58 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 444 VSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRdtstfkskdllgfrrhVQPVFQNPYGSLDPMYsifr 523
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------------VAYVPQQAWIQNDSLR---- 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 524 siEEPLRIHKIGDKKWRA--NRVKELLDMVEMPA---SVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVL 598
Cdd:TIGR00957 717 --ENILFGKALNEKYYQQvlEACALLPDLEILPSgdrTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 599 VQDQVL-RLLNDLQAEKGLSYLFITHDLAVVRQIaDEVVVMQHGKLVEHATTDEVFD 654
Cdd:TIGR00957 795 VGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
275-360 |
1.71e-10 |
|
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: 61.12 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 275 PHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKG 354
Cdd:cd03301 128 PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
....*.
gi 2545376782 355 QVVESG 360
Cdd:cd03301 208 QIQQIG 213
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
19-385 |
1.83e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.02 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFTtdtGKPvhAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEEIAGAkqs 98
Cdd:PRK11248 1 MLQISHLYADYG---GKP--ALEDINLTLESGELLVVLGPSGCGKTT----LLNLIAGFVPYQHGSITLDGKPVEGP--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 99 efdklrGTKMGLVPQDpmsnlnpvwrigtqvkEALkannmdvahekrsalakalagdevevkgnddetflgakeLPelmt 178
Cdd:PRK11248 69 ------GAERGVVFQN----------------EGL---------------------------------------LP---- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 179 eakkalteagvsgeafdkavarftnewvpgsetrWRVADDlikaGVADDLIKAGVADDQAWYLAKKyvtgstmddriagL 258
Cdd:PRK11248 84 ----------------------------------WRNVQD----NVAFGLQLAGVEKMQRLEIAHQ-------------M 112
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 LSEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDL 338
Cdd:PRK11248 113 LKKVGLEGAEKR---YIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2545376782 339 GLAAERAQHIVVMykgqvvESGPSlEVLQHPQHPYTKRLVAAAPSLA 385
Cdd:PRK11248 190 EEAVFMATELVLL------SPGPG-RVVERLPLNFARRFVAGESSRS 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
277-360 |
2.10e-10 |
|
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: 60.76 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKGQV 356
Cdd:cd03269 128 ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
....
gi 2545376782 357 VESG 360
Cdd:cd03269 207 VLYG 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
279-624 |
2.65e-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: 63.42 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHmltDSLGTaVLFITHD---LGLAAE------RAQHIV 349
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ---EYPGT-VVAVTHDryfLDNVAGwileldRGRGIP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 350 vmYKG-------------QVVESGPS---------LE-VLQHP--QHPYTKRLVAAAPSLASQriiSAKERGEDADAlld 404
Cdd:TIGR03719 239 --WEGnysswleqkqkrlEQEEKEESarqktlkreLEwVRQSPkgRQAKSKARLARYEELLSQ---EFQKRNETAEI--- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 405 hHI-AGESTLEKsehIITVDHLTKEF--KLprkkemfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGK 481
Cdd:TIGR03719 311 -YIpPGPRLGDK---VIEAENLTKAFgdKL--------LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 482 VfyegrdtstfkskdLLGFRRHVQPVFQNpYGSLDPMYSIFRSIEEPLRIHKIGDkkwranrvkelldmVEMPA-SVMGR 560
Cdd:TIGR03719 379 I--------------EIGETVKLAYVDQS-RDALDPNKTVWEEISGGLDIIKLGK--------------REIPSrAYVGR 429
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 561 YpN-----------ELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVlvqdQVLRLLNDLQAEKGLSYLFITHD 624
Cdd:TIGR03719 430 F-NfkgsdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHD 499
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
447-638 |
2.67e-10 |
|
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: 61.23 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 447 SVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKV-----------FYEGRDTSTFKSKDLLGfrrHVQPVFQNPYGSL 515
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYFTKLLEG---DVKVIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 516 DPMySIFRSIEEPLrihkigDKKWRANRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSAL 595
Cdd:cd03236 99 IPK-AVKGKVGELL------KKKDERGKLDELVDQLEL-RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2545376782 596 DVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVM 638
Cdd:cd03236 171 DIKQRLNAARLIREL-AEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
439-644 |
3.02e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.21 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLL--GFRRHVQP--------VF 508
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALenGISMVHQElnlvlqrsVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 509 QNPYGSLDPMYSIFrsIEEplrihkigDKKWR-ANRVKELLDMVEMPASVMGrypnELSGGQRQRIAIARAMALDPDVIV 587
Cdd:PRK10982 92 DNMWLGRYPTKGMF--VDQ--------DKMYRdTKAIFDELDIDIDPRAKVA----TLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 588 CDEAVSALDVLVQDQVLRLLNDLQaEKGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
264-369 |
4.01e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.04 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 264 LPDAATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAE 343
Cdd:PRK11432 123 LVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFA 202
|
90 100
....*....|....*....|....*.
gi 2545376782 344 RAQHIVVMYKGQVVESGPSLEVLQHP 369
Cdd:PRK11432 203 VSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
275-379 |
4.29e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.97 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 275 PHEFSGGMRQRalIAIG--LACRPDLLIADEPTSALD--VTVQKRI-LDHLHmltDSLGTAVLFITHDLGLAAERAQHIV 349
Cdd:PRK11000 131 PKALSGGQRQR--VAIGrtLVAEPSVFLLDEPLSNLDaaLRVQMRIeISRLH---KRLGRTMIYVTHDQVEAMTLADKIV 205
|
90 100 110
....*....|....*....|....*....|
gi 2545376782 350 VMYKGQVVESGPSLEVLQHPQHpytkRLVA 379
Cdd:PRK11000 206 VLDAGRVAQVGKPLELYHYPAN----RFVA 231
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
19-337 |
4.57e-10 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 60.10 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 19 LLEVKDLAIDFT--TDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGE----EI 92
Cdd:TIGR02324 1 LLEVEDLSKTFTlhQQGGVRLPVLKNVSLTVNAGECVALSGPSGAGKST----LLKSLYANYLPDSGRILVRHEgawvDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 93 AGAKQSEFDKLRGTKMGLVPQdpmsnlnpvwrigtqvkealkannmdvahekrsalakalagdevevkgnddetflgake 172
Cdd:TIGR02324 77 AQASPREVLEVRRKTIGYVSQ----------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 173 lpelmteakkalteagvsgeaFDKAVARftnewVPGSETrwrvaddlikagVADDLIKAGVADDQAWYLAKKYVTGSTMD 252
Cdd:TIGR02324 98 ---------------------FLRVIPR-----VSALEV------------VAEPLLERGVPREAARARARELLARLNIP 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 DRIAGLlseaglpdaatrarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVL 332
Cdd:TIGR02324 140 ERLWHL---------------PPATFSGGEQQRVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKAR-GAALI 203
|
....*
gi 2545376782 333 FITHD 337
Cdd:TIGR02324 204 GIFHD 208
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
435-645 |
5.15e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 435 KEMFKAVDdvsFSVKRGTTLAIVGESGSGKSTVANMVlhllkptSGKVFYEGRDTS-TFKSKDLLGFrrhvQPVFQNPYG 513
Cdd:PRK09580 14 KAILRGLN---LEVRPGEVHAIMGPNGSGKSTLSATL-------AGREDYEVTGGTvEFKGKDLLEL----SPEDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 514 sldpmysIFRSIEEPLRIHKIGDKKW--------RANRVKELLD-------------MVEMPASVMGRYPNE-LSGGQRQ 571
Cdd:PRK09580 80 -------IFMAFQYPVEIPGVSNQFFlqtalnavRSYRGQEPLDrfdfqdlmeekiaLLKMPEDLLTRSVNVgFSGGEKK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 572 RIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKgLSYLFITHDLAVVRQIA-DEVVVMQHGKLVE 645
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGK-RSFIIVTHYQRILDYIKpDYVHVLYQGRIVK 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
26-368 |
5.16e-10 |
|
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: 62.43 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 26 AIDFT-TDTGKPvhAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEEIAGAKqseFDKLR 104
Cdd:TIGR02203 335 NVTFRyPGRDRP--ALDSISLVIEPGETVALVGRSGSGKST----LVNLIPRFYEPDSGQILLDGHDLADYT---LASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 105 gTKMGLVPQDPM------SNlNPVWRIGTQVKEAlkannmdvahEKRSALAKALAGDEVEvkgnddetflgakELPELMT 178
Cdd:TIGR02203 406 -RQVALVSQDVVlfndtiAN-NIAYGRTEQADRA----------EIERALAAAYAQDFVD-------------KLPLGLD 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 179 eakkalTEAGVSGeafdkavarftnewvpgsetrwrvaddlikagvaddlikagvaddqawylakkyvtgstmddriaGL 258
Cdd:TIGR02203 461 ------TPIGENG-----------------------------------------------------------------VL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 LSeaglpdaatrarqfphefsGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDslGTAVLFITHDL 338
Cdd:TIGR02203 470 LS-------------------GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRL 528
|
330 340 350
....*....|....*....|....*....|
gi 2545376782 339 GlAAERAQHIVVMYKGQVVESGPSLEVLQH 368
Cdd:TIGR02203 529 S-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
33-368 |
5.34e-10 |
|
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: 62.46 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 33 TGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAgakQSEFDKLrGTKMGLVP 112
Cdd:COG4618 343 SKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTA----GSVRLDGADLS---QWDREEL-GRHIGYLP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 113 QDPmsNLNPvwriGTqVKEalkannmdvahekrsalakalagdevevkgNddetflgakelpelmteakkalteagvsge 192
Cdd:COG4618 413 QDV--ELFD----GT-IAE------------------------------N------------------------------ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 193 afdkaVARFTNewvpgsetrwrvADDlikagvaDDLIKAgvaddqawylAKKyvTGstMDDRIAGL-------LSEAGLP 265
Cdd:COG4618 426 -----IARFGD------------ADP-------EKVVAA----------AKL--AG--VHEMILRLpdgydtrIGEGGAR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 266 daatrarqfpheFSGGMRQRaliaIGLA----CRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLA 341
Cdd:COG4618 468 ------------LSGGQRQR----IGLAralyGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLL 530
|
330 340
....*....|....*....|....*..
gi 2545376782 342 AErAQHIVVMYKGQVVESGPSLEVLQH 368
Cdd:COG4618 531 AA-VDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
221-643 |
5.36e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.57 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 221 KAGVADDLIKAGVADdqaWYLAKKYVTGSTMDDRIAGLLseAGLPDAATRARQFPHEFSGGMRQRALIAIGLACRPDLLI 300
Cdd:PLN03073 293 KDGVDKDAVSQRLEE---IYKRLELIDAYTAEARAASIL--AGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 301 ADEPTSALDVTV-------------QKRILDHLHMLTDSLGTAVLFItHDLGLAA--------ERAQHIVVMYKGQVVES 359
Cdd:PLN03073 368 LDEPTNHLDLHAvlwletyllkwpkTFIVVSHAREFLNTVVTDILHL-HGQKLVTykgdydtfERTREEQLKNQQKAFES 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 360 gpSLEVLQHPQHPYTK-RLVAAAPSLASQRiISAKERGEDADALL---DHHIAGESTLEK-SEHIITVDHLTkeFKLPRK 434
Cdd:PLN03073 447 --NERSRSHMQAFIDKfRYNAKRASLVQSR-IKALDRLGHVDAVVndpDYKFEFPTPDDRpGPPIISFSDAS--FGYPGG 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 435 KEMFKavdDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGR-DTSTFKSKDLLGFRRHVQPVFQnpyg 513
Cdd:PLN03073 522 PLLFK---NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQHHVDGLDLSSNPLLY---- 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 514 sldpMYSIFRSI-EEPLRIHkIGDKKWRANrvkelLDMVEMpasvmgrypNELSGGQRQRIAIARAMALDPDVIVCDEAV 592
Cdd:PLN03073 595 ----MMRCFPGVpEQKLRAH-LGSFGVTGN-----LALQPM---------YTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2545376782 593 SALDVlvqDQVLRLLNDLQAEKGlSYLFITHDLAVVRQIADEVVVMQHGKL 643
Cdd:PLN03073 656 NHLDL---DAVEALIQGLVLFQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
39-360 |
8.22e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.90 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 39 AVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLL-----PGTGHvvngsIKLDGEEIAGAKQSefdKLRgTKMGLVPQ 113
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKST----LINLLqrvfdPQSGR-----ILIDGTDIRTVTRA---SLR-RNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 114 DPM-------SNLnpvwRIGtqvkealkannmdvahekrsalaKALAGDEvevkgnddetflgakelpELMTEAKKAlte 186
Cdd:PRK13657 417 DAGlfnrsieDNI----RVG-----------------------RPDATDE------------------EMRAAAERA--- 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 187 agvsgeafdkavarftnewvpgsetrwrVADDLIkagvaddlikagvaddqawylakkyvtgstmDDRIAGLLSEAGlpd 266
Cdd:PRK13657 449 ----------------------------QAHDFI-------------------------------ERKPDGYDTVVG--- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 267 aaTRARQfpheFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVlfITHDLGLAAErAQ 346
Cdd:PRK13657 467 --ERGRQ----LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVRN-AD 537
|
330
....*....|....
gi 2545376782 347 HIVVMYKGQVVESG 360
Cdd:PRK13657 538 RILVFDNGRVVESG 551
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
279-367 |
1.02e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.47 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 279 SGGMRQRALIA-----IGLACRPD--LLIADEPTSALDVTvQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVM 351
Cdd:COG4138 128 SGGEWQRVRLAavllqVWPTINPEgqLLLLDEPMNSLDVA-QQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLL 206
|
90
....*....|....*.
gi 2545376782 352 YKGQVVESGPSLEVLQ 367
Cdd:COG4138 207 KQGKLVASGETAEVMT 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
34-360 |
1.04e-09 |
|
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: 59.14 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 34 GKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIagaKQSEFDKLRGtKMGLVPQ 113
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTS----GSVLLDGTDI---RQLDPADLRR-NIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 114 DPmsnlnpvwrigTQVKEALKANnmdvahekrSALAKALAGDEvevkgnddetflgakelpELMteakkalteagvsgea 193
Cdd:cd03245 86 DV-----------TLFYGTLRDN---------ITLGAPLADDE------------------RIL---------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 194 fdkAVARFtnewvpgsetrwrvaddlikAGVADdlikagvaddqawyLAKKYVTGSTMddriagLLSEAGlpdaatrarq 273
Cdd:cd03245 112 ---RAAEL--------------------AGVTD--------------FVNKHPNGLDL------QIGERG---------- 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 274 fpHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDslGTAVLFITHDLGLaAERAQHIVVMYK 353
Cdd:cd03245 139 --RGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSL-LDLVDRIIVMDS 213
|
....*..
gi 2545376782 354 GQVVESG 360
Cdd:cd03245 214 GRIVADG 220
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-349 |
1.35e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 58.65 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIdftTDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGHVvNGSIKLDGEEIAgAKQSE 99
Cdd:COG4136 2 LSLENLTI---TLGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSA-SGEVLLNGRRLT-ALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 fdkLRGtkMGLVPQDPMsnLNPvwrigtqvkealkanNMDVAHEkrsaLAKALAGDevevkgnddetflgakelpelmte 179
Cdd:COG4136 75 ---QRR--IGILFQDDL--LFP---------------HLSVGEN----LAFALPPT------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 180 akkalteagvsgeafdkavarftnewVPGSETRwrvaddlikagvaddlikagvaddqawylakkyvtgstmdDRIAGLL 259
Cdd:COG4136 105 --------------------------IGRAQRR----------------------------------------ARVEQAL 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 260 SEAGLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLG 339
Cdd:COG4136 119 EEAGLAGFADR---DPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
330
....*....|
gi 2545376782 340 LAAERAQHIV 349
Cdd:COG4136 196 DAPAAGRVLD 205
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
40-368 |
1.48e-09 |
|
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: 60.82 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 40 VRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEIagaKQSEFDKLrGTKMGLVPQDpmsnl 119
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPT----SGSVRLDGADL---KQWDRETF-GKHIGYLPQD----- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 120 npvwrigTQVKEALKANNMdvahekrsalakALAGDEVEvkgnddetflgakelPELMTEAKKAlteAGVSgeafdKAVA 199
Cdd:TIGR01842 401 -------VELFPGTVAENI------------ARFGENAD---------------PEKIIEAAKL---AGVH-----ELIL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 200 RFTNewvpGSETrwrvaddlikagvaddlikagvaddqawylakkyvtgstmddriagLLSEAGLPdaatrarqfpheFS 279
Cdd:TIGR01842 439 RLPD----GYDT----------------------------------------------VIGPGGAT------------LS 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 280 GGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTaVLFITHDLGLaAERAQHIVVMYKGQVVES 359
Cdd:TIGR01842 457 GGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGIT-VVVITHRPSL-LGCVDKILVLQDGRIARF 534
|
....*....
gi 2545376782 360 GPSLEVLQH 368
Cdd:TIGR01842 535 GERDEVLAK 543
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
279-374 |
1.51e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.02 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLgtAVLFITHDLGLAAERAQHIVVMYKGQVVE 358
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIE 227
|
90
....*....|....*.
gi 2545376782 359 SGPSLEVLQHPQHPYT 374
Cdd:PRK14239 228 YNDTKQMFMNPKHKET 243
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
275-369 |
1.54e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.24 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 275 PHEFSGGMRQRalIAIGLAC--RPDLLIADEPTSALD--VTVQKRI-LDHLHMltdSLGTAVLFITHDLGLAAERAQHIV 349
Cdd:PRK11650 132 PRELSGGQRQR--VAMGRAIvrEPAVFLFDEPLSNLDakLRVQMRLeIQRLHR---RLKTTSLYVTHDQVEAMTLADRVV 206
|
90 100
....*....|....*....|
gi 2545376782 350 VMYKGQVVESGPSLEVLQHP 369
Cdd:PRK11650 207 VMNGGVAEQIGTPVEVYEKP 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
257-336 |
1.68e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 257 GLLSEAGLPDAAT-RARqfPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFIT 335
Cdd:COG2401 117 ELLNAVGLSDAVLwLRR--FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVAT 194
|
.
gi 2545376782 336 H 336
Cdd:COG2401 195 H 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
440-643 |
1.92e-09 |
|
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: 61.18 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 440 AVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTfkskDLLGFRRHVQPVFQNpygslDPMY 519
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQSLGMCPQH-----NILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 SIFRSIEEPLRIHKIGDKKWRANRVkELLDMVEMPASVMGR--YPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDV 597
Cdd:TIGR01257 1016 HHLTVAEHILFYAQLKGRSWEEAQL-EMEAMLEDTGLHHKRneEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2545376782 598 LVQDQVLRLLndLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKL 643
Cdd:TIGR01257 1095 YSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
443-651 |
1.98e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.29 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTS-------GKVFYEGRDTSTFKSKdllgFRRHVqpVFQNPYgsl 515
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdasvvirGTVAYVPQVSWIFNAT----VRDNI--LFGSPF--- 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 516 DPmysifrsieeplrihkigDKKWRANRVKELL-DMVEMPA---SVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEA 591
Cdd:PLN03130 706 DP------------------ERYERAIDVTALQhDLDLLPGgdlTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2545376782 592 VSALDVLVQDQVLRllNDLQAE-KGLSYLFITHDLAVVRQIaDEVVVMQHGKLVEHATTDE 651
Cdd:PLN03130 768 LSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEE 825
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-360 |
2.17e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.54 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDL--AIDfttdtGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLlPGTgHVVNGSIKLDGEEIagakq 97
Cdd:COG0396 1 LEIKNLhvSVE-----GKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKY-EVTSGSILLDGEDI----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 98 sefdklrgtkmglvpqdpmsnlnpvwrigtqvkealkaNNMDVahEKRsalakALAG------DEVEVKGNDDETFLgak 171
Cdd:COG0396 67 --------------------------------------LELSP--DER-----ARAGiflafqYPVEIPGVSVSNFL--- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 172 elpelmTEAKKALTEAGVSGEAFDKAVarftNEWvpgsetrwrvADDLikaGVADDLIKAGVADDqawylakkyvtgstm 251
Cdd:COG0396 99 ------RTALNARRGEELSAREFLKLL----KEK----------MKEL---GLDEDFLDRYVNEG--------------- 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 252 ddriagllseaglpdaatrarqfpheFSGGMRQRALIAIGLACRPDLLIADEPTSALDV-TVQK--RILDHLHmltdSLG 328
Cdd:COG0396 141 --------------------------FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdALRIvaEGVNKLR----SPD 190
|
330 340 350
....*....|....*....|....*....|....
gi 2545376782 329 TAVLFITH--DLgLAAERAQHIVVMYKGQVVESG 360
Cdd:COG0396 191 RGILIITHyqRI-LDYIKPDFVHVLVDGRIVKSG 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
145-623 |
2.66e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 145 RSALAKALAGdevevkgnddetflgakELPELMTEAKKALTE-AGVSGEAFDKAVArftNEWVpgsetrwRVADDLIKAG 223
Cdd:PRK10938 42 KSALARALAG-----------------ELPLLSGERQSQFSHiTRLSFEQLQKLVS---DEWQ-------RNNTDMLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 224 VAD------DLIKAGVADDQAW-YLAKKYvtgstmddRIAGLLSeaglpdaatraRQFPHeFSGGMRQRALIAIGLACRP 296
Cdd:PRK10938 95 EDDtgrttaEIIQDEVKDPARCeQLAQQF--------GITALLD-----------RRFKY-LSTGETRKTLLCQALMSEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 297 DLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFIT--HDLglaAERAQHIVVMYKGQVVESGPSLEVLQHpqhpyt 374
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNrfDEI---PDFVQFAGVLADCTLAETGEREEILQQ------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 375 krlvaaapSLASQRIISAKERGE---DADALLDHHiagesTLEKSEHIITVDHLTKEFKLPRkkemfkAVDDVSFSVKRG 451
Cdd:PRK10938 226 --------ALVAQLAHSEQLEGVqlpEPDEPSARH-----ALPANEPRIVLNNGVVSYNDRP------ILHNLSWQVNPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 452 TTLAIVGESGSGKSTVANMV-----------LHLL--KPTSGKVFYEGRDTSTFKSKDL-LGFR--RHVQPVFQNpyGSL 515
Cdd:PRK10938 287 EHWQIVGPNGAGKSTLLSLItgdhpqgysndLTLFgrRRGSGETIWDIKKHIGYVSSSLhLDYRvsTSVRNVILS--GFF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 516 DPMySIFRSIEEPLRIhkigdkkwranRVKELLDMVEMPASVMGRYPNELSGGQrQRIA-IARAMALDPDVIVCDEAVSA 594
Cdd:PRK10938 365 DSI-GIYQAVSDRQQK-----------LAQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQG 431
|
490 500
....*....|....*....|....*....
gi 2545376782 595 LDVLVQDQVLRLLNDLQAEKGLSYLFITH 623
Cdd:PRK10938 432 LDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
252-342 |
3.06e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.82 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 252 DDRIAGLLSEAGLPDAATR---ARQFPHEFSGGMRQ-----RALIAiglacRPDLLIADEPTSALDVTVQKRIldhLHML 323
Cdd:COG4178 457 DAELREALEAVGLGHLAERldeEADWDQVLSLGEQQrlafaRLLLH-----KPDWLFLDEATSALDEENEAAL---YQLL 528
|
90 100
....*....|....*....|
gi 2545376782 324 TDSL-GTAVLFITHDLGLAA 342
Cdd:COG4178 529 REELpGTTVISVGHRSTLAA 548
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
253-360 |
3.66e-09 |
|
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: 57.73 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 DRIAGLLSEAGLPDAATRarqfphEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVL 332
Cdd:cd03267 135 DELSELLDLEELLDTPVR------QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVL 208
|
90 100
....*....|....*....|....*...
gi 2545376782 333 FITHDLGLAAERAQHIVVMYKGQVVESG 360
Cdd:cd03267 209 LTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
259-379 |
3.90e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.77 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 259 LSEAGLPDaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVtvqkriLDHLHM--LTDSL----GTAVL 332
Cdd:PRK11247 118 LAAVGLAD---RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA------LTRIEMqdLIESLwqqhGFTVL 188
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2545376782 333 FITHDLGLAAERAQHIVVMYKGQVvesGPSLEV-LQHPQHPYTKRLVA 379
Cdd:PRK11247 189 LVTHDVSEAVAMADRVLLIEEGKI---GLDLTVdLPRPRRRGSARLAE 233
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
264-371 |
4.29e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.91 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 264 LPDAATRARQFPHEFSGGMRQRALIAIGLA---------CRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFI 334
Cdd:PRK13547 132 LAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAI 211
|
90 100 110
....*....|....*....|....*....|....*..
gi 2545376782 335 THDLGLAAERAQHIVVMYKGQVVESGPSLEVLQhPQH 371
Cdd:PRK13547 212 VHDPNLAARHADRIAMLADGAIVAHGAPADVLT-PAH 247
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
278-367 |
5.05e-09 |
|
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: 56.77 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 278 FSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAE-RAQHIVVMYKGQV 356
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYiKPDRVHVLYDGRI 183
|
90
....*....|.
gi 2545376782 357 VESGPSLEVLQ 367
Cdd:cd03217 184 VKSGDKELALE 194
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-360 |
5.34e-09 |
|
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: 59.45 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 2 TDNTNAKMLAMQkehGPLLEVKDlaIDFTTDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMavlgLLPGTGHVV 81
Cdd:COG5265 343 ADAPDAPPLVVG---GGEVRFEN--VSFGYDPERPI--LKGVSFEVPAGKTVAIVGPSGAGKSTLAR----LLFRFYDVT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 82 NGSIKLDGEEIAGAKQsefDKLRGTkMGLVPQDP-MSNlnpvwrigtqvkEALKANnmdvahekrSALAKALAGDEvEVk 160
Cdd:COG5265 412 SGRILIDGQDIRDVTQ---ASLRAA-IGIVPQDTvLFN------------DTIAYN---------IAYGRPDASEE-EV- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 161 gnddetflgakelpelmteakkalteagvsgeafdkavarftnewvpgsetrWRVAddliKAGVADDLIKAgvaddqawy 240
Cdd:COG5265 465 ----------------------------------------------------EAAA----RAAQIHDFIES--------- 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 241 LAKKYVTgstmddriagLLSEAGLpdaatrarqfphEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHL 320
Cdd:COG5265 480 LPDGYDT----------RVGERGL------------KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAAL 537
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2545376782 321 HMLtdSLGTAVLFITHDLGLAAeRAQHIVVMYKGQVVESG 360
Cdd:COG5265 538 REV--ARGRTTLVIAHRLSTIV-DADEILVLEAGRIVERG 574
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
539-644 |
6.28e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 539 WR-ANRVKELLDMVEMPASVMgryPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVlvqDQVLRLLNDLQAEKGlS 617
Cdd:PRK11147 133 WQlENRINEVLAQLGLDPDAA---LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI---ETIEWLEGFLKTFQG-S 205
|
90 100
....*....|....*....|....*..
gi 2545376782 618 YLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:PRK11147 206 IIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
254-388 |
6.88e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.97 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 254 RIAGLLSEAGLPDaatRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLF 333
Cdd:PRK10535 124 RAQELLQRLGLED---RVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVII 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 334 ITHDLGLAAErAQHIVVMYKGQVVESGPSlevlqHPQHPYTKRLVAAAPSLASQR 388
Cdd:PRK10535 200 VTHDPQVAAQ-AERVIEIRDGEIVRNPPA-----QEKVNVAGGTEPVVNTASGWR 248
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
439-644 |
7.17e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.81 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 KAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLLgfRRHVQPVfqnPYGSldpm 518
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM--REAVAIV---PEGR---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 519 ySIFR--SIEEPLRIHK-IGDKKWRANRVKELLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSAL 595
Cdd:PRK11614 90 -RVFSrmTVEENLAMGGfFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2545376782 596 DVLVQDQVLRLLNDLQAEkGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-360 |
7.66e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.70 E-value: 7.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIdFTTDtGKPvhAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvngSIKLDGEEIagaKQSE 99
Cdd:PRK11174 350 IEAEDLEI-LSPD-GKT--LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG-----SLKINGIEL---RELD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 FDKLRGtKMGLVPQDPMsnlnpvwrigtQVKEALKANnmdvahekrSALAKALAGDEvevkgnddetflgakelpelmtE 179
Cdd:PRK11174 418 PESWRK-HLSWVGQNPQ-----------LPHGTLRDN---------VLLGNPDASDE----------------------Q 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 180 AKKALTEAGVsgeafdkavarftNEWVPgsetrwRVADDLikagvaDDLIKagvadDQAwylakkyvtgstmddriagll 259
Cdd:PRK11174 455 LQQALENAWV-------------SEFLP------LLPQGL------DTPIG-----DQA--------------------- 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 260 seAGLpdaatrarqfphefSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLtdSLGTAVLFITHDLG 339
Cdd:PRK11174 484 --AGL--------------SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHQLE 545
|
330 340
....*....|....*....|.
gi 2545376782 340 lAAERAQHIVVMYKGQVVESG 360
Cdd:PRK11174 546 -DLAQWDQIWVMQDGQIVQQG 565
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
270-362 |
8.04e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.20 E-value: 8.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 270 RARQFpHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHiV 349
Cdd:PRK15056 136 RHRQI-GELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDY-T 212
|
90
....*....|...
gi 2545376782 350 VMYKGQVVESGPS 362
Cdd:PRK15056 213 VMVKGTVLASGPT 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
443-653 |
9.75e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTsgkvfyegrDTSTFKSKDLLGFRRHVQPVFQNPYGSldpmYSIF 522
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA---------ETSSVVIRGSVAYVPQVSWIFNATVRE----NILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 523 RSIEEPLRIhkigdkkWRANRVKELL-DMVEMPA---SVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVL 598
Cdd:PLN03232 702 GSDFESERY-------WRAIDVTALQhDLDLLPGrdlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 599 VQDQVLR--LLNDLQaekGLSYLFITHDLAVVRQIaDEVVVMQHGKLVEHATTDEVF 653
Cdd:PLN03232 775 VAHQVFDscMKDELK---GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
444-635 |
1.09e-08 |
|
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: 55.58 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 444 VSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDtstfkskdlLGFRRHVQPVFQNPYGSLDPMYSIFr 523
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP---------LDFQRDSIARGLLYLGHAPGIKTTL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 524 SIEEPLRI-HKIGDKkwraNRVKELLDMVEMpASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQ 602
Cdd:cd03231 89 SVLENLRFwHADHSD----EQVEEALARVGL-NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|...
gi 2545376782 603 VLRLLNDLQAEKGLSYLFITHDLAVVRQIADEV 635
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
441-623 |
1.33e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEG----RDTSTFKSKdlLGFRRHVQPVfqNPYGSL- 515
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikKDLCTYQKQ--LCFVGHRSGI--NPYLTLr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 516 -DPMYSIFRS-----IEEPLRIHKIGdkkwranrvkELLDmvempasvmgrYP-NELSGGQRQRIAIARAMALDPDVIVC 588
Cdd:PRK13540 93 eNCLYDIHFSpgavgITELCRLFSLE----------HLID-----------YPcGLLSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 2545376782 589 DEAVSALDVLvqdQVLRLLNDLQA--EKGLSYLFITH 623
Cdd:PRK13540 152 DEPLVALDEL---SLLTIITKIQEhrAKGGAVLLTSH 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
273-370 |
1.60e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.89 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 273 QFP-HEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVM 351
Cdd:PRK09544 115 DAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
90
....*....|....*....
gi 2545376782 352 yKGQVVESGPSLEVLQHPQ 370
Cdd:PRK09544 195 -NHHICCSGTPEVVSLHPE 212
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
433-655 |
1.64e-08 |
|
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: 56.07 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 433 RKKEMFKAV-DDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNP 511
Cdd:cd03288 28 RYENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL---RSRLSIILQDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 512 Y---GS----LDPMYSIfrsieeplrihkIGDKKWRANRVKELLDMVE-MPA---SVMGRYPNELSGGQRQRIAIARAMA 580
Cdd:cd03288 105 IlfsGSirfnLDPECKC------------TDDRLWEALEIAQLKNMVKsLPGgldAVVTEGGENFSVGQRQLFCLARAFV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 581 LDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKglSYLFITHDLAVVRQiADEVVVMQHGKLVEHATTDEVFDH 655
Cdd:cd03288 173 RKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-377 |
2.60e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.14 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDlaIDFTTDtGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDGEEIAGAKQ 97
Cdd:PRK11160 337 VSLTLNN--VSFTYP-DQPQPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLTRAWDPQQGEILLNGQPIADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 98 SEfdkLRGTkMGLVPQdpmsnlnpvwRI----GTqvkeaLKANnmdvahekrSALAKALAGDEvevkgnddetflgakel 173
Cdd:PRK11160 410 AA---LRQA-ISVVSQ----------RVhlfsAT-----LRDN---------LLLAAPNASDE----------------- 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 174 pelmteakkALTEAgvsgeafdkavarftnewvpgsetrwrvaddLIKAGVaDDLIKagvaDDQ---AWylakkyvtgst 250
Cdd:PRK11160 445 ---------ALIEV-------------------------------LQQVGL-EKLLE----DDKglnAW----------- 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 251 mddriaglLSEAGlpdaatraRQFphefSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDslGTA 330
Cdd:PRK11160 469 --------LGEGG--------RQL----SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKT 526
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2545376782 331 VLFITHDLgLAAERAQHIVVMYKGQVVESGPSLEVLQhpQHPYTKRL 377
Cdd:PRK11160 527 VLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLA--QQGRYYQL 570
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
245-360 |
2.64e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.28 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 245 YVTGSTMD-------DRIAGLLSEAGLPDAATRARQfphEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRIL 317
Cdd:NF000106 108 YMIGR*LDlsrkdarARADELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2545376782 318 DHLH-MLTDslGTAVLFITHDLGLAAERAQHIVVMYKGQVVESG 360
Cdd:NF000106 185 DEVRsMVRD--GATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
279-356 |
2.72e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 2.72e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKGQV 356
Cdd:PRK15439 405 SGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
275-367 |
2.95e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.51 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 275 PHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKG 354
Cdd:PRK13643 142 PFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKG 220
|
90
....*....|...
gi 2545376782 355 QVVESGPSLEVLQ 367
Cdd:PRK13643 221 HIISCGTPSDVFQ 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
279-356 |
4.07e-08 |
|
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: 54.40 E-value: 4.07e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRIldHLHMLTDSLGTAVLFITHDLGLaAERAQHIVVMYKGQV 356
Cdd:cd03248 152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV--QQALYDWPERRTVLVIAHRLST-VERADQILVLDGGRI 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
436-668 |
4.17e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 436 EMFKAVDdvsFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRdtSTFKSKDLLGFRRHVQPVFQNPYgsL 515
Cdd:PRK15439 25 EVLKGID---FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--PCARLTPAKAHQLGIYLVPQEPL--L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 516 DPMYSIFRSIEEPLRIHKiGDKKWRANRVKEL---LDMvEMPASVmgrypneLSGGQRQRIAIARAMALDPDVIVCDEAV 592
Cdd:PRK15439 98 FPNLSVKENILFGLPKRQ-ASMQKMKQLLAALgcqLDL-DSSAGS-------LEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 593 SALDVLVQDQVLRLLNDLQAeKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATTDEVFDHpqkqytrDLLDAI 668
Cdd:PRK15439 169 ASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD-------DIIQAI 236
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
278-360 |
4.67e-08 |
|
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: 53.47 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 278 FSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHL-HMLTDSlgtAVLFITHDLgLAAERAQHIVVMYKGQV 356
Cdd:cd03247 99 FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIfEVLKDK---TLIWITHHL-TGIEHMDKILFLENGKI 174
|
....
gi 2545376782 357 VESG 360
Cdd:cd03247 175 IMQG 178
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
254-360 |
4.79e-08 |
|
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: 54.04 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 254 RIAGLLSEAGLpdaATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLF 333
Cdd:cd03298 108 AIEVALARVGL---AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLM 184
|
90 100
....*....|....*....|....*..
gi 2545376782 334 ITHDLGLAAERAQHIVVMYKGQVVESG 360
Cdd:cd03298 185 VTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
443-607 |
5.57e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 53.72 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEG---RDTSTFKSKDLLGFRRHVQPVFqnpygsldpmy 519
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiDDPDVAEACHYLGHRNAMKPAL----------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 sifrSIEEPLRIhkigdkkWRANRVKELLDMVEMPASVmGRYP------NELSGGQRQRIAIARAMALDPDVIVCDEAVS 593
Cdd:PRK13539 89 ----TVAENLEF-------WAAFLGGEELDIAAALEAV-GLAPlahlpfGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170
....*....|....
gi 2545376782 594 ALDVLVQDQVLRLL 607
Cdd:PRK13539 157 ALDAAAVALFAELI 170
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
263-367 |
6.94e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 53.82 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 263 GLPDAATRarqFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAA 342
Cdd:PRK10771 118 GIEDLLAR---LPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAA 194
|
90 100
....*....|....*....|....*
gi 2545376782 343 ERAQHIVVMYKGQVVESGPSLEVLQ 367
Cdd:PRK10771 195 RIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
277-360 |
7.55e-08 |
|
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: 53.69 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHL-HMLTDslGTAVLFITHDLGLAAERAQHIVVMYKGQ 355
Cdd:cd03220 142 TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQ--GKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
....*
gi 2545376782 356 VVESG 360
Cdd:cd03220 220 IRFDG 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
276-366 |
7.96e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 54.47 E-value: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 276 HEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQ 355
Cdd:PRK13636 140 HCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
90
....*....|.
gi 2545376782 356 VVESGPSLEVL 366
Cdd:PRK13636 220 VILQGNPKEVF 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-92 |
9.00e-08 |
|
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: 52.91 E-value: 9.00e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 20 LEVKDLAIdftTDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGlLPGTgHVVNGSIKLDGEEI 92
Cdd:cd03217 1 LEIKDLHV---SVGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKY-EVTEGEILFKGEDI 66
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
278-355 |
1.33e-07 |
|
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: 51.30 E-value: 1.33e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 278 FSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDhlhMLTDSLGTaVLFITHDLGLAAERAQHIVVMYKGQ 355
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE---ALKEYPGT-VILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
451-642 |
1.93e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.50 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 451 GTTLAIVGESGSGKSTVANMVLHLLKPTS--GKVFYEGRDTsTFKSKDLLGFrrhvqpVFQNpygslDPMYS-------- 520
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP-TKQILKRTGF------VTQD-----DILYPhltvretl 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 521 IFRSIeepLRIHKI---GDKKWRANRVKELLDMVEMPASVMGR-YPNELSGGQRQRIAIARAMALDPDVIVCDEAVSALD 596
Cdd:PLN03211 162 VFCSL---LRLPKSltkQEKILVAESVISELGLTKCENTIIGNsFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2545376782 597 VLVQDQVLRLLNDLqAEKGLSYLFITHDLAV-VRQIADEVVVMQHGK 642
Cdd:PLN03211 239 ATAAYRLVLTLGSL-AQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGR 284
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
18-369 |
1.97e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.68 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTdtgkpVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEIAGakq 97
Cdd:PRK11300 4 PLLSVSGLMMRFGG-----LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTG----GTILLRGQHIEG--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 98 sefdkLRGTK---MGLVpqdpmsnlnpvwRIGTQV---KEALKANNMDVA---HEKRSALAKALAgdevevkgnddetfl 168
Cdd:PRK11300 72 -----LPGHQiarMGVV------------RTFQHVrlfREMTVIENLLVAqhqQLKTGLFSGLLK--------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 169 gakelpelmTEA-KKAlteagvSGEAFDKAVarftnEWvpgsetrwrvaddLIKAGVADdlikagVADDQAWYLAkkYvt 247
Cdd:PRK11300 120 ---------TPAfRRA------ESEALDRAA-----TW-------------LERVGLLE------HANRQAGNLA--Y-- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 248 gstmddriagllseaglpdaatrarqfphefsgGMRQRALIAIGLACRPDLLIADEPTSALDVTvQKRILDHL-HMLTDS 326
Cdd:PRK11300 157 ---------------------------------GQQRRLEIARCMVTQPEILMLDEPAAGLNPK-ETKELDELiAELRNE 202
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2545376782 327 LGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHP 369
Cdd:PRK11300 203 HNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-368 |
2.28e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.87 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDlaIDFTTDtGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAmavlGLLPGTGHVVNGSIKLDGEEIagaKQSE 99
Cdd:PRK11176 342 IEFRN--VTFTYP-GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIA----NLLTRFYDIDEGEILLDGHDL---RDYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 100 FDKLRgTKMGLVPQDpmsnlnpVWRIGTQVkealkANNMDVAHEKRsalakalagdevevkgnddetflgakelpelmte 179
Cdd:PRK11176 412 LASLR-NQVALVSQN-------VHLFNDTI-----ANNIAYARTEQ---------------------------------- 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 180 akkalteagVSGEAFDKAVarftnewvpgsetrwrvaddliKAGVADDLIkagvaddqawylakkyvtgSTMDDRIAGLL 259
Cdd:PRK11176 445 ---------YSREQIEEAA----------------------RMAYAMDFI-------------------NKMDNGLDTVI 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 260 SEAGLpdaatrarqfphEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRI---LDHLHMltdslGTAVLFITH 336
Cdd:PRK11176 475 GENGV------------LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIqaaLDELQK-----NRTSLVIAH 537
|
330 340 350
....*....|....*....|....*....|..
gi 2545376782 337 DLGlAAERAQHIVVMYKGQVVESGPSLEVLQH 368
Cdd:PRK11176 538 RLS-TIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
251-379 |
2.62e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.48 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 251 MDDRIAGLLSEAGLPDAAT-RARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLgt 329
Cdd:PRK14243 124 MDELVERSLRQAALWDEVKdKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY-- 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 330 AVLFITHDLGLAAeRAQHIVVMYK----------GQVVESGPSLEVLQHPQHPYTKRLVA 379
Cdd:PRK14243 202 TIIIVTHNMQQAA-RVSDMTAFFNveltegggryGYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
232-370 |
2.71e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.52 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 232 GVADDQAWYLAKKYvtgstmddriaglLSEAGLPDAAtrARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVT 311
Cdd:PRK13641 115 GFSEDEAKEKALKW-------------LKKVGLSEDL--ISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 312 VQKRILDhLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHPQ 370
Cdd:PRK13641 180 GRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-114 |
2.83e-07 |
|
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: 51.40 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAI---DFTTDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvVNGSIKLDGeeiagaK 96
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQL--LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG--VSGEVLING------R 73
|
90
....*....|....*...
gi 2545376782 97 QSEFDKLRGtKMGLVPQD 114
Cdd:cd03213 74 PLDKRSFRK-IIGYVPQD 90
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-115 |
3.52e-07 |
|
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: 50.77 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDlaIDFTTDtGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSamavLGLLPGTGHVVNGSIKLDGEEIagakqSE 99
Cdd:cd03247 1 LSINN--VSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTL----LQLLTGDLKPQQGEITLDGVPV-----SD 68
|
90
....*....|....*.
gi 2545376782 100 FDKLRGTKMGLVPQDP 115
Cdd:cd03247 69 LEKALSSLISVLNQRP 84
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
251-380 |
3.80e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 51.96 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 251 MDDRIAGLLSEAGLPD-AATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGT 329
Cdd:PRK14258 123 IDDIVESALKDADLWDeIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSEL 202
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 330 AVLFITHDLGlAAERAQHIVVMYKG------QVVESGPSLEVLQHPQHPYTKRLVAA 380
Cdd:PRK14258 203 TMVIVSHNLH-QVSRLSDFTAFFKGnenrigQLVEFGLTKKIFNSPHDSRTREYVLS 258
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
284-651 |
4.58e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 284 QRALIAIGLACRPD--LLIADEPTSALdvtvQKRILDHLHMLTDSL---GTAVLFITHDLGLAAERAQHIVVMYKGQVVE 358
Cdd:PRK10982 139 QMQMIEIAKAFSYNakIVIMDEPTSSL----TEKEVNHLFTIIRKLkerGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 359 SGPslevlqhpqhpytkrlvaaAPSLASQRIISAKERGEdadalLDHHIAgESTLEKSEHIITVDHLTkEFKLPrkkemf 438
Cdd:PRK10982 215 TQP-------------------LAGLTMDKIIAMMVGRS-----LTQRFP-DKENKPGEVILEVRNLT-SLRQP------ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 439 kAVDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLL--GF------RRHVqpvfqN 510
Cdd:PRK10982 263 -SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAInhGFalvteeRRST-----G 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 511 PYGSLDPMY-SIFRSIEEPLRIHKIGDKKWRANRVKELLDMVEMPASVMGRYPNELSGGQRQRIAIARAMALDPDVIVCD 589
Cdd:PRK10982 337 IYAYLDIGFnSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLD 416
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 590 EAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGK---LVEHATTDE 651
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGLvagIVDTKTTTQ 480
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-85 |
5.11e-07 |
|
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: 50.93 E-value: 5.11e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 20 LEVKDLAIDFTTDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGT-GHV-VNGSI 85
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLsGSVsVPGSI 68
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
237-667 |
6.10e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 237 QAWylakkyvtgsTMDDRIAGLLSeaGLPDAATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDvtvqkri 316
Cdd:PRK10636 121 DAW----------TIRSRAASLLH--GLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 317 LDHLHMLTDSL----GTAVLfITHD---LGLAAERAQHI----VVMYKGQvvesgpslevlqhpqhpYTKRLVAAAPSLA 385
Cdd:PRK10636 182 LDAVIWLEKWLksyqGTLIL-ISHDrdfLDPIVDKIIHIeqqsLFEYTGN-----------------YSSFEVQRATRLA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 386 SQRII--SAKERGEDADALLDHHIAGES----------TLEKSEhIITVDHLTKEFK--------LPR---KKEMFKA-- 440
Cdd:PRK10636 244 QQQAMyeSQQERVAHLQSYIDRFRAKATkakqaqsrikMLERME-LIAPAHVDNPFHfsfrapesLPNpllKMEKVSAgy 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 -----VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKV-FYEGRDTSTFKSKDLLGFRRHVQPVfqNPYGS 514
Cdd:PRK10636 323 gdriiLDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLRADESPL--QHLAR 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 515 LDPmysifRSIEEPLRIHkIGDKKWRANRVKElldmvempasVMGRYpnelSGGQRQRIAIARAMALDPDVIVCDEAVSA 594
Cdd:PRK10636 401 LAP-----QELEQKLRDY-LGGFGFQGDKVTE----------ETRRF----SGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 595 LDVLVQDQVLRLLNDLQAekglSYLFITHDLAVVRQIADEVVVMQHGKLvehattdEVFDHPQKQYTRDLLDA 667
Cdd:PRK10636 461 LDLDMRQALTEALIDFEG----ALVVVSHDRHLLRSTTDDLYLVHDGKV-------EPFDGDLEDYQQWLSDV 522
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
441-652 |
6.42e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.37 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTvanmvlhLLKPTSGKVFYEGRDTSTFKSKDL--------------LGFRRHV-- 504
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKST-------LLKALAGDLTGGGAPRGARVTGDVtlngeplaaidaprLARLRAVlp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 505 ---QPVFqnPYgSLDPMYSIFR---SIEEPLRIHKIGDKKWRAnrvKELLDmvemPASVMGRYPNELSGGQRQRIAIARA 578
Cdd:PRK13547 90 qaaQPAF--AF-SAREIVLLGRyphARRAGALTHRDGEIAWQA---LALAG----ATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 579 MA---------LDPDVIVCDEAVSALDVLVQDQVLRLLNDLQAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLVEHATT 649
Cdd:PRK13547 160 LAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
...
gi 2545376782 650 DEV 652
Cdd:PRK13547 240 ADV 242
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
418-644 |
6.49e-07 |
|
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: 50.32 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 418 HIITVDHLTKEFKLPRKKEMFkaVDDVSFSVKRGTTLAIVGESGSGKSTVANmVLHLLKpTSGKVfyEGRDTSTFKSKDl 497
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKRQL--LNNISGYVKPGTLTALMGESGAGKTTLLD-VLAGRK-TAGVI--TGEILINGRPLD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 498 LGFRRHVQPVFQNPygSLDPMYsifrSIEEPLRIHkigdkkwranrvkelldmvempASVMGrypneLSGGQRQRIAIAR 577
Cdd:cd03232 75 KNFQRSTGYVEQQD--VHSPNL----TVREALRFS----------------------ALLRG-----LSVEQRKRLTIGV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 578 AMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHD-LAVVRQIADEVVVMQH-GKLV 644
Cdd:cd03232 122 ELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL-ADSGQAILCTIHQpSASIFEKFDRLLLLKRgGKTV 189
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
281-361 |
7.39e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.63 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 281 GMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVESG 360
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDG 237
|
.
gi 2545376782 361 P 361
Cdd:COG4586 238 S 238
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
246-368 |
7.54e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 51.34 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 246 VTGSTMDDRIAGLLSEAGLpdaATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTD 325
Cdd:PRK13537 110 LSAAAARALVPPLLEFAKL---ENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLA 186
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2545376782 326 SlGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQH 368
Cdd:PRK13537 187 R-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
279-366 |
8.39e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.70 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 279 SGGMRQRA-LIAIGLACRPD------LLIADEPTSALDVTvQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVM 351
Cdd:PRK03695 128 SGGEWQRVrLAAVVLQVWPDinpagqLLLLDEPMNSLDVA-QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLL 206
|
90
....*....|....*
gi 2545376782 352 YKGQVVESGPSLEVL 366
Cdd:PRK03695 207 KQGKLLASGRRDEVL 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
273-366 |
8.81e-07 |
|
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: 52.11 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 273 QFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMY 352
Cdd:TIGR03269 423 KYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMR 502
|
90
....*....|....
gi 2545376782 353 KGQVVESGPSLEVL 366
Cdd:TIGR03269 503 DGKIVKIGDPEEIV 516
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
271-362 |
9.43e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 50.78 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 271 ARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVV 350
Cdd:PRK09984 146 AHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVA 225
|
90
....*....|..
gi 2545376782 351 MYKGQVVESGPS 362
Cdd:PRK09984 226 LRQGHVFYDGSS 237
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
279-355 |
1.05e-06 |
|
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: 49.78 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 279 SGGMRQRaliaIGLA----CRPDLLIADEPTSALDVTVQKRILDH--LHMLTDslGTAVLFITHDLGLaAERAQHIVVMY 352
Cdd:cd03250 129 SGGQKQR----ISLAravySDADIYLLDDPLSAVDAHVGRHIFENciLGLLLN--NKTRILVTHQLQL-LPHADQIVVLD 201
|
...
gi 2545376782 353 KGQ 355
Cdd:cd03250 202 NGR 204
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
443-641 |
1.08e-06 |
|
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: 49.24 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVLHllkpTSGKVFYEGrDTSTFkSKDLLGFRRHVQPVFQNPYGSLDPmysif 522
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----ASGKARLIS-FLPKF-SRNKLIFIDQLQFLIDVGLGYLTL----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 523 rsieeplrihkigdkkwranrvkelldmvempasvmGRYPNELSGGQRQRIAIARAMA--LDPDVIVCDEAVSALDvlvQ 600
Cdd:cd03238 82 ------------------------------------GQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLH---Q 122
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2545376782 601 DQVLRLLNDLQA--EKGLSYLFITHDLAVVRQiADEVVVMQHG 641
Cdd:cd03238 123 QDINQLLEVIKGliDLGNTVILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-316 |
1.46e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 27 IDFTTDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLL-----PGTGHV-VNGSIKLDGEEIagakqsef 100
Cdd:PTZ00265 388 VRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKST----ILKLIerlydPTEGDIiINDSHNLKDINL-------- 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 101 dKLRGTKMGLVPQDPMsnlnpvwrigtqvkeaLKANNmdvahekrsalakalagdeveVKGNDDETFLGAKELPELMTEA 180
Cdd:PTZ00265 456 -KWWRSKIGVVSQDPL----------------LFSNS---------------------IKNNIKYSLYSLKDLEALSNYY 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 181 KKALTEAGVSGEAFDKAVARFTNEWvpgsetrwrvaDDLIKAGVADDLIKAG-----VADDQAWYLAKKYVtgstmddrI 255
Cdd:PTZ00265 498 NEDGNDSQENKNKRNSCRAKCAGDL-----------NDMSNTTDSNELIEMRknyqtIKDSEVVDVSKKVL--------I 558
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 256 AGLLSeaGLPDA-ATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALD----VTVQKRI 316
Cdd:PTZ00265 559 HDFVS--ALPDKyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDnkseYLVQKTI 622
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
443-645 |
1.55e-06 |
|
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: 51.87 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTSTFKSKDLlgfRRHVQPVFQNPY---GSLDPMY 519
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL---RFKITIIPQDPVlfsGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 520 SIFRSIEEplrihkigDKKWRANRVKELLDMVE-MPASV---MGRYPNELSGGQRQRIAIARAMALDPDVIVCDEAVSAL 595
Cdd:TIGR00957 1381 DPFSQYSD--------EEVWWALELAHLKTFVSaLPDKLdheCAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 596 DV----LVQDQVLRLLNDlqaekgLSYLFITHDLAVVRQIAdEVVVMQHGKLVE 645
Cdd:TIGR00957 1453 DLetdnLIQSTIRTQFED------CTVLTIAHRLNTIMDYT-RVIVLDKGEVAE 1499
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
273-356 |
1.91e-06 |
|
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: 49.09 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 273 QFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMY 352
Cdd:TIGR01277 124 RLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVS 203
|
....
gi 2545376782 353 KGQV 356
Cdd:TIGR01277 204 QGKI 207
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
278-403 |
2.23e-06 |
|
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: 51.10 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 278 FSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHL----HMLTDSlgTAVLfITHDLGLAAErAQHIVVMYK 353
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpeGVLKNK--TRIL-VTHGISYLPQ-VDVIIVMSG 836
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 354 GQVVESGPSLEVLQHpQHPYTKRLVAAAPS---LASQRIISAKERGEDADALL 403
Cdd:TIGR00957 837 GKISEMGSYQELLQR-DGAFAEFLRTYAPDeqqGHLEDSWTALVSGEGKEAKL 888
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
281-644 |
2.45e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.56 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 281 GMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLfITHDLGLAAERAQHIVVMYKGQVVESg 360
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVLRDGRTIET- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 361 pslevlqhpqhpytkrLVAAAPSLASQRIISAKErGEDadalLDH-------HIaGESTLEKSEHiiTVDHltkefklPR 433
Cdd:NF040905 221 ----------------LDCRADEVTEDRIIRGMV-GRD----LEDrypertpKI-GEVVFEVKNW--TVYH-------PL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 434 KKEMfKAVDDVSFSVKRGTTLAIVGESGSGKSTVAnMVL---HLLKPTSGKVFYEGR--DTSTFK----------SKDll 498
Cdd:NF040905 270 HPER-KVVDDVSLNVRRGEIVGIAGLMGAGRTELA-MSVfgrSYGRNISGTVFKDGKevDVSTVSdaidaglayvTED-- 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 499 gfRRHvqpvfqnpYGsLDPMYSIFRSIEEPlRIHKIGDKKWrANRVKELLDMVEMPASVMGRYPN------ELSGGQRQR 572
Cdd:NF040905 346 --RKG--------YG-LNLIDDIKRNITLA-NLGKVSRRGV-IDENEEIKVAEEYRKKMNIKTPSvfqkvgNLSGGNQQK 412
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2545376782 573 IAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLLNDLqAEKGLSYLFITHDLAVVRQIADEVVVMQHGKLV 644
Cdd:NF040905 413 VVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
266-360 |
2.90e-06 |
|
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: 48.41 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 266 DAATRAR--QFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFIthdLGLAAE 343
Cdd:cd03233 105 DFALRCKgnEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVS---LYQASD 181
|
90 100
....*....|....*....|.
gi 2545376782 344 RA----QHIVVMYKGQVVESG 360
Cdd:cd03233 182 EIydlfDKVLVLYEGRQIYYG 202
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-81 |
2.91e-06 |
|
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: 47.92 E-value: 2.91e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 20 LEVKDLAIdfTTDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLP-GTGHVV 81
Cdd:cd03223 1 IELENLSL--ATPDGRVL--LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPwGSGRIG 59
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
38-92 |
3.21e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.80 E-value: 3.21e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 38 HAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvVNGSIKLDGEEI 92
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTP--VAGCVDVPDNQF 96
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
39-103 |
4.16e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.97 E-value: 4.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 39 AVRDANFTVYPGQWVAIVGESGSGKSTSAMavlgLLPGTGHVVNGSIKLDGEEIAGAKQSEFDKL 103
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAM----LLTGLYQPQSGEILLDGKPVTAEQPEDYRKL 398
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-89 |
5.81e-06 |
|
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: 47.91 E-value: 5.81e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 16 HGPLLEVKDLAIDFTTDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTsamaVLGLLPGTGHVVNGSIKLDG 89
Cdd:cd03220 14 KGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKST----LLRLLAGIYPPDSGTVTVRG 83
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
357-402 |
5.83e-06 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 44.31 E-value: 5.83e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2545376782 357 VESGPSLEVLQHPQHPYTKRLVAAAPSLASQRIISAKERGEDADAL 402
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLL 46
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
279-473 |
6.27e-06 |
|
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: 49.63 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 279 SGGMRQRALIA--IGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDsLGTAVLFITHDLGlAAERAQHIVVM----- 351
Cdd:TIGR00630 490 SGGEAQRIRLAtqIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHDED-TIRAADYVIDIgpgag 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 352 -YKGQVVESGPSLEVLQHPQhpytkrlvaaapSLASQriisakergedadalldhHIAGESTLEksehiitvdhlTKEFK 430
Cdd:TIGR00630 568 eHGGEVVASGTPEEILANPD------------SLTGQ------------------YLSGRKKIE-----------VPAER 606
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2545376782 431 LPRKKEMFKAVD-------DVSFSVKRGTTLAIVGESGSGKSTVANMVLH 473
Cdd:TIGR00630 607 RPGNGKFLTLKGarennlkNITVSIPLGLFTCITGVSGSGKSTLINDTLY 656
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
279-624 |
7.17e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 279 SGGMRQR-ALiaiglaCR-----PDLLIADEPTSALDV-TVQ--KRildHLHmltDSLGTaVLFITHD---LGLAAE--- 343
Cdd:PRK11819 165 SGGERRRvAL------CRlllekPDMLLLDEPTNHLDAeSVAwlEQ---FLH---DYPGT-VVAVTHDryfLDNVAGwil 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 344 ---RAQHIVvmYKG-------------QVVESGPS---------LE-VLQHPQHPYTK---RLvAAAPSLASQriiSAKE 394
Cdd:PRK11819 232 eldRGRGIP--WEGnysswleqkakrlAQEEKQEAarqkalkreLEwVRQSPKARQAKskaRL-ARYEELLSE---EYQK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 395 RGEDADAlldhHI-AGESTLEKsehIITVDHLTKEF--KLprkkemfkAVDDVSFSVKRGTTLAIVGESGSGKSTVANMV 471
Cdd:PRK11819 306 RNETNEI----FIpPGPRLGDK---VIEAENLSKSFgdRL--------LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMI 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 472 LHLLKPTSGKVfyegRDTSTFKskdlLGFrrhvqpVFQNpYGSLDPMYSIFRSIEEPLRIHKIGDkkwranrvkelldmV 551
Cdd:PRK11819 371 TGQEQPDSGTI----KIGETVK----LAY------VDQS-RDALDPNKTVWEEISGGLDIIKVGN--------------R 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 552 EMPA-SVMGRYpN-----------ELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVlvqdQVLRLLNDLQAEKGLSYL 619
Cdd:PRK11819 422 EIPSrAYVGRF-NfkggdqqkkvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV----ETLRALEEALLEFPGCAV 496
|
....*
gi 2545376782 620 FITHD 624
Cdd:PRK11819 497 VISHD 501
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
253-370 |
7.47e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 47.72 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 DRIAGLLSEAGLpdaATRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALD-VTVQ--KRILDHLHmltdSLGT 329
Cdd:COG1137 115 ERLEELLEEFGI---THLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpIAVAdiQKIIRHLK----ERGI 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2545376782 330 AVLfIT-HD----LGLaAERAqhiVVMYKGQVVESGPSLEVLQHPQ 370
Cdd:COG1137 188 GVL-ITdHNvretLGI-CDRA---YIISEGKVLAEGTPEEILNNPL 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
279-336 |
9.27e-06 |
|
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: 46.78 E-value: 9.27e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITH 336
Cdd:cd03213 113 SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIH 169
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
448-639 |
9.28e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.80 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 448 VKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGrdtstfkskdllgfrrhVQPVFQNPYGSLdpmysifrsiee 527
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-----------------ITPVYKPQYIDL------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 528 plrihkigdkkwranrvkelldmvempasvmgrypnelSGGQRQRIAIARAMALDPDVIVCDEAVSALDVLVQDQVLRLL 607
Cdd:cd03222 73 --------------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180 190
....*....|....*....|....*....|..
gi 2545376782 608 NDLQAEKGLSYLFITHDLAVVRQIADEVVVMQ 639
Cdd:cd03222 115 RRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
253-337 |
1.07e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.02 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 253 DRIAGLLSEAGLPDaaTRARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVL 332
Cdd:PRK10247 115 AIFLDDLERFALPD--TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVL 192
|
....*
gi 2545376782 333 FITHD 337
Cdd:PRK10247 193 WVTHD 197
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
252-366 |
1.14e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 47.69 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 252 DDRIAGLLSEAGLPDAATRARQFPHE-FSGGMRQRALIAIGLACRPDLLIADEPTSALD-------VTVQKRILDHlhml 323
Cdd:PRK13638 110 EAEITRRVDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrtqmIAIIRRIVAQ---- 185
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2545376782 324 tdslGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVL 366
Cdd:PRK13638 186 ----GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-129 |
1.26e-05 |
|
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: 48.75 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIDFTTDtGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPgtghvVNGSIKLDGEEIAGAKQSE 99
Cdd:TIGR01271 1218 MDVQGLTAKYTEA-GRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-----TEGEIQIDGVSWNSVTLQT 1289
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2545376782 100 FDKlrgtKMGLVPQDPM-------SNLNP--------VWRIGTQV 129
Cdd:TIGR01271 1290 WRK----AFGVIPQKVFifsgtfrKNLDPyeqwsdeeIWKVAEEV 1330
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
416-624 |
1.27e-05 |
|
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: 48.39 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 416 SEHIITVDHLTKEFklPRKKEMFKavdDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGkvfyEGRDTSTFKSK 495
Cdd:TIGR03719 1 AQYIYTMNRVSKVV--PPKKEILK---DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----EARPQPGIKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 496 DLLgfrrhvqpvfQNPYgsLDPMYSIFRSIEEPLRihKIGDKKWRANRVKELL-----DM-------------------- 550
Cdd:TIGR03719 72 YLP----------QEPQ--LDPTKTVRENVEEGVA--EIKDALDRFNEISAKYaepdaDFdklaaeqaelqeiidaadaw 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 551 -----VEMPASVMgRYP------NELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVlvqDQVLRLLNDLQAEKGlSYL 619
Cdd:TIGR03719 138 dldsqLEIAMDAL-RCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESVAWLERHLQEYPG-TVV 212
|
....*
gi 2545376782 620 FITHD 624
Cdd:TIGR03719 213 AVTHD 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
277-361 |
1.56e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 47.52 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTdSLGTAVLFITHDLGLAAERAQHIVVMYKG-Q 355
Cdd:PRK13536 172 DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGrK 250
|
....*.
gi 2545376782 356 VVESGP 361
Cdd:PRK13536 251 IAEGRP 256
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-115 |
1.77e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.79 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAidFTTDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPgtghVVNGSIKLDGEEIAGAKQSe 99
Cdd:PRK10790 341 IDIDNVS--FAYRDDNLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP----LTEGEIRLDGRPLSSLSHS- 411
|
90
....*....|....*..
gi 2545376782 100 fdKLR-GTKMglVPQDP 115
Cdd:PRK10790 412 --VLRqGVAM--VQQDP 424
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
278-368 |
2.01e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 278 FSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKGQVV 357
Cdd:PRK13545 144 YSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVK 222
|
90
....*....|.
gi 2545376782 358 ESGPSLEVLQH 368
Cdd:PRK13545 223 EYGDIKEVVDH 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-93 |
2.43e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 46.25 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 14 KEHGPLLEVKDlaIDFTTDTGKPVHAVrdaNFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEIA 93
Cdd:PRK10247 2 QENSPLLQLQN--VGYLAGDAKILNNI---SFSLRAGEFKLITGPSGCGKSTLLKIVASLISPT----SGTLLFEGEDIS 72
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-92 |
3.50e-05 |
|
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: 47.10 E-value: 3.50e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 20 LEVKDLAIDFTTDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEI 92
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPES----GEILLDGQPV 396
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
250-369 |
4.05e-05 |
|
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: 45.61 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 250 TMDDRIAGLLSEAGLPDA--ATRARQFPHEF-------------SGGMRQRALIAIGLACRPDLLIADEPTSALD-VTVQ 313
Cdd:cd03218 91 TVEENILAVLEIRGLSKKerEEKLEELLEEFhithlrkskasslSGGERRRVEIARALATNPKFLLLDEPFAGVDpIAVQ 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 314 --KRILDHLHmltdSLGTAVLFITHDLGLAAERAQHIVVMYKGQVVESGPSLEVLQHP 369
Cdd:cd03218 171 diQKIIKILK----DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
271-372 |
4.90e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.53 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 271 ARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVV 350
Cdd:PRK11831 137 AKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYI 216
|
90 100
....*....|....*....|..
gi 2545376782 351 MYKGQVVESGpSLEVLQHPQHP 372
Cdd:PRK11831 217 VADKKIVAHG-SAQALQANPDP 237
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
355-384 |
6.01e-05 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 41.96 E-value: 6.01e-05
10 20 30
....*....|....*....|....*....|
gi 2545376782 355 QVVESGPSLEVLQHPQHPYTKRLVAAAPSL 384
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTI 30
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-83 |
7.75e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.46 E-value: 7.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 13 QKEHGPLLEVKDLaidFTTDTgKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSaMAVL-GLL-PGTGHV-VNG 83
Cdd:COG4586 15 EKEPGLKGALKGL---FRREY-REVEAVDDISFTIEPGEIVGFIGPNGAGKSTT-IKMLtGILvPTSGEVrVLG 83
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
442-632 |
8.08e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 44.02 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 442 DDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEGRDTST----FKSKDL-LGFRRHVQPVfqnpygsLD 516
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRqrdeYHQDLLyLGHQPGIKTE-------LT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 517 PmysifrsiEEPLRI-HKIG-----DKKWRAnrvkelLDMV------EMPASVmgrypneLSGGQRQRIAIARAMALDPD 584
Cdd:PRK13538 91 A--------LENLRFyQRLHgpgddEALWEA------LAQVglagfeDVPVRQ-------LSAGQQRRVALARLWLTRAP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 585 VIVCDEAVSALDVLVQDQVLRLLnDLQAEKGLSYLFITH-DLAV----VRQIA 632
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALL-AQHAEQGGMVILTTHqDLPVasdkVRKLR 201
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
279-353 |
8.62e-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: 43.50 E-value: 8.62e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 279 SGGMRQRALIAIGLA---CRPD-LLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLaAERAQHIVVMYK 353
Cdd:cd03227 79 SGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPEL-AELADKLIHIKK 155
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
277-368 |
1.04e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 277 EFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLAAERAQHIVVMYKGQV 356
Cdd:PRK13546 143 KYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
90
....*....|..
gi 2545376782 357 VESGPSLEVLQH 368
Cdd:PRK13546 222 KDYGELDDVLPK 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
40-124 |
1.24e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 40 VRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLpgtgHVVNGSIKLDGEEIAGAKQSEfdkLRgTKMGLVPQDPM--- 116
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMV----EVCGGEIRVNGREIGAYGLRE---LR-RQFSMIPQDPVlfd 1397
|
90 100
....*....|....*....|
gi 2545376782 117 ----SNLNP--------VWR 124
Cdd:PTZ00243 1398 gtvrQNVDPfleassaeVWA 1417
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-84 |
1.60e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 44.67 E-value: 1.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2545376782 18 PLLEVKDLAIDFTtdtGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLL-PGTGHVVNGS 84
Cdd:COG0488 314 KVLELEGLSKSYG---DKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELePDSGTVKLGE 376
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
44-123 |
1.61e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 43.77 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 44 NFTVYPGQWVAIVGESGSGKST--SAMAvlGLLPGTghvvnGSIKLDGEEIAGAKQSEFDKLRGTkmgLVPQDPMSNLNP 121
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTllARMA--GLLPGS-----GSIQFAGQPLEAWSAAELARHRAY---LSQQQTPPFAMP 85
|
..
gi 2545376782 122 VW 123
Cdd:PRK03695 86 VF 87
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
226-361 |
1.62e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.04 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 226 DDL-IKAGVADDQAWYLA----KKYVTGSTMDDRIAGLLSEAGLPDAATRARQFPHE---FSGGMRQRALIAIGLACRPD 297
Cdd:TIGR00955 107 DDLfIPTLTVREHLMFQAhlrmPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPP 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2545376782 298 LLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFI---THDLglaAERAQHIVVMYKGQVVESGP 361
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIhqpSSEL---FELFDKIILMAEGRVAYLGS 250
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-89 |
1.78e-04 |
|
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: 44.07 E-value: 1.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 20 LEVKDLAIDFTtDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPgtghvVNGSIKLDG 89
Cdd:cd03289 3 MTVKDLTAKYT-EGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-----TEGDIQIDG 64
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-113 |
1.94e-04 |
|
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: 45.00 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAIDFTTdTGKPvhAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEIagakQ 97
Cdd:TIGR01257 927 PGVCVKNLVKIFEP-SGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT----SGTVLVGGKDI----E 995
|
90
....*....|....*.
gi 2545376782 98 SEFDKLRGTkMGLVPQ 113
Cdd:TIGR01257 996 TNLDAVRQS-LGMCPQ 1010
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
278-370 |
2.18e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 43.34 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 278 FSGGMRQRALIAIGLACRPDLLIADEPTSALD---VTVQKRILDHLHmltDSlGTAVLFITHDLGLAAERAQHIVVMYKG 354
Cdd:PRK10895 138 LSGGERRRVEIARALAANPKFILLDEPFAGVDpisVIDIKRIIEHLR---DS-GLGVLITDHNVRETLAVCERAYIVSQG 213
|
90
....*....|....*.
gi 2545376782 355 QVVESGPSLEVLQHPQ 370
Cdd:PRK10895 214 HLIAHGTPTEILQDEH 229
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
279-331 |
3.38e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 43.71 E-value: 3.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAV 331
Cdd:PLN03211 208 SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIV 260
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
279-309 |
3.46e-04 |
|
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: 42.64 E-value: 3.46e-04
10 20 30
....*....|....*....|....*....|.
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTSALD 309
Cdd:cd03234 145 SGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
20-84 |
3.53e-04 |
|
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: 41.28 E-value: 3.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2545376782 20 LEVKDLAIDFTtdtGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLG-LLPGTGHVVNGS 84
Cdd:cd03221 1 IELENLSKTYG---GKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGeLEPDEGIVTWGS 61
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
279-401 |
4.50e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.61 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLfITHDLGLAAeRAQHIVVMYKGQVVE 358
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVL-ATHQVHVVP-RADYVVALGDGRVEF 861
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2545376782 359 SGPSLEVLQHPQHpytkrlvaaaPSLASQRIISAKERGEDADA 401
Cdd:PTZ00243 862 SGSSADFMRTSLY----------ATLAAELKENKDSKEGDADA 894
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
278-381 |
4.53e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 278 FSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGlAAERAQHIVVM----YK 353
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVVFnnpdRT 1437
|
90 100
....*....|....*....|....*...
gi 2545376782 354 GQVVESGPSLEVLQHPQHPYTKRLVAAA 381
Cdd:PTZ00265 1438 GSFVQAHGTHEELLSVQDGVYKKYVKLA 1465
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
40-121 |
5.16e-04 |
|
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: 43.40 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 40 VRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGEEIAgakQSEFDKLRgTKMGLVPQDPM--- 116
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA----EGEIIIDGLNIA---KIGLHDLR-FKITIIPQDPVlfs 1373
|
....*....
gi 2545376782 117 ----SNLNP 121
Cdd:TIGR00957 1374 gslrMNLDP 1382
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
34-92 |
5.26e-04 |
|
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: 41.87 E-value: 5.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 34 GKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhVVNGSIKLDGEEI 92
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGG-TTSGQILFNGQPR 74
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
420-651 |
5.94e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 420 ITVDHLTKEFKlprKKEMFKavdDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVF--------YEGRDTST 491
Cdd:PRK15064 320 LEVENLTKGFD---NGPLFK---NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsenanigYYAQDHAY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 492 FKSKDLLGFrrhvqpvfqnpygslDPMYsifrsieeplrihkigdkKWRANRVKELldMVEmpaSVMGRY---------- 561
Cdd:PRK15064 394 DFENDLTLF---------------DWMS------------------QWRQEGDDEQ--AVR---GTLGRLlfsqddikks 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 562 PNELSGGQRQRIAIARAMALDPDVIVCDEAVSALDVlvqDQVLRLLNDLQAEKGlSYLFITHDLAVVRQIADEVVVMQHG 641
Cdd:PRK15064 436 VKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM---ESIESLNMALEKYEG-TLIFVSHDREFVSSLATRIIEITPD 511
|
250
....*....|.
gi 2545376782 642 KLVE-HATTDE 651
Cdd:PRK15064 512 GVVDfSGTYEE 522
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
40-98 |
6.55e-04 |
|
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: 41.48 E-value: 6.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 40 VRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGHvVNGSIKLDGEEIAGAKQS 98
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS-VEGDIHYNGIPYKEFAEK 80
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
48-97 |
6.89e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 42.73 E-value: 6.89e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2545376782 48 YPGQWVAIVGESGSGKSTsAMAVLGLLPGTGHVVNGSIKLDGEEIaGAKQ 97
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTT-LMNALAFRSPKGVKGSGSVLLNGMPI-DAKE 96
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
644-669 |
7.04e-04 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 38.54 E-value: 7.04e-04
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
18-92 |
7.24e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.94 E-value: 7.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 18 PLLEVKDLAIdfTTDTGKPVHAVrdaNFTVYPGQWVAIVGESGSGKSTSAMAVlgllpgTGH----VVNGSIKLDGEEI 92
Cdd:CHL00131 6 PILEIKNLHA--SVNENEILKGL---NLSINKGEIHAIMGPNGSGKSTLSKVI------AGHpaykILEGDILFKGESI 73
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-121 |
1.07e-03 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 41.74 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 24 DLAIDFTTDT----GKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLL-PGTGHVVngsikldgeeIAGAKQS 98
Cdd:PRK13536 39 TVAIDLAGVSksygDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTsPDAGKIT----------VLGVPVP 106
|
90 100
....*....|....*....|...
gi 2545376782 99 EFDKLRGTKMGLVPQdpMSNLNP 121
Cdd:PRK13536 107 ARARLARARIGVVPQ--FDNLDL 127
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-92 |
1.10e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 1.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2545376782 19 LLEVKDLAIDFTTDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGllPGTGHVVNGSIKLDGEEI 92
Cdd:NF040905 257 VFEVKNWTVYHPLHPERKV--VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG--RSYGRNISGTVFKDGKEV 326
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
272-355 |
1.14e-03 |
|
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: 41.24 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 272 RQFPhEFSGGMRQRALIAIGLACRPDLLIADEPTSALDV-------TVQKRILDHlhmlTDSlgTAvLFITHDLGLAAER 344
Cdd:cd03237 111 REVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlmasKVIRRFAEN----NEK--TA-FVVEHDIIMIDYL 182
|
90
....*....|.
gi 2545376782 345 AQHIVVmYKGQ 355
Cdd:cd03237 183 ADRLIV-FEGE 192
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
276-348 |
1.16e-03 |
|
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: 40.55 E-value: 1.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2545376782 276 HEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHI 348
Cdd:cd03231 124 AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
441-605 |
1.17e-03 |
|
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: 41.38 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 441 VDDVSFSVKRGTTLAIVGESGSGKSTVANMVLHLLKpTSGKVFYEGrdtSTFKSKDLLGFRRHVQPVFQNPYgsldpmys 520
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG---VSWNSVPLQKWRKAFGVIPQKVF-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 521 IFRSieePLRIHKIGDKKWRANRVKELLDMVEMpASVMGRYPNE-----------LSGGQRQRIAIARAMALDPDVIVCD 589
Cdd:cd03289 88 IFSG---TFRKNLDPYGKWSDEEIWKVAEEVGL-KSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLD 163
|
170
....*....|....*.
gi 2545376782 590 EAVSALDVlVQDQVLR 605
Cdd:cd03289 164 EPSAHLDP-ITYQVIR 178
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
279-369 |
1.25e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.01 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 279 SGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDslGTAVLFITHDLGLAAErAQHIVVMYKGQVVE 358
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQ 529
|
90
....*....|.
gi 2545376782 359 SGPSLEVLQHP 369
Cdd:PRK10789 530 RGNHDQLAQQS 540
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-92 |
1.75e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 40.24 E-value: 1.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2545376782 18 PLLEVKDLAIdftTDTGKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTGhvvnGSIKLDGEEI 92
Cdd:PRK13539 1 MMLEGEDLAC---VRGGRVL--FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAA----GTIKLDGGDI 66
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
53-92 |
1.78e-03 |
|
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: 39.28 E-value: 1.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2545376782 53 VAIVGESGSGKSTSAMAVLGLLPGTGHVVngsIKLDGEEI 92
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGV---IYIDGEDI 41
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
256-363 |
1.80e-03 |
|
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: 41.92 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 256 AGLLSEAGLPDAAT--RARQFPHEFSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLhmLTDSLGTAVLF 333
Cdd:TIGR01257 1038 AQLEMEAMLEDTGLhhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIM 1115
|
90 100 110
....*....|....*....|....*....|
gi 2545376782 334 ITHDLGLAAERAQHIVVMYKGQVVESGPSL 363
Cdd:TIGR01257 1116 STHHMDEADLLGDRIAIISQGRLYCSGTPL 1145
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
283-309 |
2.28e-03 |
|
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: 39.53 E-value: 2.28e-03
10 20
....*....|....*....|....*..
gi 2545376782 283 RQRALIAIGLACRPDLLIADEPTSALD 309
Cdd:cd03232 114 RKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-116 |
2.37e-03 |
|
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: 40.28 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 17 GPLLEVKDLAIDFTTDTgKPVhaVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLpgtgHVVNGSIKLDGEEIAgak 96
Cdd:cd03288 17 GGEIKIHDLCVRYENNL-KPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMV----DIFDGKIVIDGIDIS--- 86
|
90 100
....*....|....*....|
gi 2545376782 97 QSEFDKLRgTKMGLVPQDPM 116
Cdd:cd03288 87 KLPLHTLR-SRLSIILQDPI 105
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
278-360 |
3.02e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.77 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 278 FSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSLGTAVLFITHDLGLAAERAQHIVVMYKGQVV 357
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIV 225
|
...
gi 2545376782 358 ESG 360
Cdd:PRK09580 226 KSG 228
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
278-360 |
3.98e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 39.63 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 278 FSGGMRQRALIAIGLACRPDLLIADEPTSALDVTVQKRILDHLHMLTDSlGTAVLFITHDLGLaaerAQHIV-----VMY 352
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRL----LDYIKpdyvhVMQ 226
|
....*...
gi 2545376782 353 KGQVVESG 360
Cdd:CHL00131 227 NGKIIKTG 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
278-396 |
4.01e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.73 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 278 FSGGMRQRALIAIGLACRPDLLIADEPTSALDVT----VQKRILDHLHMLTdslgtaVLFITHDLGLAAErAQHIVVMYK 353
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRtdslIQRTIREEFKSCT------MLVIAHRLNTIID-CDKILVLSS 1444
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2545376782 354 GQVVESGPSLEVLQHPQHPYTKRLVAAAPSLA---SQRIISAKERG 396
Cdd:PLN03232 1445 GQVLEYDSPQELLSRDTSAFFRMVHSTGPANAqylSNLVFERRENG 1490
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
47-92 |
4.76e-03 |
|
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: 38.76 E-value: 4.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2545376782 47 VYPGQWVAIVGESGSGKSTsamaVLGLLPG--TGHVVNGSIKLDGEEI 92
Cdd:cd03232 30 VKPGTLTALMGESGAGKTT----LLDVLAGrkTAGVITGEILINGRPL 73
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-90 |
5.06e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 5.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2545376782 22 VKDLAIDFttDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGLLPGTghvvNGSIKLDGE 90
Cdd:PRK13546 24 MKDALIPK--HKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPT----VGKVDRNGE 86
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
443-670 |
5.56e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.21 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 443 DVSFSVKRGTTLAIVGESGSGKSTVANMVlhllkptsgkvfyEGRDTSTFKSKDLL--GFRRhVQPVFQNPYG------- 513
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVL-------------AGRKTGGYIEGDIRisGFPK-KQETFARISGyceqndi 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 514 ---------SLdpMYSIFrsieepLRIHKIGDKKWRANRVKELLDMVEMPA---SVMGrYP--NELSGGQRQRIAIARAM 579
Cdd:PLN03140 964 hspqvtvreSL--IYSAF------LRLPKEVSKEEKMMFVDEVMELVELDNlkdAIVG-LPgvTGLSTEQRKRLTIAVEL 1034
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 580 ALDPDVIVCDEAVSALDVLVQDQVLRLLNDlQAEKGLSYLFITHDLAV-VRQIADEVVVMQHGKLVEHATTDEVFDHPQK 658
Cdd:PLN03140 1035 VANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSIdIFEAFDELLLMKRGGQVIYSGPLGRNSHKII 1113
|
250
....*....|..
gi 2545376782 659 QYtrdlLDAIPG 670
Cdd:PLN03140 1114 EY----FEAIPG 1121
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-110 |
7.75e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.49 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 18 PLLEVKDLAidFTTDTGKPVHAVRDANFTVYPGQWVAIVGESGSGKSTSAMAVLGL-LPGTGHV-VNGSIKLDG------ 89
Cdd:PRK13545 20 PFDKLKDLF--FRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPNKGTVdIKGSAALIAissgln 97
|
90 100
....*....|....*....|.
gi 2545376782 90 EEIAGAKQSEfdkLRGTKMGL 110
Cdd:PRK13545 98 GQLTGIENIE---LKGLMMGL 115
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
44-90 |
9.49e-03 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 38.41 E-value: 9.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2545376782 44 NFTVYPGQWVAIVGESGSGKST--SAMAvlGLLPGTGhvvnGSIKLDGE 90
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTllNLIA--GFLTPAS----GSLTLNGQ 61
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
445-548 |
9.72e-03 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 38.74 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2545376782 445 SFSVKRGTTLAIVGESGSGKSTVANMVLHLLKPTSGKVFYEgrdtstFkskdllgfrrhvqpvfqNPY---GSLDPMYSI 521
Cdd:COG4928 23 SSDADEPLVIGLDGEWGSGKTSFLNLIEKELESNEKVIVVY------F-----------------NAWlydGEEDLLAAL 79
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90 100
....*....|....*....|....*..
gi 2545376782 522 FRSIEEplrihKIGDKKWRANRVKELL 548
Cdd:COG4928 80 LSEIAA-----ELEKKKKKDKKAAKKL 101
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