|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-572 |
0e+00 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 1003.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 1 MRALLPYLALYKRHKWLLSLGVVLAIVTLLASIGLLTLSGWFLSASAVVGMAGLYSFNYMLPAAGVRGAAIIRTAGRYFE 80
Cdd:PRK11160 1 MRALLPFLKLYKRHWFMLSLGILLAIVTLLASIGLLTLSGWFLSASAVAGLAGLYSFNYMLPAAGVRGAAIGRTAGRYGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 81 RLVSHEGTFRVLEHLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLDV 160
Cdd:PRK11160 81 RLVSHDATFRVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 161 TLALTLGGIMLATLLLLPPLFYRAGRPVGEALTMLRASYRQQLTGWLQGQAELSIFGAAGRYREQLDTTEQVWHEAQRRQ 240
Cdd:PRK11160 161 TLALTLGGILLLLLLLLPLLFYRLGKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 241 AGLTALSQAMMTLISGMTVVLILWMAAGGVGGNSTPGSLIALFVFCALAAFEALAPVGGAFQHLGQVIASARRVSDVIDQ 320
Cdd:PRK11160 241 ANLTGLSQALMILANGLTVVLMLWLAAGGVGGNAQPGALIALFVFAALAAFEALMPVAGAFQHLGQVIASARRINEITEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 321 PADITFAESGKDAPREASLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLD 400
Cdd:PRK11160 321 KPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 401 GVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLD-DEGLNAWLGEGGRQLSGGE 479
Cdd:PRK11160 401 GQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLEdDKGLNAWLGEGGRQLSGGE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 480 LRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKEL 559
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
570
....*....|...
gi 495163667 560 LAQQGRYYQFRAR 572
Cdd:PRK11160 561 LAQQGRYYQLKQR 573
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-572 |
0e+00 |
|
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: 750.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 2 RALLPYLALYKRHKWLLSLGVVLAIVTLLASIGLLTLSGWFLSASAVVGMAglysFNYMLPAAGVRGAAIIRTAGRYFER 81
Cdd:COG4987 1 RDLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPPI----LNLFVPIVGVRAFAIGRTVFRYLER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 82 LVSHEGTFRVLEHLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLDVT 161
Cdd:COG4987 77 LVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 162 LALTLGGIMLATLLLLPPLFYRAGRPVGEALTMLRASYRQQLTGWLQGQAELSIFGAAGRYREQLDTTEQVWHEAQRRQA 241
Cdd:COG4987 157 LALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 242 GLTALSQAMMTLISGMTVVLILWMAAGGVGGNSTPGSLIALFVFCALAAFEALAPVGGAFQHLGQVIASARRVSDVIDQP 321
Cdd:COG4987 237 RLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 322 ADITFAESGKDAPREASLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDG 401
Cdd:COG4987 317 PAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 402 VSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLDD--EGLNAWLGEGGRQLSGGE 479
Cdd:COG4987 397 VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAAlpDGLDTWLGEGGRRLSGGE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 480 LRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKEL 559
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
570
....*....|...
gi 495163667 560 LAQQGRYYQFRAR 572
Cdd:COG4987 557 LAQNGRYRQLYQR 569
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-533 |
9.69e-173 |
|
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: 499.96 E-value: 9.69e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 4 LLPYLALYKRHKWLLSLGVVLAIVTLLASIGLLTLSGWFLSASAVVGmAGLYsfnYMLPAAGVRGAAIIRTAGRYFERLV 83
Cdd:TIGR02868 1 LLRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMP-PVLY---LSVAAVAVRAFGIGRAVFRYLERLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 84 SHEGTFRVLEHLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLDVTLA 163
Cdd:TIGR02868 77 GHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 164 LTLGGIMLATLLLLPPLFYRAGRPVGEALTMLRASYRQQLTGWLQGQAELSIFGAAGRYREQLDTTEQVWHEAQRRQAGL 243
Cdd:TIGR02868 157 LILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 244 TALSQAMMTLISGMTVVLILWMAAGGVGGNSTPGSLIALFVFCALAAFEALAPVGGAFQHLGQVIASARRVSDVIDQP-- 321
Cdd:TIGR02868 237 TALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAgp 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 322 -ADITFAESGKDAPREASLSLRNVSFSYPGQPqPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLD 400
Cdd:TIGR02868 317 vAEGSAPAAGAVGLGKPTLELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 401 GVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLDD--EGLNAWLGEGGRQLSGG 478
Cdd:TIGR02868 396 GVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRAlpDGLDTVLGEGGARLSGG 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 479 ELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRL 533
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-569 |
1.72e-133 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 401.08 E-value: 1.72e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 1 MRALLPYLalyKRHKWLLSLGVVLAIVTLLASIGLLTLSGWFL-SASAVVGMAGLYSFnymlpAAGVRGAAIIRTAGRYF 79
Cdd:COG1132 9 LRRLLRYL---RPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGDLSALLLL-----LLLLLGLALLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 80 ERLVSHEGTFRVLEHLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLD 159
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 160 VTLALTLGgIMLATLLLLPPLFYRAGRPVGEALTMLRASYRQQLTGWLQGQAELSIFGAAGRYREQLDTTEQVWHEAQRR 239
Cdd:COG1132 161 WRLALIVL-LVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 240 QAGLTALSQAMMTLISGMTVVLILWMAAGGV-GGNSTPGSLIAlFVFCALAAFEALAPVGGAFQHLGQVIASARRVSDVI 318
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLVlSGSLTVGDLVA-FILYLLRLFGPLRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 319 DQPADITFAESGKDAPR-EASLSLRNVSFSYPGQpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDV 397
Cdd:COG1132 319 DEPPEIPDPPGAVPLPPvRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 398 MLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLDD--EGLNAWLGEGGRQL 475
Cdd:COG1132 398 LIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEAlpDGYDTVVGERGVNL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 476 SGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGS 555
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570
....*....|....
gi 495163667 556 HKELLAQQGRYYQF 569
Cdd:COG1132 558 HEELLARGGLYARL 571
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
25-314 |
1.81e-130 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 382.98 E-value: 1.81e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 25 AIVTLLASIGLLTLSGWFLSASAVVGMAGlYSFNYMLPAAGVRGAAIIRTAGRYFERLVSHEGTFRVLEHLRVYTFSRLL 104
Cdd:cd18585 1 GLLTLLASIGLLALSGWFISAAALAGLAA-PTFNYFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 105 PLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLDVTLALTLGGIMLATLLLLPPLFYRA 184
Cdd:cd18585 80 PLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 185 GRPVGEALTMLRASYRQQLTGWLQGQAELSIFGAAGRYREQLDTTEQVWHEAQRRQAGLTALSQAMMTLISGMTVVLILW 264
Cdd:cd18585 160 GKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 495163667 265 MAAGGVGGNSTPGSLIALFVFCALAAFEALAPVGGAFQHLGQVIASARRV 314
Cdd:cd18585 240 LGAPLVQNGALDGALLAMLVFAVLASFEAVAPLPLAFQYLGETRAAARRL 289
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-572 |
4.60e-108 |
|
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: 339.50 E-value: 4.60e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 2 RALLPYLALYKRH-KWLLSLGVVLAIVTLLASIGLLTLSGWFLSASA-------VVGMAGLYSFNYMLpaAGVRGAAIIR 73
Cdd:COG2274 145 RWFLRLLRRYRRLlLQVLLASLLINLLALATPLFTQVVIDRVLPNQDlstlwvlAIGLLLALLFEGLL--RLLRSYLLLR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 74 TAGRYFERLVSHegtfrvlehlrvyTFSRLLPLSPSGLARFRQGELLNRlVADVDTLDHLylrVISPLIGALA--VIAVV 151
Cdd:COG2274 223 LGQRIDLRLSSR-------------FFRHLLRLPLSFFESRSVGDLASR-FRDVESIREF---LTGSLLTALLdlLFVLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 152 TLG-LSLLDVTLALtlggIMLATLLLLPPLFYRAGRPVGEAL-TMLRASYRQQltGWL----QGQAELSIFGAAGRYREQ 225
Cdd:COG2274 286 FLIvLFFYSPPLAL----VVLLLIPLYVLLGLLFQPRLRRLSrEESEASAKRQ--SLLvetlRGIETIKALGAESRFRRR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 226 LDTTEQVWHEAQRRQAGLTALSQAMMTLISGMTVVLILWMAAGGV-GGNSTPGSLIAlfvfCALAAFEALAPVG---GAF 301
Cdd:COG2274 360 WENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLViDGQLTLGQLIA----FNILSGRFLAPVAqliGLL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 302 QHLGQVIASARRVSDVIDQPADITFAESGKDAPR-EASLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKS 380
Cdd:COG2274 436 QRFQDAKIALERLDDILDLPPEREEGRSKLSLPRlKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 381 TLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLD 460
Cdd:COG2274 516 TLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIE 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 461 D--EGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTA 538
Cdd:COG2274 596 AlpMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRL 675
|
570 580 590
....*....|....*....|....*....|....
gi 495163667 539 FDRIIVMDNGQITEQGSHKELLAQQGRYYQFRAR 572
Cdd:COG2274 676 ADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-564 |
1.36e-101 |
|
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: 318.24 E-value: 1.36e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 1 MRALLPYL-ALYKRHKWLLSLGVVLAIVTLLASIGLLTLSGWFLSAsAVVGMAGLYSFnyMLPAAGVRGAAIIRTAGRYF 79
Cdd:COG4988 1 QKPLDKRLkRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAG-LIIGGAPLSAL--LPLLGLLLAVLLLRALLAWL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 80 ERLVSHEGTFRVLEHLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLD 159
Cdd:COG4988 78 RERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 160 VTLALtlggIMLATLLLLpplfyragrPVGEALTMLRA---SYRQ-----QLTG----WLQGQAELSIFGAAGRYREQLD 227
Cdd:COG4988 158 WLSGL----ILLVTAPLI---------PLFMILVGKGAakaSRRQwralaRLSGhfldRLRGLTTLKLFGRAKAEAERIA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 228 T-TEQVwheaqrRQAGLTALSqamMTLISGMtvVLILwMAAGGVGgnstpgsLIALFV---------------FCALAAF 291
Cdd:COG4988 225 EaSEDF------RKRTMKVLR---VAFLSSA--VLEF-FASLSIA-------LVAVYIgfrllggsltlfaalFVLLLAP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 292 EALAP---VGGAFQHLGQVIASARRVSDVIDQPADITFAESGK-DAPREASLSLRNVSFSYPGQpQPALRDITLDVAPGE 367
Cdd:COG4988 286 EFFLPlrdLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPlPAAGPPSIELEDVSFSYPGG-RPALDGLSLTIPPGE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 368 HIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQADDAALG 447
Cdd:COG4988 365 RVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 448 AVLARVGLEKLLDD--EGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKT 525
Cdd:COG4988 445 AALEAAGLDEFVAAlpDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT 524
|
570 580 590
....*....|....*....|....*....|....*....
gi 495163667 526 LLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQG 564
Cdd:COG4988 525 VILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
339-554 |
5.42e-81 |
|
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: 251.85 E-value: 5.42e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYrEAALRATMSV 418
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSATLRDNLllaapqaddaalgavlarvglekllddeglnawlgegGRQLSGGELRRLGIARALLHNAPMLLL 498
Cdd:cd03247 80 LNQRPYLFDTTLRNNL-------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 499 DEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQG 554
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-571 |
3.18e-80 |
|
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: 262.73 E-value: 3.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 2 RALLPYLALYKrhkWLLSLGVVLAIVTLLASIGLLTLSGWFLSASAVVGMAGLYSFnymLPAaGVRGAAIIRTAGRYFER 81
Cdd:TIGR02203 3 RRLWSYVRPYK---AGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWW---VPL-VVIGLAVLRGICSFVST 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 82 LVSHEGTFRVLEHLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPL-------IGALAVIAVVTLG 154
Cdd:TIGR02203 76 YLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLvretltvIGLFIVLLYYSWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 155 LSLLDVTLALTLGGIMlatllllpPLFYRAGRPVGEALTMLRASYRQQLTGWLQGQAELSIFGAAGRYREQLDTTEQVWH 234
Cdd:TIGR02203 156 LTLIVVVMLPVLSILM--------RRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 235 EAQRRQAGLTALSQAMMTLISGMTVVLILWMAA-GGVGGNSTPGSLIALFVFCAL--AAFEALAPVGGAFQhlgQVIASA 311
Cdd:TIGR02203 228 RLAMKMTSAGSISSPITQLIASLALAVVLFIALfQAQAGSLTAGDFTAFITAMIAliRPLKSLTNVNAPMQ---RGLAAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 312 RRVSDVIDQPADitfAESGKDAPREAS--LSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRA 389
Cdd:TIGR02203 305 ESLFTLLDSPPE---KDTGTRAIERARgdVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 390 WDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAP-QADDAALGAVLARVGLEKLLD--DEGLNA 466
Cdd:TIGR02203 382 YEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDklPLGLDT 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 467 WLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMD 546
Cdd:TIGR02203 462 PIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMD 541
|
570 580
....*....|....*....|....*
gi 495163667 547 NGQITEQGSHKELLAQQGRYYQFRA 571
Cdd:TIGR02203 542 DGRIVERGTHNELLARNGLYAQLHN 566
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
1-569 |
1.91e-75 |
|
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: 250.39 E-value: 1.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 1 MRALLPYLAlykRHKWLLSLGVVLAIVTLLASIGL-----LTLSGWFLSASAvvgmaGLYSfNYMLPAAGVRGAAIIRTA 75
Cdd:TIGR02204 6 LAALWPFVR---PYRGRVLAALVALLITAAATLSLpyavrLMIDHGFSKDSS-----GLLN-RYFAFLLVVALVLALGTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 76 GRYFerLVSHEGTfRVLEHLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLY-------LRVISPLIGALAVI 148
Cdd:TIGR02204 77 ARFY--LVTWLGE-RVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIgsslsmaLRNALMCIGGLIMM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 149 AVVTLGLSLLD------VTLALTLGGIMLATLLLLPP-LFYRAGRPVGEALTMLRA--SYRQQltgwlqgQAELSIFGAA 219
Cdd:TIGR02204 154 FITSPKLTSLVllavplVLLPILLFGRRVRKLSRESQdRIADAGSYAGETLGAIRTvqAFGHE-------DAERSRFGGA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 220 gryreqldtTEQVWHEAQRRQAGLTALSQAMMTLISGmTVVLILWMAAGGVGGNSTPGSLIALFVFCALAAFEALAPVGG 299
Cdd:TIGR02204 227 ---------VEKAYEAARQRIRTRALLTAIVIVLVFG-AIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 300 AFQHLGQVIASARRVSDVIDQPADITFAESGKD--APREASLSLRNVSFSYPGQP-QPALRDITLDVAPGEHIAILGRTG 376
Cdd:TIGR02204 297 VWGELQRAAGAAERLIELLQAEPDIKAPAHPKTlpVPLRGEIEFEQVNFAYPARPdQPALDGLNLTVRPGETVALVGPSG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 377 CGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQADDAAL--GAVLARVG 454
Cdd:TIGR02204 377 AGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVeaAARAAHAH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 455 --LEKLldDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHR 532
Cdd:TIGR02204 457 efISAL--PEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHR 534
|
570 580 590
....*....|....*....|....*....|....*..
gi 495163667 533 LQGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYYQF 569
Cdd:TIGR02204 535 LATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
338-554 |
1.36e-74 |
|
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: 236.72 E-value: 1.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMS 417
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQRVHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLDDE--GLNAWLGEGGRQLSGGELRRLGIARALLHNAPM 495
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHpnGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 496 LLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQG 554
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
241-562 |
2.78e-73 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 247.47 E-value: 2.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 241 AGLTALSQAMMTLISGMTVVLILWMAAGGvggNSTPGSLIAlfvfCALAAFEALAPVG---GAFQHLGQVIASARRVSDV 317
Cdd:TIGR03375 369 NLATNFAQFIQQLVSVAIVVVGVYLISDG---ELTMGGLIA----CVMLSGRALAPLGqlaGLLTRYQQAKTALQSLDEL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 318 IDQPADITFAESGKDAPR-EASLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGD 396
Cdd:TIGR03375 442 MQLPVERPEGTRFLHRPRlQGEIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGS 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 397 VMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLDD--EGLNAWLGEGGRQ 474
Cdd:TIGR03375 522 VLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRhpDGLDMQIGERGRS 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 475 LSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQG 554
Cdd:TIGR03375 602 LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADG 681
|
....*...
gi 495163667 555 SHKELLAQ 562
Cdd:TIGR03375 682 PKDQVLEA 689
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
339-549 |
3.87e-72 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 228.42 E-value: 3.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSATLRDNLllaapqaddaalgavlarvglekllddeglnawlgeggrqLSGGELRRLGIARALLHNAPMLLL 498
Cdd:cd03228 81 VPQDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495163667 499 DEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQ 549
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
339-568 |
9.10e-72 |
|
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: 229.81 E-value: 9.10e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSATLRDNLLLAAPQADDA----ALGAVLARVGLEKLldDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAP 494
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREeveeAARAANAHEFIMEL--PEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 495 MLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYYQ 568
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
342-564 |
4.11e-68 |
|
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: 220.17 E-value: 4.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 342 RNVSFSYPGQpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQ 421
Cdd:cd03254 6 ENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 422 RVHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLDD--EGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLD 499
Cdd:cd03254 85 DTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKlpNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 500 EPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQG 564
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
339-568 |
1.83e-67 |
|
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: 218.64 E-value: 1.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSATLRDNLLLAAPQADD-----AALGAVLARVgLEKLldDEGLNAWLGEGGRQLSGGELRRLGIARALLHNA 493
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDeevieAAKAAQIHDK-IMRF--PDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 494 PMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYYQ 568
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
341-569 |
1.25e-66 |
|
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: 216.64 E-value: 1.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 341 LRNVSFSYPGQP-QPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVV 419
Cdd:cd03249 3 FKNVSFRYPSRPdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 420 PQRVHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLDD--EGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLL 497
Cdd:cd03249 83 SQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSlpDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163667 498 LDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYYQF 569
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
216-568 |
2.12e-65 |
|
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: 224.31 E-value: 2.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 216 FGAAGRYREQLDTTEQVWHEAQRRQAGLTALSQAMMTLISGMTVVLILWMAAGGV-GGNSTPGSLIALFVFcALAAFEAL 294
Cdd:COG5265 234 FGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVvAGTMTVGDFVLVNAY-LIQLYIPL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 295 APVGGAFQHLGQVIASARRVSDVIDQPADITFAESGKD-APREASLSLRNVSFSYpgQPQ-PALRDITLDVAPGEHIAIL 372
Cdd:COG5265 313 NFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPlVVGGGEVRFENVSFGY--DPErPILKGVSFEVPAGKTVAIV 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 373 GRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQADDAALGAV--L 450
Cdd:COG5265 391 GPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAarA 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 451 ARvgleklLDD------EGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK 524
Cdd:COG5265 471 AQ------IHDfieslpDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR 544
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 495163667 525 TLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYYQ 568
Cdd:COG5265 545 TTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQ 588
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-545 |
2.63e-65 |
|
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: 222.16 E-value: 2.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 17 LLSLGVVLAIVTLLASIglltLSGWFLSASAVVGMAGLysfnymlpAAGVRGAAIIRTAGRYFERLVSHEGTFRVLEHLR 96
Cdd:TIGR02857 13 VLGALLIIAQAWLLARV----VDGLISAGEPLAELLPA--------LGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 97 VYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIgaLAVIAVVTLGLSLLdvTLALTLGGIMLATLLL 176
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLV--LAVIVPLAILAAVF--PQDWISGLILLLTAPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 177 LPPLFYRAGRPVgEALTMLRASYRQQLTGW----LQGQAELSIFGAAGRYREQLDTTEQVWHEAQRRQAGLTALSQAMMT 252
Cdd:TIGR02857 157 IPIFMILIGWAA-QAAARKQWAALSRLSGHfldrLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 253 LISGMTVVLI-----LWMAAGGVggnstpgSLIALFVFCALA--AFEALAPVGGAFQHLGQVIASARRVSDVIDQPADIT 325
Cdd:TIGR02857 236 LFATLSVALVavyigFRLLAGDL-------DLATGLFVLLLApeFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 326 FAESGKDAPREASLSLRNVSFSYPGQPqPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSIT 405
Cdd:TIGR02857 309 AGKAPVTAAPASSLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 406 GYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLDD--EGLNAWLGEGGRQLSGGELRRL 483
Cdd:TIGR02857 388 DADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAAlpQGLDTPIGEGGAGLSGGQAQRL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163667 484 GIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVM 545
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
25-311 |
1.12e-63 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 210.60 E-value: 1.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 25 AIVTLLASIGLLTLSGWFLSASAVVGMAGLYSFNYMLPAAGVRGAAIIRTAGRYFERLVSHEGTFRVLEHLRVYTFSRLL 104
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 105 PLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLDVtLALTLGGIMLATLLLLPPLFYRA 184
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDP-LVALILLVFALLIPLSPALWDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 185 GRPVGEALTMLRASYRQQLTGWLQGQAELSIFGAAGRYREQLDTTEQVWHEAQRRQAGLTALSQAMMTLISGMTVVLILW 264
Cdd:cd18561 160 AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALG 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 495163667 265 MAAGGVGGNStPGSLIALFVFCALAAFEALAPVGGAFQHLGQVIASA 311
Cdd:cd18561 240 VGALRVLGGQ-LTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISA 285
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
207-568 |
1.88e-63 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 218.35 E-value: 1.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 207 LQGQAELSIFGAAGRYREQLDTTEQvwheaQRRQAGL-----TALSQAMMTLISGMTVVLILWMAA-GGVGGNSTPGSLI 280
Cdd:PRK11176 211 LKGHKEVLIFGGQEVETKRFDKVSN-----RMRQQGMkmvsaSSISDPIIQLIASLALAFVLYAASfPSVMDTLTAGTIT 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 281 ALF--VFCALAAFEALAPVGGAFQhlgQVIASARRVSDVID--QPADitfaeSGKDAPREAS--LSLRNVSFSYPGQPQP 354
Cdd:PRK11176 286 VVFssMIALMRPLKSLTNVNAQFQ---RGMAACQTLFAILDleQEKD-----EGKRVIERAKgdIEFRNVTFTYPGKEVP 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNL 434
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNI 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 435 LLAA------PQADDAALGAvLARVGLEKLldDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAE 508
Cdd:PRK11176 438 AYARteqysrEQIEEAARMA-YAMDFINKM--DNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 509 TERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYYQ 568
Cdd:PRK11176 515 SERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
338-555 |
8.08e-62 |
|
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: 203.49 E-value: 8.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMS 417
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQRVHLFSATLRDNLllaAP--QADDAALGAVLARVGLEKLLDD--EGLNAWLGEGGRQLSGGELRRLGIARALLHNA 493
Cdd:cd03244 82 IIPQDPVLFSGTIRSNL---DPfgEYSDEELWQALERVGLKEFVESlpGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163667 494 PMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGS 555
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
238-569 |
2.15e-57 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 202.11 E-value: 2.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 238 RRQAGLTALSQAMMTLISGMTVVLILWMAAGGVGGNSTPGSLIALFVFCALAAFEALAPVGG--AF--------QHLGQV 307
Cdd:PRK13657 213 RIEAETQALRDIADNLLAAQMPVLSWWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEvvAFvgfatlliGRLDQV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 308 IASARRVS----------DVIDQPADITFAESGKDAPR-EASLSLRNVSFSYPGQPQpALRDITLDVAPGEHIAILGRTG 376
Cdd:PRK13657 293 VAFINQVFmaapkleeffEVEDAVPDVRDPPGAIDLGRvKGAVEFDDVSFSYDNSRQ-GVEDVSFEAKPGQTVAIVGPTG 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 377 CGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQADDAALGAVLARVGLE 456
Cdd:PRK13657 372 AGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAH 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 457 KLLD--DEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQ 534
Cdd:PRK13657 452 DFIErkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLS 531
|
330 340 350
....*....|....*....|....*....|....*
gi 495163667 535 GLTAFDRIIVMDNGQITEQGSHKELLAQQGRYYQF 569
Cdd:PRK13657 532 TVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
339-568 |
4.34e-55 |
|
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: 186.15 E-value: 4.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLDD--EGLNAWLGEGGRQLSGGELRRLGIARALLHNAPML 496
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISElpEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163667 497 LLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYYQ 568
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
340-549 |
5.08e-52 |
|
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: 176.89 E-value: 5.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 340 SLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVV 419
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 420 PQ--RVHLFSATLRD-------NLLLAAPQAdDAALGAVLARVGLEKLLDDEglnawlgegGRQLSGGELRRLGIARALL 490
Cdd:cd03225 81 FQnpDDQFFGPTVEEevafgleNLGLPEEEI-EERVEEALELVGLEGLRDRS---------PFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163667 491 HNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGL-TAFDRIIVMDNGQ 549
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
339-563 |
1.21e-51 |
|
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: 176.75 E-value: 1.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:COG1122 1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQ--RVHLFSATLRD-------NLLLAAPQADDAALgAVLARVGLEKLLDdeglnawlgeggR---QLSGGELRRLGIA 486
Cdd:COG1122 80 VFQnpDDQLFAPTVEEdvafgpeNLGLPREEIRERVE-EALELVGLEHLAD------------RpphELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 487 RALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTA-FDRIIVMDNGQITEQGSHKELLAQQ 563
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
339-550 |
5.83e-50 |
|
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: 171.90 E-value: 5.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQ--PQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAAL---- 412
Cdd:cd03255 1 IELKNLSKTYGGGgeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 413 RATMSVVPQRVHL---FSAtlRDNLLLAA-------PQADDAALgAVLARVGLEKLLDdeglnawlgEGGRQLSGGELRR 482
Cdd:cd03255 81 RRHIGFVFQSFNLlpdLTA--LENVELPLllagvpkKERRERAE-ELLERVGLGDRLN---------HYPSELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 483 LGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ--KTLLMVTHRLQGLTAFDRIIVMDNGQI 550
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
339-553 |
1.05e-49 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 171.38 E-value: 1.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYP--GQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLI---TRawdPTSGDVMLDGVSITGYREAAL- 412
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILgglDR---PTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 413 ---RATMSVVPQRVHLF-SATLRDNLLLAA------PQADDAALGAVLARVGLEKLLDDEGlnawlgeggRQLSGGELRR 482
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLpELTALENVALPLllagvsRKERRERARELLERVGLGDRLDHRP---------SQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163667 483 LGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ--KTLLMVTHRLQGLTAFDRIIVMDNGQITEQ 553
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
339-562 |
6.34e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 167.16 E-value: 6.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAAlRATMSV 418
Cdd:COG1131 1 IEVRGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSA-TLRDNLLLAA------PQADDAALGAVLARVGLEKLLDDEGlnawlgeggRQLSGGELRRLGIARALLH 491
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFFArlyglpRKEARERIDELLELFGLTDAADRKV---------GTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163667 492 NAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQ 562
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
232-573 |
1.21e-47 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 175.46 E-value: 1.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 232 VWHEAQRRQAGLTALSQAMMTLISGMTVVLILWMAAGGVGGNSTPGSLIALFVFCA-------LAAFEALAPVGGAFQHL 304
Cdd:TIGR01192 207 VVHSYNRIEAETSALKQFTNNLLSAQYPVLDWWALASGLNRMASTISMMCILVIGTvlvikgeLSVGEVIAFIGFANLLI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 305 G----------QVIASARRVSDVIDQPADITFAESGKDAPR----EASLSLRNVSFSYPGQPQpALRDITLDVAPGEHIA 370
Cdd:TIGR01192 287 GrldqmsgfitQIFEARAKLEDFFDLEDSVFQREEPADAPElpnvKGAVEFRHITFEFANSSQ-GVFDVSFEAKAGQTVA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 371 ILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQADDAALGAVL 450
Cdd:TIGR01192 366 IVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 451 ARVGLEKLLDDE--GLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLM 528
Cdd:TIGR01192 446 KAAAAHDFILKRsnGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFI 525
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 495163667 529 VTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYYQFRARS 573
Cdd:TIGR01192 526 IAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRS 570
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
346-574 |
2.13e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 174.65 E-value: 2.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 346 FSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITrAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHL 425
Cdd:PRK11174 358 LSPDGKT--LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL-GFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 426 FSATLRDNLLLAAPQADDAALGAVLARVGLEKLLDD--EGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTE 503
Cdd:PRK11174 435 PHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLlpQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163667 504 GLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYYQFRARSV 574
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQ 585
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
233-562 |
3.31e-47 |
|
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: 173.78 E-value: 3.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 233 WHEAQRRQAGLTALSQAMMTLISGMT--VVLILWMAAGGVG------GNSTPGSLIAlfvfCALAAFEALAPVGGAF--- 301
Cdd:COG4618 220 WQRANARALALQARASDRAGGFSALSkfLRLLLQSAVLGLGaylviqGEITPGAMIA----ASILMGRALAPIEQAIggw 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 302 QHLGQVIASARRVSDVIDQPADitfAESGKDAPR-EASLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKS 380
Cdd:COG4618 296 KQFVSARQAYRRLNELLAAVPA---EPERMPLPRpKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKS 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 381 TLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLllaA--PQADDAALGAVLARVGLEKL 458
Cdd:COG4618 373 TLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI---ArfGDADPEKVVAAAKLAGVHEM 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 459 LDD--EGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEV-AVQKTLLMVTHRLQG 535
Cdd:COG4618 450 ILRlpDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSL 529
|
330 340
....*....|....*....|....*..
gi 495163667 536 LTAFDRIIVMDNGQITEQGSHKELLAQ 562
Cdd:COG4618 530 LAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
217-568 |
4.25e-46 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 172.98 E-value: 4.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 217 GAAGRYREQLDTTEQVWHEAQRRQAGLTALSQAMMTLIsgmtVVLILWMaaGG---VGGNSTPGSLIAlFVFCALAAFEA 293
Cdd:TIGR00958 361 GEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLI----QVLVLYY--GGqlvLTGKVSSGNLVS-FLLYQEQLGEA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 294 LAPVGGAFQHLGQVIASARRVSDVIDQPADITFAESGKDAPREASLSLRNVSFSYPGQP-QPALRDITLDVAPGEHIAIL 372
Cdd:TIGR00958 434 VRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPdVPVLKGLTFTLHPGEVVALV 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 373 GRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQADDAALGAVLAR 452
Cdd:TIGR00958 514 GPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKA 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 453 VGLEKLL--DDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKevAVQKTLLMVT 530
Cdd:TIGR00958 594 ANAHDFImeFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIA 671
|
330 340 350
....*....|....*....|....*....|....*...
gi 495163667 531 HRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYYQ 568
Cdd:TIGR00958 672 HRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
339-550 |
1.26e-45 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 158.53 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSATLRDNLllaapqaddaalgavlarvglekllddeglnawlgeggrqLSGGELRRLGIARALLHNAPMLLL 498
Cdd:cd03246 81 LPQDDELFSGSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495163667 499 DEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAFDRIIVMDNGQI 550
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAAgATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
339-554 |
3.61e-45 |
|
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: 159.21 E-value: 3.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQ--PQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREA---ALR 413
Cdd:cd03257 2 LEVKNLSVSFPTGggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 414 ATMSVVPQ----------RV-HLFSATLRDNLLLAAPQADDAALGAVLARVGLEKllddeglnAWLGEGGRQLSGGELRR 482
Cdd:cd03257 82 KEIQMVFQdpmsslnprmTIgEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPE--------EVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 483 LGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLqGLTAF--DRIIVMDNGQITEQG 554
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDL-GVVAKiaDRVAVMYAGKIVEEG 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
339-560 |
5.25e-45 |
|
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: 159.82 E-value: 5.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHL-FSATLRD----------NLLLAAPQADDAALGAVLARVGLEKLLDdeglnawlgeggR---QLSGGELRRLG 484
Cdd:COG1120 80 VPQEPPApFGLTVRElvalgryphlGLFGRPSAEDREAVEEALERTGLEHLAD------------RpvdELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 485 IARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ--KTLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKELL 560
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
339-550 |
5.37e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 158.06 E-value: 5.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQpaLRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:COG4619 1 LELEGLSFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSATLRDNLL----LAAPQADDAALGAVLARVGL-EKLLDDEGlnawlgeggRQLSGGELRRLGIARALLHNA 493
Cdd:COG4619 79 VPQEPALWGGTVRDNLPfpfqLRERKFDRERALELLERLGLpPDILDKPV---------ERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 494 PMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTH-RLQGLTAFDRIIVMDNGQI 550
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
339-561 |
2.91e-44 |
|
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: 157.66 E-value: 2.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQP--QPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATM 416
Cdd:COG1124 2 LEVRNLSVSYGQGGrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVVPQrvHLFSA-----TLRDnlLLAAP------QADDAALGAVLARVGLEKllddeglnAWLGEGGRQLSGGELRRLGI 485
Cdd:COG1124 82 QMVFQ--DPYASlhprhTVDR--ILAEPlrihglPDREERIAELLEQVGLPP--------SFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 486 ARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLA 561
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLA 228
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
245-568 |
7.26e-44 |
|
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: 166.45 E-value: 7.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 245 ALSQAMMTLISGMTVVLILWMAAGGV-GGNSTPGSLIAlfvFCALAAFeALAPVGGAFqHLGQVIASAR----RVSDVID 319
Cdd:TIGR01193 379 QGQQAIKAVTKLILNVVILWTGAYLVmRGKLTLGQLIT---FNALLSY-FLTPLENII-NLQPKLQAARvannRLNEVYL 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 320 QPADitFAESGKDAPRE---ASLSLRNVSFSYpGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGD 396
Cdd:TIGR01193 454 VDSE--FINKKKRTELNnlnGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGE 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 397 VMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAP-----QADDAALGAVLARVGLEKLldDEGLNAWLGEG 471
Cdd:TIGR01193 531 ILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenvsqDEIWAACEIAEIKDDIENM--PLGYQTELSEE 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 472 GRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILA-LVKevAVQKTLLMVTHRLQGLTAFDRIIVMDNGQI 550
Cdd:TIGR01193 609 GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNnLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
330
....*....|....*...
gi 495163667 551 TEQGSHKELLAQQGRYYQ 568
Cdd:TIGR01193 687 IEQGSHDELLDRNGFYAS 704
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
306-562 |
1.69e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 162.38 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 306 QVIASARRVSDVIDQPADITFAESGKDAPREAsLSLRNVSFSYP---GQPQPALRDITLDVAPGEHIAILGRTGCGKSTL 382
Cdd:COG1123 229 EILAAPQALAAVPRLGAARGRAAPAAAAAEPL-LEVRNLSKRYPvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 383 LQLITRAWDPTSGDVMLDGVSITGYREAALRA---TMSVVPQRVhlFSA-----TLRDNLLLAAPQADDAALGAVLARVg 454
Cdd:COG1123 308 ARLLLGLLRPTSGSILFDGKDLTKLSRRSLRElrrRVQMVFQDP--YSSlnprmTVGDIIAEPLRLHGLLSRAERRERV- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 455 lEKLLDDEGLNAWLGEggR---QLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ--KTLLMV 529
Cdd:COG1123 385 -AELLERVGLPPDLAD--RyphELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElgLTYLFI 461
|
250 260 270
....*....|....*....|....*....|....*
gi 495163667 530 THRLqGLTAF--DRIIVMDNGQITEQGSHKELLAQ 562
Cdd:COG1123 462 SHDL-AVVRYiaDRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
339-565 |
2.49e-43 |
|
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: 155.02 E-value: 2.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYpgQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRAtMSV 418
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSA-TLRDNLLLAAPQADDAaLGAVLARVglEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLL 497
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAELYGLF-DEELKKRI--EELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 498 LDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTA-FDRIIVMDNGQITEQGSHKELLAQQGR 565
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
345-571 |
2.81e-43 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 162.96 E-value: 2.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 345 SFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVH 424
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 425 LFSATLRDNLLLAAPQADDAALGAV--LARVGLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPT 502
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVarLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 503 EGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQG------RYYQFRA 571
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGwyrdmyRYQQLEA 554
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
339-552 |
3.07e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 154.05 E-value: 3.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYRE---AALRAT 415
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreiPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 416 MSVVPQRVHLFSA-TLRDNLLLA------APQADDAALGAVLARVGLEKLLDdeglnawlgeggR---QLSGGELRRLGI 485
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAK------------AlphELSGGEQQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 486 ARALLHNAPMLLLDEPTEGLDAETERQILALVKEV-AVQKTLLMVTHRLQGLTAFD-RIIVMDNGQITE 552
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPkRVLELEDGRLVR 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
334-561 |
3.36e-43 |
|
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: 154.37 E-value: 3.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 334 PREASLSLRNVSFSYpGqPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREA--- 410
Cdd:COG1127 1 MSEPMIEVRNLTKSF-G-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKely 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 411 ALRATMSVVPQRVHLFSA-TLRDNLL--------LAAPQADDAALgAVLARVGLEkllDDEGLNAwlgeggRQLSGGELR 481
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSlTVFENVAfplrehtdLSEAEIRELVL-EKLELVGLP---GAADKMP------SELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 482 RLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEV--AVQKTLLMVTHRLQglTAF---DRIIVMDNGQITEQGSH 556
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVTHDLD--SAFaiaDRVAVLADGKIIAEGTP 226
|
....*
gi 495163667 557 KELLA 561
Cdd:COG1127 227 EELLA 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
333-552 |
4.43e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.86 E-value: 4.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 333 APREASLSLRNVSFSYP--GQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGyrea 410
Cdd:COG1116 2 SAAAPALELRGVSKRFPtgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 411 aLRATMSVVPQRVHLFS-ATLRDNLLLA-------APQADDAALgAVLARVGLEKLLDdeglnAWlgegGRQLSGGELRR 482
Cdd:COG1116 78 -PGPDRGVVFQEPALLPwLTVLDNVALGlelrgvpKAERRERAR-ELLELVGLAGFED-----AY----PHQLSGGMRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 483 LGIARALLHNAPMLLLDEPTEGLDAET----ERQILALVKEvaVQKTLLMVTH------RLqgltAfDRIIVMDN--GQI 550
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTrerlQDELLRLWQE--TGKTVLFVTHdvdeavFL----A-DRVVVLSArpGRI 219
|
..
gi 495163667 551 TE 552
Cdd:COG1116 220 VE 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
339-562 |
4.89e-43 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 154.00 E-value: 4.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYRE--AALRATM 416
Cdd:COG1126 2 IEIENLHKSFGDLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKdiNKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVVPQRVHLFS-ATLRDNLLLA--------APQADDAALgAVLARVGLEkllddEGLNAWLGeggrQLSGGELRRLGIAR 487
Cdd:COG1126 80 GMVFQQFNLFPhLTVLENVTLApikvkkmsKAEAEERAM-ELLERVGLA-----DKADAYPA----QLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 488 ALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK-TLLMVTHRLqgltAF-----DRIIVMDNGQITEQGSHKELLA 561
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGmTMVVVTHEM----GFarevaDRVVFMDGGRIVEEGPPEEFFE 225
|
.
gi 495163667 562 Q 562
Cdd:COG1126 226 N 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
334-563 |
6.64e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 153.71 E-value: 6.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 334 PREASLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSItgyreAALR 413
Cdd:COG1121 2 MMMPAIELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 414 ATMSVVPQRVHL---FSATLRD----------NLLLAAPQADDAALGAVLARVGLEKLLDdeglnAWLGEggrqLSGGEL 480
Cdd:COG1121 75 RRIGYVPQRAEVdwdFPITVRDvvlmgrygrrGLFRRPSRADREAVDEALERVGLEDLAD-----RPIGE----LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 481 RRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTA-FDRIIVMDNGQITEqGSHKE 558
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEE 224
|
....*
gi 495163667 559 LLAQQ 563
Cdd:COG1121 225 VLTPE 229
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
339-550 |
4.39e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 151.75 E-value: 4.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMS- 417
Cdd:COG3638 3 LELRNLSKRYPGG-TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 --VVPQRVHLFS-ATLRDNLLLAA--------------PQAD-DAALGAvLARVGLEKLLDDeglnawlgeggR--QLSG 477
Cdd:COG3638 82 igMIFQQFNLVPrLSVLTNVLAGRlgrtstwrsllglfPPEDrERALEA-LERVGLADKAYQ-----------RadQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 478 GELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQ-GLTAFDRIIVMDNGQI 550
Cdd:COG3638 150 GQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDlARRYADRIIGLRDGRV 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
334-555 |
1.07e-41 |
|
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: 149.10 E-value: 1.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 334 PREASLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALR 413
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 414 ATMSVVPQRVHLFSATLRDNLLLAAPQADDAALGAVlaRVglekllddeglnawlGEGGRQLSGGELRRLGIARALLHNA 493
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL--RV---------------SEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163667 494 PMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGS 555
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
339-562 |
1.60e-41 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 152.92 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYP--GQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRAT- 415
Cdd:COG1135 2 IELENLSKTFPtkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 416 --MSVVPQRVHLFSA-TLRDN----LLLA-APQADDAA-LGAVLARVGLEklldDEGlNAWLgeggRQLSGGELRRLGIA 486
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENvalpLEIAgVPKAEIRKrVAELLELVGLS----DKA-DAYP----SQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 487 RALLHNAPMLLLDEPTEGLDAETERQILALVKEVAvQK---TLLMVTH-----RlqglTAFDRIIVMDNGQITEQGSHKE 558
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDIN-RElglTIVLITHemdvvR----RICDRVAVLENGRIVEQGPVLD 227
|
....
gi 495163667 559 LLAQ 562
Cdd:COG1135 228 VFAN 231
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
304-568 |
3.78e-41 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 157.19 E-value: 3.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 304 LGQVIASARRVSDVIDQPA-----DITFAESGkdapreaSLSLRNVSFSYPGQpQPALRDITLDVAPGEHIAILGRTGCG 378
Cdd:PRK10790 308 LQQAVVAGERVFELMDGPRqqygnDDRPLQSG-------RIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSG 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 379 KSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPqADDAALGAVLARVGLEKL 458
Cdd:PRK10790 380 KSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAEL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 459 LDD--EGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGL 536
Cdd:PRK10790 459 ARSlpDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTI 538
|
250 260 270
....*....|....*....|....*....|..
gi 495163667 537 TAFDRIIVMDNGQITEQGSHKELLAQQGRYYQ 568
Cdd:PRK10790 539 VEADTILVLHRGQAVEQGTHQQLLAAQGRYWQ 570
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
340-549 |
6.68e-41 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 145.47 E-value: 6.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 340 SLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVV 419
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 420 PQrvhlfsatlrdnlllaapqaddaalgavlarvglekllddeglnawlgeggrqLSGGELRRLGIARALLHNAPMLLLD 499
Cdd:cd00267 79 PQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495163667 500 EPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLT-AFDRIIVMDNGQ 549
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
339-562 |
7.83e-41 |
|
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: 147.73 E-value: 7.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQ--PALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRA-- 414
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 415 -TMSVVPQRVHLFSA-TLRDNLLLA-----APQAD-DAALGAVLARVGLEKLLDDEGlnawlgeggRQLSGGELRRLGIA 486
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALPleiagVPKAEiEERVLELLELVGLEDKADAYP---------AQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 487 RALLHNAPMLLLDEPTEGLDAETERQILALVKEVAvQK---TLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQ 562
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDIN-RElglTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
342-550 |
1.06e-40 |
|
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: 147.23 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 342 RNVSFSYPGQP-QPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVP 420
Cdd:cd03248 15 QNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 421 QRVHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLDD--EGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLL 498
Cdd:cd03248 95 QEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISElaSGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495163667 499 DEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQI 550
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
336-562 |
3.95e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 153.14 E-value: 3.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 336 EASLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPT---SGDVMLDGVSITGYREAAL 412
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 413 RATMSVVPQ--RVHLFSATLRD-------NLLLAAPQADDAALgAVLARVGLEKLLDDEglnawlgegGRQLSGGELRRL 483
Cdd:COG1123 82 GRRIGMVFQdpMTQLNPVTVGDqiaealeNLGLSRAEARARVL-ELLEAVGLERRLDRY---------PHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 484 GIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ--KTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELL 560
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEIL 231
|
..
gi 495163667 561 AQ 562
Cdd:COG1123 232 AA 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
340-554 |
7.50e-40 |
|
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: 143.34 E-value: 7.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 340 SLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVV 419
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 420 PQrvhlfsatlrdnlllaapqaddaalgaVLARVGLEKLLdDEGLNawlgeggrQLSGGELRRLGIARALLHNAPMLLLD 499
Cdd:cd03214 79 PQ---------------------------ALELLGLAHLA-DRPFN--------ELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 500 EPTEGLDAETERQILALVKEVA--VQKTLLMVTHRL-QGLTAFDRIIVMDNGQITEQG 554
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLAreRGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
339-550 |
1.04e-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: 142.54 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRAtMSV 418
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSA-TLRDNLllaapqaddaalgavlarvglekllddeglnawlgeggrQLSGGELRRLGIARALLHNAPMLL 497
Cdd:cd03230 78 LPEEPSLYENlTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 498 LDEPTEGLDAETERQILALVKE-VAVQKTLLMVTHRLQGLTA-FDRIIVMDNGQI 550
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
339-549 |
2.66e-39 |
|
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: 142.61 E-value: 2.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQ---PALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGvsitgyreaalraT 415
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 416 MSVVPQRVHLFSATLRDNLLLAAPqADDAALGAVLARVGLEKLLD--DEGLNAWLGEGGRQLSGGELRRLGIARALLHNA 493
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP-FDEERYEKVIKACALEPDLEilPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 494 PMLLLDEPTEGLDAETERQIL--ALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQ 549
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIFenCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
339-547 |
3.03e-39 |
|
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: 143.00 E-value: 3.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYP--GQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGyreaaLRATM 416
Cdd:cd03293 1 LEVRNVSKTYGggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVVPQRVHLFS-ATLRDNLLL-------AAPQADDAALGAvLARVGLEKLlddegLNAWlgegGRQLSGGELRRLGIARA 488
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALglelqgvPKAEARERAEEL-LELVGLSGF-----ENAY----PHQLSGGMRQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 489 LLHNAPMLLLDEPTEGLDAET----ERQILALVKEvaVQKTLLMVTHRL-QGLTAFDRIIVMDN 547
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTreqlQEELLDIWRE--TGKTVLLVTHDIdEAVFLADRVVVLSA 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
339-563 |
3.26e-39 |
|
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: 143.60 E-value: 3.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFS-ATLRDNL-----LLAAPQAD-DAALGAVLARVGLEKllddeglNAWLGEGGRQLSGGELRRLGIARALLH 491
Cdd:cd03295 80 VIQQIGLFPhMTVEENIalvpkLLKWPKEKiRERADELLALVGLDP-------AEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 492 NAPMLLLDEPTEGLDAETERQILALVKEV--AVQKTLLMVTHRLQglTAF---DRIIVMDNGQITEQGSHKELLAQQ 563
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDID--EAFrlaDRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
339-559 |
3.70e-39 |
|
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: 143.09 E-value: 3.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYpGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWD-----PTSGDVMLDGVSITGYREA--A 411
Cdd:cd03260 1 IELRDLNVYY-GDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 412 LRATMSVVPQRVHLFSATLRDNLLLAAP-------QADDAALGAVLARVGLEKLLDDEgLNAwlgeggRQLSGGELRRLG 484
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgiklkEELDERVEEALRKAALWDEVKDR-LHA------LGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 485 IARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKEL 559
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMqQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
340-548 |
4.69e-38 |
|
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: 139.59 E-value: 4.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 340 SLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAalratMSVV 419
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 420 PQRVHL---FSATLRD----------NLLLAAPQADDAALGAVLARVGLEKLLDDEglnawLGEggrqLSGGELRRLGIA 486
Cdd:cd03235 74 PQRRSIdrdFPISVRDvvlmglyghkGLFRRLSKADKAKVDEALERVGLSELADRQ-----IGE----LSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 487 RALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTA-FDRIIVMDNG 548
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
339-563 |
5.10e-38 |
|
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: 139.94 E-value: 5.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREA---ALRAT 415
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 416 MSVVPQRVHLFSAT---------LRDNLLLAAPQADDAALgAVLARVGL---EKLLDDEglnawlgeggrqLSGGELRRL 483
Cdd:cd03261 79 MGMLFQSGALFDSLtvfenvafpLREHTRLSEEEIREIVL-EKLEAVGLrgaEDLYPAE------------LSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 484 GIARALLHNAPMLLLDEPTEGLDAETERQILALVKEV--AVQKTLLMVTHRLQglTAF---DRIIVMDNGQITEQGSHKE 558
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLD--TAFaiaDRIAVLYDGKIVAEGTPEE 223
|
....*
gi 495163667 559 LLAQQ 563
Cdd:cd03261 224 LRASD 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
339-550 |
8.11e-38 |
|
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: 138.82 E-value: 8.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYpgQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAA--LRATM 416
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVVPQRVHLFS-ATLRDNLLLA--------APQADDAALGAvLARVGLEkllddEGLNAWlgegGRQLSGGELRRLGIAR 487
Cdd:cd03262 79 GMVFQQFNLFPhLTVLENITLApikvkgmsKAEAEERALEL-LEKVGLA-----DKADAY----PAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 488 ALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK-TLLMVTHRLqgltAF-----DRIIVMDNGQI 550
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGmTMVVVTHEM----GFarevaDRVIFMDDGRI 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
356-502 |
2.20e-37 |
|
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: 135.47 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSA-TLRDNL 434
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 435 LLAAP------QADDAALGAVLARVGLEKLLDDEglnawLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPT 502
Cdd:pfam00005 81 RLGLLlkglskREKDARAEEALEKLGLGDLADRP-----VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
310-575 |
3.58e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 148.20 E-value: 3.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 310 SARRVSDVIDQPADIT-FAESGKDA---PREASLSLRNVSFSY-PGQPqPALRDITLDVAPGEHIAILGRTGCGKSTLLQ 384
Cdd:PLN03232 1202 SVERVGNYIDLPSEATaIIENNRPVsgwPSRGSIKFEDVHLRYrPGLP-PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLN 1280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 385 LITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLllaAP--QADDAALGAVLARVGLEKLLDDE 462
Cdd:PLN03232 1281 ALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPfsEHNDADLWEALERAHIKDVIDRN 1357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 463 --GLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFD 540
Cdd:PLN03232 1358 pfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCD 1437
|
250 260 270
....*....|....*....|....*....|....*
gi 495163667 541 RIIVMDNGQITEQGSHKELLAQQGRYYqfrARSVH 575
Cdd:PLN03232 1438 KILVLSSGQVLEYDSPQELLSRDTSAF---FRMVH 1469
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
339-560 |
6.04e-37 |
|
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: 137.52 E-value: 6.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVM------LDGVSItgyreAAL 412
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDV-----WEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 413 RATMSVVPQRVHLF---SATLRDNLLLAA---------PQADDAALG-AVLARVGLEKLLDDeglnAWlgeggRQLSGGE 479
Cdd:COG1119 77 RKRIGLVSPALQLRfprDETVLDVVLSGFfdsiglyrePTDEQRERArELLELLGLAHLADR----PF-----GTLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 480 LRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ--KTLLMVTHRLQ-GLTAFDRIIVMDNGQITEQGSH 556
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEeIPPGITHVLLLKDGRVVAAGPK 227
|
....
gi 495163667 557 KELL 560
Cdd:COG1119 228 EEVL 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
339-559 |
6.23e-37 |
|
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: 136.48 E-value: 6.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRaTMSV 418
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQ-SLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSA-TLRDNLLLAA-----PQADDAALGAVLAR-VGLEKLLDDEGlnawlgeggRQLSGGELRRLGIARALLH 491
Cdd:cd03263 80 CPQFDALFDElTVREHLRFYArlkglPKSEIKEEVELLLRvLGLTDKANKRA---------RTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 492 NAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKEL 559
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
339-554 |
2.00e-36 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 134.95 E-value: 2.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGyREAALRATmSV 418
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-VPPERRNI-GM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLF-SATLRDNL-----LLAAPQAD-DAALGAVLARVGLEKLLDdeglnawlgEGGRQLSGGELRRLGIARALLH 491
Cdd:cd03259 77 VFQDYALFpHLTVAENIafglkLRGVPKAEiRARVRELLELVGLEGLLN---------RYPHELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 492 NAPMLLLDEPTEGLDAETERQILALVKEV--AVQKTLLMVTHRLQ-GLTAFDRIIVMDNGQITEQG 554
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
339-563 |
4.28e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 134.88 E-value: 4.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQpalrDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYrEAALRAtMSV 418
Cdd:COG3840 2 LRLDDLTYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL-PPAERP-VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSA-TLRDNLLLA-AP-----QADDAALGAVLARVGLEKLLDdeglnawlgeggR---QLSGGELRRLGIARA 488
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGlRPglkltAEQRAQVEQALERVGLAGLLD------------RlpgQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 489 LLHNAPMLLLDEPTEGLDAETERQILALVKEVA--VQKTLLMVTHRLQ-GLTAFDRIIVMDNGQITEQGSHKELLAQQ 563
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCreRGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
340-551 |
4.55e-36 |
|
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: 133.92 E-value: 4.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 340 SLRNVSFSYPGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSItgyREAALRATMSVV 419
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 420 PQRV--HLFSATLRDNLLLAAPQADDAALGAvlarvglEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLL 497
Cdd:cd03226 77 MQDVdyQLFTDSVREELLLGLKELDAGNEQA-------ETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 498 LDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQIT 551
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQgKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
339-562 |
6.04e-36 |
|
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: 136.72 E-value: 6.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRN--VSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDP---TSGDVMLDGVSITGYREAALR 413
Cdd:COG0444 2 LEVRNlkVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 414 A----TMSVVPQ----------RV-HLFSATLRDNLLLAAPQADDAALgAVLARVGL---EKLLDdeglnawlgeggR-- 473
Cdd:COG0444 82 KirgrEIQMIFQdpmtslnpvmTVgDQIAEPLRIHGGLSKAEARERAI-ELLERVGLpdpERRLD------------Ryp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 474 -QLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEvaVQK----TLLMVTHRLqGLTAF--DRIIVMD 546
Cdd:COG0444 149 hELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKD--LQRelglAILFITHDL-GVVAEiaDRVAVMY 225
|
250
....*....|....*.
gi 495163667 547 NGQITEQGSHKELLAQ 562
Cdd:COG0444 226 AGRIVEEGPVEELFEN 241
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
300-549 |
9.38e-36 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 141.48 E-value: 9.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 300 AFQHLGQVIASARRVS---DVIDQPADITFAESGKDAPREASLSLRNVSFSYPGQpQPALRDITLDVAPGEHIAILGRTG 376
Cdd:COG4178 321 NYQSLAEWRATVDRLAgfeEALEAADALPEAASRIETSEDGALALEDLTLRTPDG-RPLLEDLSLSLKPGERLLITGPSG 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 377 CGKSTLLQLITRAWDPTSGDVMLDGvsitgyreaalRATMSVVPQRVHLFSATLRDNLL--LAAPQADDAALGAVLARVG 454
Cdd:COG4178 400 SGKSTLLRAIAGLWPYGSGRIARPA-----------GARVLFLPQRPYLPLGTLREALLypATAEAFSDAELREALEAVG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 455 LEKL---LDDEglNAWlgegGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTH 531
Cdd:COG4178 469 LGHLaerLDEE--ADW----DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
250
....*....|....*....
gi 495163667 532 RlQGLTAF-DRIIVMDNGQ 549
Cdd:COG4178 543 R-STLAAFhDRVLELTGDG 560
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
339-555 |
2.58e-35 |
|
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: 132.56 E-value: 2.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAAL-RATMS 417
Cdd:cd03219 1 LEVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQRVHLFSA-TLRDNLLLAA-----------------PQADDAALgAVLARVGLEKLLDDEglnawlgegGRQLSGGE 479
Cdd:cd03219 79 RTFQIPRLFPElTVLENVMVAAqartgsglllararreeREARERAE-ELLERVGLADLADRP---------AGELSYGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 480 LRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK-TLLMVTHRLQGLTAF-DRIIVMDNGQITEQGS 555
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGiTVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGT 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
339-561 |
3.09e-35 |
|
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: 132.17 E-value: 3.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYR-EAALRATMS 417
Cdd:cd03224 1 LEVENLNAGYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQRVHLF-SATLRDNLLLAAPQADDAALGAVLARV-GLEKLLDDEglnawLGEGGRQLSGGELRRLGIARALLHNAPM 495
Cdd:cd03224 79 YVPEGRRIFpELTVEENLLLGAYARRRAKRKARLERVyELFPRLKER-----RKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 496 LLLDEPTEGLDAETERQILALVKEVAVQK-TLLMVTHRLQG-LTAFDRIIVMDNGQITEQGSHKELLA 561
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDEGvTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
339-561 |
3.91e-35 |
|
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: 132.03 E-value: 3.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYR-EAALRATMS 417
Cdd:COG0410 4 LEVENLHAGYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQRVHLFSA-TLRDNLLLAA-PQADDAALGAVLARVG-----LEKLLDDEGlnawlgeggRQLSGGELRRLGIARALL 490
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLLLGAyARRDRAEVRADLERVYelfprLKERRRQRA---------GTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163667 491 HNAPMLLLDEPTEGLDAETERQILALVKEVAVQK-TLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLA 561
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGvTILLVEQNARFALEIaDRAYVLERGRIVLEGTAAELLA 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
333-552 |
2.02e-34 |
|
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: 130.25 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 333 APREASLSLRNVSFSYPGQPQP--ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYRE- 409
Cdd:COG4181 3 SSSAPIIELRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 410 --AALRA-TMSVVPQRVHLFSA-TLRDN----LLLA-APQADDAALgAVLARVGLEKLLDdeglNAWlgeggRQLSGGEL 480
Cdd:COG4181 83 arARLRArHVGFVFQSFQLLPTlTALENvmlpLELAgRRDARARAR-ALLERVGLGHRLD----HYP-----AQLSGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 481 RRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTAFDRIIVMDNGQITE 552
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
335-559 |
2.32e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 133.30 E-value: 2.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 335 REASLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLItrA--WDPTSGDVMLDGVSITGyREAAL 412
Cdd:COG3842 2 AMPALELENVSKRYGDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMI--AgfETPDSGRILLDGRDVTG-LPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 413 RAtMSVVPQRV----HLfsaTLRDNL-----LLAAPQAD-DAALGAVLARVGLEKLLDdeglnawlgeggR---QLSGGE 479
Cdd:COG3842 77 RN-VGMVFQDYalfpHL---TVAENVafglrMRGVPKAEiRARVAELLELVGLEGLAD------------RyphQLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 480 LRRLGIARALLHNAPMLLLDEPTEGLDA----ETERQILALVKEVAVqkTLLMVTH-RLQGLTAFDRIIVMDNGQITEQG 554
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAklreEMREELRRLQRELGI--TFIYVTHdQEEALALADRIAVMNDGRIEQVG 218
|
....*
gi 495163667 555 SHKEL 559
Cdd:COG3842 219 TPEEI 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
337-553 |
2.56e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 130.75 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 337 ASLSLRNVSFSYPG--QPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGyrEAALRA 414
Cdd:COG4525 2 SMLTVRHVSVRYPGggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 415 tmsVVPQRVHLFS-ATLRDNLLLA------APQADDAALGAVLARVGLEkllDDEGLNAWlgeggrQLSGGELRRLGIAR 487
Cdd:COG4525 80 ---VVFQKDALLPwLNVLDNVAFGlrlrgvPKAERRARAEELLALVGLA---DFARRRIW------QLSGGMRQRVGIAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163667 488 ALLHNAPMLLLDEPTEGLDAETERQILALVKEV--AVQKTLLMVTHRL-QGLTAFDRIIVMDN--GQITEQ 553
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVeEALFLATRLVVMSPgpGRIVER 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
335-560 |
2.89e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.88 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 335 REASLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRA 414
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 415 TMSVVPQRvhlfsatlRDNLLLAAPQADDAALG----------------AVLARVGLEKLLDDEGLNawlgeggrqLSGG 478
Cdd:PRK13632 84 KIGIIFQN--------PDNQFIGATVEDDIAFGlenkkvppkkmkdiidDLAKKVGMEDYLDKEPQN---------LSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 479 ELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ--KTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSH 556
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrkKTLISITHDMDEAILADKVIVFSEGKLIAQGKP 226
|
....
gi 495163667 557 KELL 560
Cdd:PRK13632 227 KEIL 230
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
339-549 |
3.31e-34 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 127.69 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYRE--AALRATM 416
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVVPQRVHLFS-ATLRDNLLLAapqaddaalgavlarvglekllddeglnawlgeggrqLSGGELRRLGIARALLHNAPM 495
Cdd:cd03229 79 GMVFQDFALFPhLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 496 LLLDEPTEGLDAETERQILALVKEVAVQ--KTLLMVTHRLQGLTAF-DRIIVMDNGQ 549
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
339-559 |
1.92e-33 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 127.80 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYpGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWD-----PTSGDVMLDGVSITGYR--EAA 411
Cdd:TIGR00972 2 IEIENLNLFY-GEKE-ALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYDKKidVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 412 LRATMSVVPQRVHLFSATLRDNLLLAaPQA----DDAALGAVLarvglEKLLDDEGLnaW------LGEGGRQLSGGELR 481
Cdd:TIGR00972 80 LRRRVGMVFQKPNPFPMSIYDNIAYG-PRLhgikDKKELDEIV-----EESLKKAAL--WdevkdrLHDSALGLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 482 RLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKEL 559
Cdd:TIGR00972 152 RLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMqQAARISDRTAFFYDGELVEYGPTEQI 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
339-550 |
3.54e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 127.46 E-value: 3.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYReAALRATMSV 418
Cdd:COG0411 5 LEVRGLTKRFGGLV--AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-PHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VP--QRVHLFSA-TLRDNLLLAAPQADDAALGAVLARVGL------------EKLLDDEGLNAWLGEGGRQLSGGELRRL 483
Cdd:COG0411 82 ARtfQNPRLFPElTVLENVLVAAHARLGRGLLAALLRLPRarreereareraEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163667 484 GIARALLHNAPMLLLDEPTEGL-DAETERqILALVKEVAVQK--TLLMVTHRLQGLTAF-DRIIVMDNGQI 550
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLnPEETEE-LAELIRRLRDERgiTILLIEHDMDLVMGLaDRIVVLDFGRV 231
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
337-559 |
3.63e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.81 E-value: 3.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 337 ASLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGyREAALRAtM 416
Cdd:COG3839 2 ASLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD-LPPKDRN-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVVPQRVHLF-SATLRDNLLLA-----APQAD-DAALGAVLARVGLEKLLDdeglnawlgeggR---QLSGGELRRLGIA 486
Cdd:COG3839 78 AMVFQSYALYpHMTVYENIAFPlklrkVPKAEiDRRVREAAELLGLEDLLD------------RkpkQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 487 RALLHNAPMLLLDEPTEGLDA----ETERQILALVKEVAVqkTLLMVTH-RLQGLTAFDRIIVMDNGQITEQGSHKEL 559
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAklrvEMRAEIKRLHRRLGT--TTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
53-567 |
6.01e-33 |
|
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: 135.07 E-value: 6.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 53 GLYSFNYMLPAAGVRGAAIIRTAGRYFERLVSHEGtfrvLEHLRVYTFSRLLPLSPSGlarfrqgELLNRLVADVDTLDH 132
Cdd:TIGR00957 1009 SVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQD----LLHNKLRSPMSFFERTPSG-------NLVNRFSKELDTVDS 1077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 133 LYLRVISPLIGAL-AVIAVVTLglslldVTLALTLGGIM---LATLLLLPPLFYRA-GRPVGEALTMLRASYRQQLTGWL 207
Cdd:TIGR00957 1078 MIPPVIKMFMGSLfNVIGALIV------ILLATPIAAVIippLGLLYFFVQRFYVAsSRQLKRLESVSRSPVYSHFNETL 1151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 208 QGQAELSIFGAAGRYREQLDTTEqvwhEAQRRQAGLTALSQAMMTL---ISGMTVVLILWMAAGgVGGNSTPGSLIALFV 284
Cdd:TIGR00957 1152 LGVSVIRAFEEQERFIHQSDLKV----DENQKAYYPSIVANRWLAVrleCVGNCIVLFAALFAV-ISRHSLSAGLVGLSV 1226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 285 FCALAAFEALAPVGGAFQHLGQVIASARRVSDV----IDQPADITFAESGKDAPREASLSLRNVSFSYPGQPQPALRDIT 360
Cdd:TIGR00957 1227 SYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYseteKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHIN 1306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 361 LDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQ 440
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQY 1386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 441 ADDAALGAV-LARV-GLEKLLDDeGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVK 518
Cdd:TIGR00957 1387 SDEEVWWALeLAHLkTFVSALPD-KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR 1465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 495163667 519 EVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYY 567
Cdd:TIGR00957 1466 TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFY 1514
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
354-562 |
7.87e-33 |
|
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: 126.99 E-value: 7.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 354 PALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRA----TMSVVPQRVHLF-SA 428
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 429 TLRDNlllaapqaddAALGAVLARVGLE-------KLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEP 501
Cdd:cd03294 118 TVLEN----------VAFGLEVQGVPRAereeraaEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 502 TEGLD----AETERQILALVKEvaVQKTLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKELLAQ 562
Cdd:cd03294 188 FSALDplirREMQDELLRLQAE--LQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
334-564 |
1.59e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 133.71 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 334 PREASLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALR 413
Cdd:PLN03130 1233 PSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLR 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 414 ATMSVVPQRVHLFSATLRDNLllaAP--QADDAALGAVLARVGLEKLL--DDEGLNAWLGEGGRQLSGGELRRLGIARAL 489
Cdd:PLN03130 1313 KVLGIIPQAPVLFSGTVRFNL---DPfnEHNDADLWESLERAHLKDVIrrNSLGLDAEVSEAGENFSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 490 LHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQG 564
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
339-559 |
2.94e-32 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 124.22 E-value: 2.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRAT--- 415
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 416 MSVVPQRVHLFS-ATLRDNLLLAA--------------PQADDAALGAVLARVGLEKLlddeglnAWLGEGgrQLSGGEL 480
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfglfPKEEKQRALAALERVGLLDK-------AYQRAD--QLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 481 RRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHK 557
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYaDRIVGLKDGRIVFDGPPA 230
|
..
gi 495163667 558 EL 559
Cdd:cd03256 231 EL 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
341-555 |
3.10e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 127.22 E-value: 3.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 341 LRNVS--FSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRAT--- 415
Cdd:PRK11153 4 LKNISkvFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 416 MSVVPQRVHLFSA-TLRDNLLLA-----APQAD-DAALGAVLARVGLEKLLDdeglnawlgeggR---QLSGGELRRLGI 485
Cdd:PRK11153 84 IGMIFQHFNLLSSrTVFDNVALPlelagTPKAEiKARVTELLELVGLSDKAD------------RypaQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 486 ARALLHNAPMLLLDEPTEGLDAETERQILALVKEvaVQK----TLLMVTHRLQGLTAF-DRIIVMDNGQITEQGS 555
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILELLKD--INRelglTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGT 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
337-547 |
6.92e-32 |
|
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: 122.20 E-value: 6.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 337 ASLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAaLRATM 416
Cdd:COG4133 1 MMLEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-YRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVVPQRVHLFSA-TLRDNLLLAA----PQADDAALGAVLARVGLEKLLDDEGlnawlgeggRQLSGGELRRLGIARALLH 491
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAGLADLPV---------RQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 492 NAPMLLLDEPTEGLDAETERQILALVKE-VAVQKTLLMVTHRLQGLtAFDRIIVMDN 547
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLEL-AAARVLDLGD 204
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
339-554 |
2.05e-31 |
|
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: 121.15 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHiAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAaLRATMSV 418
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSA-TLRDNLLLAA-----PQAD-DAALGAVLARVGLEKLLDDEglnawLGeggrQLSGGELRRLGIARALLH 491
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDYIAwlkgiPSKEvKARVDEVLELVNLGDRAKKK-----IG----SLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 492 NAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQG 554
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
337-554 |
4.06e-31 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 119.58 E-value: 4.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 337 ASLSLRNVSFSYPGQPQPA----LRDITLDVAPGEHIAILGRTGCGKSTLLQLIT--RAWDPTSGDVMLDGVSItgyREA 410
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---DKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 411 ALRATMSVVPQRVHLFSA-TLRDNLLLAApqaddaalgavlarvgleKLlddeglnawlgeggRQLSGGELRRLGIARAL 489
Cdd:cd03213 79 SFRKIIGYVPQDDILHPTlTVRETLMFAA------------------KL--------------RGLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 490 LHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRL--QGLTAFDRIIVMDNGQITEQG 554
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
339-562 |
1.67e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.51 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRvhlfsatlRDNLLLAAPQADDAALG----------------AVLARVGLEKLLDDEglnawlgegGRQLSGGELRR 482
Cdd:PRK13635 86 VFQN--------PDNQFVGATVQDDVAFGlenigvpreemvervdQALRQVGMEDFLNRE---------PHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 483 LGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELL 560
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
..
gi 495163667 561 AQ 562
Cdd:PRK13635 229 KS 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
341-560 |
6.39e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 117.89 E-value: 6.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 341 LRNVSFSYpGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITG----YREAALRATM 416
Cdd:PRK09493 4 FKNVSKHF-GPTQ-VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvdERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 svVPQRVHLF-SATLRDNLL--------LAAPQADDAALgAVLARVGLEkllddEGLNAWLGEggrqLSGGELRRLGIAR 487
Cdd:PRK09493 82 --VFQQFYLFpHLTALENVMfgplrvrgASKEEAEKQAR-ELLAKVGLA-----ERAHHYPSE----LSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 488 ALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLqgltAF-----DRIIVMDNGQITEQGSHKELL 560
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEI----GFaekvaSRLIFIDKGRIAEDGDPQVLI 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
339-558 |
8.81e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 120.82 E-value: 8.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYreAALRATMSV 418
Cdd:PRK09452 15 VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV--PAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFS-ATLRDNLLLA-----------APQADDAalgavLARVGLEKLLDDEGlnawlgeggRQLSGGELRRLGIA 486
Cdd:PRK09452 91 VFQSYALFPhMTVFENVAFGlrmqktpaaeiTPRVMEA-----LRMVQLEEFAQRKP---------HQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 487 RALLHNAPMLLLDEPTEGLDAETERQILALVKevAVQKTL----LMVTH-RLQGLTAFDRIIVMDNGQITEQGSHKE 558
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELK--ALQRKLgitfVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
339-551 |
9.02e-30 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 114.83 E-value: 9.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDG--VSITGYREaALRATM 416
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPRD-ARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVVPqrvhlfsatlrdnlllaapqaddaalgavlarvglekllddeglnawlgeggrQLSGGELRRLGIARALLHNAPML 496
Cdd:cd03216 78 AMVY-----------------------------------------------------QLSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 497 LLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQIT 551
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
339-563 |
1.21e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 116.61 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpaLRdITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITgyREAALRATMSV 418
Cdd:PRK10771 2 LKLTDITWLYHHLP---MR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT--TTPPSRRPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFS-ATLRDN--------LLLAAPQADdaALGAVLARVGLEKLLDDegLNAwlgeggrQLSGGELRRLGIARAL 489
Cdd:PRK10771 76 LFQENNLFShLTVAQNiglglnpgLKLNAAQRE--KLHAIARQMGIEDLLAR--LPG-------QLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 490 LHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQ-GLTAFDRIIVMDNGQITEQGSHKELLAQQ 563
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
339-559 |
1.45e-29 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 116.57 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYreAALRATMSV 418
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL--PPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFS-ATLRDNLllaapqaddaALGAVLARVG-------LEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALL 490
Cdd:cd03300 77 VFQNYALFPhLTVFENI----------AFGLRLKKLPkaeikerVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 491 HNAPMLLLDEPTEGLDA----ETERQILALVKEVAVqkTLLMVTH-RLQGLTAFDRIIVMDNGQITEQGSHKEL 559
Cdd:cd03300 147 NEPKVLLLDEPLGALDLklrkDMQLELKRLQKELGI--TFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
341-550 |
2.92e-29 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 115.20 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 341 LRNVSFSYPGQpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAA---LRATMS 417
Cdd:cd03292 3 FINVTKTYPNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQRVHLFSA-TLRDNLLLA------APQADDAALGAVLARVGLEKLLDDEglnawlgegGRQLSGGELRRLGIARALL 490
Cdd:cd03292 82 VVFQDFRLLPDrNVYENVAFAlevtgvPPREIRKRVPAALELVGLSHKHRAL---------PAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163667 491 HNAPMLLLDEPTEGLDAETERQILALVKEV-AVQKTLLMVTHRLQGLTAFD-RIIVMDNGQI 550
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
338-569 |
4.69e-29 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 123.13 E-value: 4.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVmldgvsitgyreaALRATMS 417
Cdd:TIGR00957 636 SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQRVHLFSATLRDNLLLAAPQADD---AALGAVLARVGLEKLldDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAP 494
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENILFGKALNEKyyqQVLEACALLPDLEIL--PSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 495 MLLLDEPTEGLDAETERQILALV---KEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYYQF 569
Cdd:TIGR00957 781 IYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
339-554 |
4.73e-29 |
|
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: 114.66 E-value: 4.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITgYREAALRaTMSV 418
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-DLPPKDR-DIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLF-SATLRDNL-----LLAAPQAD-DAALGAVLARVGLEKLLDDEglnawlgegGRQLSGGELRRLGIARALLH 491
Cdd:cd03301 77 VFQNYALYpHMTVYDNIafglkLRKVPKDEiDERVREVAELLQIEHLLDRK---------PKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 492 NAPMLLLDEPTEGLDAETERQILALVKEV--AVQKTLLMVTH-RLQGLTAFDRIIVMDNGQITEQG 554
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLqqRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
317-559 |
4.90e-29 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 122.97 E-value: 4.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 317 VIDQPADITFAesgkdAPR---EASLSLRNVSFSY-PGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDP 392
Cdd:PTZ00243 1289 VVIEPASPTSA-----APHpvqAGSLVFEGVQMRYrEGLPL-VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEV 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 393 TSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLllaAP--QADDAALGAVLARVGLEKLL--DDEGLNAWL 468
Cdd:PTZ00243 1363 CGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVasESEGIDSRV 1439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 469 GEGGRQLSGGELRRLGIARALL-HNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDN 547
Cdd:PTZ00243 1440 LEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDH 1519
|
250
....*....|..
gi 495163667 548 GQITEQGSHKEL 559
Cdd:PTZ00243 1520 GAVAEMGSPREL 1531
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
316-552 |
5.70e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 120.55 E-value: 5.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 316 DVIDQPADITF---AESGKDApreasLSLRNVSFSYPGQPQpaLRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDP 392
Cdd:COG0488 295 PRRDKTVEIRFpppERLGKKV-----LELEGLSKSYGDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 393 TSGDVML-DGVSItGYreaalratmsvVPQRVHLF--SATLRDNLLLAAPQADDAALGAVLARVGLekllddeglnawlg 469
Cdd:COG0488 368 DSGTVKLgETVKI-GY-----------FDQHQEELdpDKTVLDELRDGAPGGTEQEVRGYLGRFLF-------------- 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 470 EGGRQ------LSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETeRQILalvkEVAVQK---TLLMVTH-R--LQGLT 537
Cdd:COG0488 422 SGDDAfkpvgvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET-LEAL----EEALDDfpgTVLLVSHdRyfLDRVA 496
|
250
....*....|....*
gi 495163667 538 afDRIIVMDNGQITE 552
Cdd:COG0488 497 --TRILEFEDGGVRE 509
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
339-568 |
5.77e-29 |
|
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: 116.11 E-value: 5.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDpTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSATLRDNLllaAP--QADDAALGAVLARVGLEKLLDD--EGLNAWLGEGGRQLSGGELRRLGIARALLHNAP 494
Cdd:cd03289 82 IPQKVFIFSGTFRKNL---DPygKWSDEEIWKVAEEVGLKSVIEQfpGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 495 MLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYYQ 568
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
353-569 |
8.14e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 114.85 E-value: 8.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 353 QPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYRE--------AALRATMSVVPQRVH 424
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgliRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 425 LFS-ATLRDNLLLA------APQADDAALG-AVLARVGLEKLLDDEGlnawlgeggRQLSGGELRRLGIARALLHNAPML 496
Cdd:PRK11264 96 LFPhRTVLENIIEGpvivkgEPKEEATARArELLAKVGLAGKETSYP---------RRLSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 497 LLDEPTEGLDAETERQILALVKEVAVQK-TLLMVTHRLQ-GLTAFDRIIVMDNGQITEQGSHKELLA--QQGRYYQF 569
Cdd:PRK11264 167 LFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKALFAdpQQPRTRQF 243
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
10-552 |
9.69e-29 |
|
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: 120.29 E-value: 9.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 10 LYKRHKWLLSLGVVLAIVTLLASIGLLTLSGWFLSASAVVGMAGLYSFnymlpaagVRGAAIIRTAGRYFERLVSHEGtF 89
Cdd:COG4615 7 LLRESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLF--------AGLLVLLLLSRLASQLLLTRLG-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 90 RVLEHLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRvISPLIGALAVIAVVTLGLSLLDVTLALTLGGI 169
Cdd:COG4615 78 HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPPLFLLTLVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 170 MLATLLLLPPLFYRAGRPVGEAlTMLRASYRQQLTGWLQGQAELSIFGAAGR--YREQLDTTEQVW----HEAQRRQAGL 243
Cdd:COG4615 157 LGLGVAGYRLLVRRARRHLRRA-REAEDRLFKHFRALLEGFKELKLNRRRRRafFDEDLQPTAERYrdlrIRADTIFALA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 244 TALSQAMMTLISGmtvvLILWMAAGGVggnSTPGSLIALFVFCALAAFEALAPVGGAFQHLGQVIASARRVSDV---IDQ 320
Cdd:COG4615 236 NNWGNLLFFALIG----LILFLLPALG---WADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELelaLAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 321 PADITFAESGKDAPRE-ASLSLRNVSFSYPGQPQP---ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGD 396
Cdd:COG4615 309 AEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 397 VMLDGVSITGYREAALRATMSVVPQRVHLFsatlrDNLLLAAPQADDAALGAVLARVGLEKLLDDeglnawlgEGGR--- 473
Cdd:COG4615 389 ILLDGQPVTADNREAYRQLFSAVFSDFHLF-----DRLLGLDGEADPARARELLERLELDHKVSV--------EDGRfst 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 474 -QLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETER----QILALVKevAVQKTLLMVTHRLQGLTAFDRIIVMDNG 548
Cdd:COG4615 456 tDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRvfytELLPELK--ARGKTVIAISHDDRYFDLADRVLKMDYG 533
|
....
gi 495163667 549 QITE 552
Cdd:COG4615 534 KLVE 537
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
339-554 |
1.35e-28 |
|
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: 113.36 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQpalrDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAalRATMSV 418
Cdd:cd03298 1 VRLDKIRFSYGEQPM----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFS-ATLRDNLLLA-AP-----QADDAALGAVLARVGLEkllddeGLNAWLGeggRQLSGGELRRLGIARALLH 491
Cdd:cd03298 75 LFQENNLFAhLTVEQNVGLGlSPglkltAEDRQAIEVALARVGLA------GLEKRLP---GELSGGERQRVALARVLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 492 NAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTA-FDRIIVMDNGQITEQG 554
Cdd:cd03298 146 DKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
338-565 |
1.62e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 115.26 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSY-PGQP--QPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYRE----A 410
Cdd:PRK13646 2 TIRFDNVSYTYqKGTPyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 411 ALRATMSVVPQ--RVHLFSATLRDNLLLAaPQADDAALGAVLARVglEKLLDDEGLNA-WLGEGGRQLSGGELRRLGIAR 487
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFG-PKNFKMNLDEVKNYA--HRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 488 ALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ--KTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQQG 564
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYaDEVIVMKEGSIVSQTSPKELFKDKK 238
|
.
gi 495163667 565 R 565
Cdd:PRK13646 239 K 239
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
339-559 |
1.93e-28 |
|
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: 113.39 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYpGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYR-EAALRATMS 417
Cdd:TIGR03410 1 LEVSNLNVYY-GQSH-ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQRVHLFSA-TLRDNLLLAAPqaddaalgavlARVGLEKLLDDE------GLNAWLGEGGRQLSGGELRRLGIARALL 490
Cdd:TIGR03410 79 YVPQGREIFPRlTVEENLLTGLA-----------ALPRRSRKIPDEiyelfpVLKEMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 491 HNAPMLLLDEPTEGLD----AETERQILALVKEVAVqkTLLMVTHRLQ-GLTAFDRIIVMDNGQITEQGSHKEL 559
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQpsiiKDIGRVIRRLRAEGGM--AILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
338-558 |
3.50e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.37 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSY-PGQP--QPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYRE--AAL 412
Cdd:PRK13637 2 SIKIENLTHIYmEGTPfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 413 RATMSVVPQ--RVHLFSATL-RD------NLLLAAPQADDAALGAvLARVGL--EKLLDDEGLnawlgeggrQLSGGELR 481
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIeKDiafgpiNLGLSEEEIENRVKRA-MNIVGLdyEDYKDKSPF---------ELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 482 RLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKE 558
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPRE 231
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
337-577 |
3.51e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 113.33 E-value: 3.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 337 ASLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATM 416
Cdd:PRK13548 1 AMLEARNLSVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVVPQRVHL-FSATLRDNLLL------AAPQADDAALGAVLARVGLEKLlddeglnawlgeGGR---QLSGGELRRLGIA 486
Cdd:PRK13548 79 AVLPQHSSLsFPFTVEEVVAMgraphgLSRAEDDALVAAALAQVDLAHL------------AGRdypQLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 487 RALL------HNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLqGLTAF--DRIIVMDNGQITEQGSH 556
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDL-NLAARyaDRIVLLHQGRLVADGTP 225
|
250 260
....*....|....*....|...
gi 495163667 557 KELLAQQ--GRYYQFRARsVHYH 577
Cdd:PRK13548 226 AEVLTPEtlRRVYGADVL-VQPH 247
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
329-559 |
4.68e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 112.82 E-value: 4.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 329 SGKDAPREASLSLRNVSFSYpGQpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWD--P---TSGDVMLDGVS 403
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYY-GD-KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 404 I--TGYREAALRATMSVVPQRVHLFSATLRDNLllaapqaddaALGAVL----------ARVglEKLLDDEGLnaW---- 467
Cdd:COG1117 80 IydPDVDVVELRRRVGMVFQKPNPFPKSIYDNV----------AYGLRLhgikskseldEIV--EESLRKAAL--Wdevk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 468 --LGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQ------GLTAF 539
Cdd:COG1117 146 drLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqaarvsDYTAF 225
|
250 260
....*....|....*....|
gi 495163667 540 driivMDNGQITEQGSHKEL 559
Cdd:COG1117 226 -----FYLGELVEFGPTEQI 240
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
355-559 |
5.71e-28 |
|
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: 111.69 E-value: 5.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITgyREAA-LRATMSVVPQRVHLFSA-TLRD 432
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV--REPReVRRRIGIVFQDLSVDDElTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 433 NLLLaapQADDAALGAVLARVGLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQ 512
Cdd:cd03265 93 NLYI---HARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495163667 513 ----ILALVKEVAVqkTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKEL 559
Cdd:cd03265 170 vweyIEKLKEEFGM--TILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
356-560 |
8.68e-28 |
|
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: 111.66 E-value: 8.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAalRATMSVVPQRVHLF-SATLRDNL 434
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 435 -----LLAAPQADDAALGAVLARV-GLEKLLDDEglnawlgegGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAE 508
Cdd:cd03299 93 ayglkKRKVDKKEIERKVLEIAEMlGIDHLLNRK---------PETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 509 TERQILALVKEV--AVQKTLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKELL 560
Cdd:cd03299 164 TKEKLREELKKIrkEFGVTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
341-551 |
1.53e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 116.32 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 341 LRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGvsitgyreaalRATMSVVP 420
Cdd:COG0488 1 LENLSKSFGGRP--LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 421 QRVHLFS-ATLRDNLL------------LAAPQADDAALGAVLARVG-LEKLLDDegLNAW------------LG----E 470
Cdd:COG0488 68 QEPPLDDdLTVLDTVLdgdaelraleaeLEELEAKLAEPDEDLERLAeLQEEFEA--LGGWeaearaeeilsgLGfpeeD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 471 GGRQ---LSGGELRRLGIARALLHNAPMLLLDEPTEGLDAET----ERQILALvkevavQKTLLMVTH-R--LQGLTafD 540
Cdd:COG0488 146 LDRPvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKNY------PGTVLVVSHdRyfLDRVA--T 217
|
250
....*....|.
gi 495163667 541 RIIVMDNGQIT 551
Cdd:COG0488 218 RILELDRGKLT 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
109-568 |
1.69e-27 |
|
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: 118.09 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 109 SGLARFRQGELLNRLVADVDTLDHL-------YLRVISPLIGALAVIAVVTLGLSLLDVTLALTLggIMLatllllPPLF 181
Cdd:TIGR01271 974 AVLNTMKAGRILNRFTKDMAIIDDMlpltlfdFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIF--IML------RAYF 1045
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 182 YRAGRPVGEALTMLRASYRQQLTGWLQGQAELSIFGAAGRYreqldttEQVWHEAQRRQAG-----LTALSQAMMTLisg 256
Cdd:TIGR01271 1046 LRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYF-------ETLFHKALNLHTAnwflyLSTLRWFQMRI--- 1115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 257 mTVVLILWMAAG---GVGGNSTPGSLIALFVFCALAAFEALAPVGGAFQHLGQVIASARRVSDVIDQPAD---------- 323
Cdd:TIGR01271 1116 -DIIFVFFFIAVtfiAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEeprpsggggk 1194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 324 --------ITFAESGKDAPREASLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDpTSG 395
Cdd:TIGR01271 1195 yqlstvlvIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEG 1273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 396 DVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAApQADDAALGAVLARVGLEKLLDD--EGLNAWLGEGGR 473
Cdd:TIGR01271 1274 EIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYE-QWSDEEIWKVAEEVGLKSVIEQfpDKLDFVLVDGGY 1352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 474 QLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQ 553
Cdd:TIGR01271 1353 VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQY 1432
|
490
....*....|....*
gi 495163667 554 GSHKELLAQQGRYYQ 568
Cdd:TIGR01271 1433 DSIQKLLNETSLFKQ 1447
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
354-559 |
2.80e-27 |
|
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: 112.10 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 354 PALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITgyREAA-LRATMSVVPQRVHLFSA-TLR 431
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV--REPRkVRRSIGIVPQYASVDEDlTGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 432 DNLLLaapQADDAALGAVLARVGLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETER 511
Cdd:TIGR01188 85 ENLEM---MGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495163667 512 QILALV-KEVAVQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKEL 559
Cdd:TIGR01188 162 AIWDYIrALKEEGVTILLTTHYMEEADKLcDRIAIIDHGRIIAEGTPEEL 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
339-550 |
1.66e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 108.63 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVS--FsYPGQP--QPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITG---YREAA 411
Cdd:COG1101 2 LELKNLSktF-NPGTVneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlpeYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 412 LRAtmsvvpqRVhlF---------SATLRDNLLLAA------------PQADDAALGAVLARV--GLEKLLDDE-GLnaw 467
Cdd:COG1101 81 YIG-------RV--FqdpmmgtapSMTIEENLALAYrrgkrrglrrglTKKRRELFRELLATLglGLENRLDTKvGL--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 468 lgeggrqLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVaVQK---TLLMVTHRL-QGLTAFDRII 543
Cdd:COG1101 149 -------LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI-VEEnnlTTLMVTHNMeQALDYGNRLI 220
|
....*..
gi 495163667 544 VMDNGQI 550
Cdd:COG1101 221 MMHEGRI 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
341-561 |
2.47e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.95 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 341 LRNVSFSY-PGQP--QPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREA----ALR 413
Cdd:PRK13634 5 FQKVEHRYqYKTPfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 414 ATMSVVPQ--RVHLFSAT-LRDnlLLAAPQ-----ADDAALGA--VLARVGL-EKLLDDEGLnawlgeggrQLSGGELRR 482
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETvEKD--ICFGPMnfgvsEEDAKQKAreMIELVGLpEELLARSPF---------ELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 483 LGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKEL 559
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARYaDQIVVMHKGTVFLQGTPREI 233
|
..
gi 495163667 560 LA 561
Cdd:PRK13634 234 FA 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
336-559 |
3.02e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.42 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 336 EASLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDG--VSITGYREaALR 413
Cdd:COG1129 2 EPLLEMRGISKSFGGVK--ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRD-AQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 414 ATMSVVPQRVHLFSA-TLRDNLLLAAPQA-----DDAAL----GAVLARVGLE----KLLDDeglnawLGEGGRQLsgge 479
Cdd:COG1129 79 AGIAIIHQELNLVPNlSVAENIFLGREPRrggliDWRAMrrraRELLARLGLDidpdTPVGD------LSVAQQQL---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 480 lrrLGIARALLHNAPMLLLDEPTEGL-DAETERqILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSH 556
Cdd:COG1129 149 ---VEIARALSRDARVLILDEPTASLtEREVER-LFRIIRRLKAQgVAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPV 224
|
...
gi 495163667 557 KEL 559
Cdd:COG1129 225 AEL 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
334-561 |
3.09e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 114.45 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 334 PREASLSLRNVSFSY-PGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDvmldgvsitgyrEAAL 412
Cdd:PLN03130 610 PGLPAISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA------------SVVI 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 413 RATMSVVPQRVHLFSATLRDNLLLAAPqADDAALGAVLARVGLEKLLD--DEGLNAWLGEGGRQLSGGELRRLGIARALL 490
Cdd:PLN03130 678 RGTVAYVPQVSWIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDllPGGDLTEIGERGVNISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163667 491 HNAPMLLLDEPTEGLDAETERQIL-ALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLA 561
Cdd:PLN03130 757 SNSDVYIFDDPLSALDAHVGRQVFdKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
347-545 |
3.69e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.78 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 347 SYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVmldgvsitgyrEAALRATMSVVPQRVHL- 425
Cdd:NF040873 1 GYGGRP--VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 426 --FSATLRD----------NLLLAAPQADDAALGAVLARVGLEKLLddeglNAWLGEggrqLSGGELRRLGIARALLHNA 493
Cdd:NF040873 68 dsLPLTVRDlvamgrwarrGLWRRLTRDDRAAVDDALERVGLADLA-----GRQLGE----LSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495163667 494 PMLLLDEPTEGLDAETERQILALVKE-VAVQKTLLMVTHRLQGLTAFDRIIVM 545
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
339-545 |
8.08e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.57 E-value: 8.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:PRK10247 8 LQLQNVGYLAGDAK--ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSATLRDNLL----LAAPQADDAALGAVLARVGLEKLLDDEGLNAwlgeggrqLSGGELRRLGIARALLHNAP 494
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIfpwqIRNQQPDPAIFLDDLERFALPDTILTKNIAE--------LSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495163667 495 MLLLDEPTEGLDAETERQILALVKEVAVQKTL--LMVTHRLQGLTAFDRIIVM 545
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIavLWVTHDKDEINHADKVITL 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
338-556 |
9.70e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 105.87 E-value: 9.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYpGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVmldgvSITGYR--------- 408
Cdd:PRK11124 2 SIQLNGINCFY-GAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL-----NIAGNHfdfsktpsd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 409 --EAALRATMSVVPQRVHLFS-ATLRDNLL--------LAAPQADDAALgAVLARVGLEKLLDDEGLnawlgeggrQLSG 477
Cdd:PRK11124 75 kaIRELRRNVGMVFQQYNLWPhLTVQQNLIeapcrvlgLSKDQALARAE-KLLERLRLKPYADRFPL---------HLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 478 GELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK-TLLMVTHRLQ-GLTAFDRIIVMDNGQITEQGS 555
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEvARKTASRVVYMENGHIVEQGD 224
|
.
gi 495163667 556 H 556
Cdd:PRK11124 225 A 225
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
356-576 |
1.11e-25 |
|
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: 105.63 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITgyREAALRAtmsVVPQRVHLFS-ATLRDNL 434
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT--EPGPDRM---VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 435 LLAApqadDAALgAVLARVGLEKLLDDE----GLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAET- 509
Cdd:TIGR01184 76 ALAV----DRVL-PDLSKSERRAIVEEHialvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTr 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 510 ---ERQILALVKEVAVqkTLLMVTHRL-QGLTAFDRIIVMDN------GQITE----QGSHKELLAQQGRYYQFRARSVH 575
Cdd:TIGR01184 151 gnlQEELMQIWEEHRV--TVLMVTHDVdEALLLSDRVVMLTNgpaaniGQILEvpfpRPRDRLEVVEDPSYYDLRNEALY 228
|
.
gi 495163667 576 Y 576
Cdd:TIGR01184 229 F 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
77-559 |
1.96e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 111.99 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 77 RYFERlVSHEGtFRVLEHLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYL----------RVISPLIGALA 146
Cdd:PLN03232 360 QYFQN-VGRVG-FRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEqlhglwsapfRIIVSMVLLYQ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 147 VIAVVTLGLSLLDVTLALTLGGIMLATLLLLPPLFYRAGRPVGEALTMLRASYRQQLTGW-------LQG--QAELSIFG 217
Cdd:PLN03232 438 QLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWeksfesrIQGirNEELSWFR 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 218 AAgryreQLdtteqvwheaqrrqagLTALSQAMM-------TLISGMTVVLIlwmaaggvGGNSTPGSlialfVFCALAA 290
Cdd:PLN03232 518 KA-----QL----------------LSAFNSFILnsipvvvTLVSFGVFVLL--------GGDLTPAR-----AFTSLSL 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 291 FEAL-APVGGAFQHLGQVI---ASARRVSDVIDQPADItFAESGKDAPREASLSLRNVSFSYPGQ-PQPALRDITLDVAP 365
Cdd:PLN03232 564 FAVLrSPLNMLPNLLSQVVnanVSLQRIEELLLSEERI-LAQNPPLQPGAPAISIKNGYFSWDSKtSKPTLSDINLEIPV 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 366 GEHIAILGRTGCGKSTLLQlitrawdptsgdVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAA---PQAD 442
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLIS------------AMLGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSdfeSERY 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 443 DAALGAVLARVGLEkLLDDEGLNAwLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQIL-ALVKEVA 521
Cdd:PLN03232 711 WRAIDVTALQHDLD-LLPGRDLTE-IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdSCMKDEL 788
|
490 500 510
....*....|....*....|....*....|....*...
gi 495163667 522 VQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKEL 559
Cdd:PLN03232 789 KGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
339-549 |
3.55e-25 |
|
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: 101.37 E-value: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREaalratmsv 418
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFE--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 vpqrvhlfsatlrdnlllaapqaddaalgavlarvglekllddeglnawlgeggrQLSGGELRRLGIARALLHNAPMLLL 498
Cdd:cd03221 70 -------------------------------------------------------QLSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 499 DEPTEGLDAETerqILALvkEVAVQK---TLLMVTH-R--LQGLTafDRIIVMDNGQ 549
Cdd:cd03221 95 DEPTNHLDLES---IEAL--EEALKEypgTVILVSHdRyfLDQVA--TKIIELEDGK 144
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
338-559 |
4.01e-25 |
|
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: 103.96 E-value: 4.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITgyREAALRATMS 417
Cdd:cd03296 2 SIEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQRVHLFS-ATLRDNL---LLAAPQADDAALGAVLARVglEKLLDDEGLNaWLGEggR---QLSGGELRRLGIARALL 490
Cdd:cd03296 78 FVFQHYALFRhMTVFDNVafgLRVKPRSERPPEAEIRAKV--HELLKLVQLD-WLAD--RypaQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163667 491 HNAPMLLLDEPTEGLDAETERQILALVKEV--AVQKTLLMVTH-RLQGLTAFDRIIVMDNGQITEQGSHKEL 559
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLhdELHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
333-559 |
4.80e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 105.97 E-value: 4.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 333 APREASLSLRNVSFSYP------GQPQPALR---DITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVS 403
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPvrgglfGRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 404 ITGYREAALRA---TMSVVPQ----------RV-HLFSATLRDNLLLAAPQADDAALgAVLARVGleklLDDEGLNawlg 469
Cdd:COG4608 82 ITGLSGRELRPlrrRMQMVFQdpyaslnprmTVgDIIAEPLRIHGLASKAERRERVA-ELLELVG----LRPEHAD---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 470 eggR---QLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEvaVQK----TLLMVTHrlqGLTAF--- 539
Cdd:COG4608 153 ---RyphEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLED--LQDelglTYLFISH---DLSVVrhi 224
|
250 260
....*....|....*....|.
gi 495163667 540 -DRIIVMDNGQITEQGSHKEL 559
Cdd:COG4608 225 sDRVAVMYLGKIVEIAPRDEL 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
314-559 |
5.18e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.84 E-value: 5.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 314 VSDVIDQPAditfAESGKDAprEASLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPT 393
Cdd:PRK11607 1 MNDAIPRPQ----AKTRKAL--TPLLEIRNLTKSFDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 394 SGDVMLDGVSITgyREAALRATMSVVPQRVHLFS-ATLRDNLLLAAPQaDDAALGAVLARVglEKLLDDEGLNAWLGEGG 472
Cdd:PRK11607 73 AGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPhMTVEQNIAFGLKQ-DKLPKAEIASRV--NEMLGLVHMQEFAKRKP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 473 RQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAE----TERQILALVKEVAVqkTLLMVTH-RLQGLTAFDRIIVMDN 547
Cdd:PRK11607 148 HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERVGV--TCVMVTHdQEEAMTMAGRIAIMNR 225
|
250
....*....|..
gi 495163667 548 GQITEQGSHKEL 559
Cdd:PRK11607 226 GKFVQIGEPEEI 237
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
339-563 |
8.78e-25 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 103.84 E-value: 8.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSATLRDNLLLAAPQADDaALGAVLARVGLEKLLDD--EGLNAWLGEGGRQLSGGELRRLGIARALLHNAPML 496
Cdd:cd03288 100 ILQDPILFSGSIRFNLDPECKCTDD-RLWEALEIAQLKNMVKSlpGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 497 LLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQ 563
Cdd:cd03288 179 IMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
336-569 |
1.28e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 109.35 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 336 EASLSLRNVSFSYPGQPQ-PALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWD----------------------- 391
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 392 -------------------------------PTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAAPQ 440
Cdd:PTZ00265 1243 qgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 441 A--DDAALGAVLARVG--LEKLLDDEGLNawLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILAL 516
Cdd:PTZ00265 1323 AtrEDVKRACKFAAIDefIESLPNKYDTN--VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163667 517 VKEV--AVQKTLLMVTHRLQGLTAFDRIIVMDNGQ-----ITEQGSHKELL-AQQGRYYQF 569
Cdd:PTZ00265 1401 IVDIkdKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLsVQDGVYKKY 1461
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
338-556 |
1.76e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDG--------VSITGYRE 409
Cdd:COG4161 2 SIQLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 410 aaLRATMSVVPQRVHLFS-ATLRDNLLlAAP---------QADDAALGaVLARVGLEKLLDDEGLnawlgeggrQLSGGE 479
Cdd:COG4161 80 --LRQKVGMVFQQYNLWPhLTVMENLI-EAPckvlglskeQAREKAMK-LLARLRLTDKADRFPL---------HLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 480 LRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK-TLLMVTHRLQ-GLTAFDRIIVMDNGQITEQGSH 556
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEfARKVASQVVYMEKGRIIEQGDA 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
339-554 |
2.02e-24 |
|
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: 101.14 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRatMSV 418
Cdd:cd03268 1 LKTNDLTKTYGKKR--VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR--IGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSA-TLRDNLLLAA--PQADDAALGAVLARVGLEkllDDEGLNAwlgeggRQLSGGELRRLGIARALLHNAPM 495
Cdd:cd03268 77 LIEAPGFYPNlTARENLRLLArlLGIRKKRIDEVLDVVGLK---DSAKKKV------KGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163667 496 LLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQITEQG 554
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
339-562 |
2.35e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 107.08 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQ---------PQPALRDITLDVAPGEHIAILGRTGCGKSTL----LQLItrawdPTSGDVMLDGVSIT 405
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 406 GYREAALRAT---MSVVPQ----------RVhlfSATLRDNLLLAAPQADDAAL----GAVLARVGleklLDDEGLNAWL 468
Cdd:COG4172 351 GLSRRALRPLrrrMQVVFQdpfgslsprmTV---GQIIAEGLRVHGPGLSAAERrarvAEALEEVG----LDPAARHRYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 469 GEggrqLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEvaVQK----TLLMVTHRLQGLTAF-DRII 543
Cdd:COG4172 424 HE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRD--LQRehglAYLFISHDLAVVRALaHRVM 497
|
250
....*....|....*....
gi 495163667 544 VMDNGQITEQGSHKELLAQ 562
Cdd:COG4172 498 VMKDGKVVEQGPTEQVFDA 516
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
338-547 |
2.68e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.02 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYPGQPQpaLRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDP---TSGDVMLDGVSITGYreAALRA 414
Cdd:COG4136 1 MLSLENLTITLGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAL--PAEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 415 TMSVVPQRVHLFS-ATLRDNLLLAAP-----QADDAALGAVLARVGLEkllddeglnawlGEGGR---QLSGGELRRLGI 485
Cdd:COG4136 77 RIGILFQDDLLFPhLSVGENLAFALPptigrAQRRARVEQALEEAGLA------------GFADRdpaTLSGGQRARVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 486 ARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTL--LMVTHRLQGLTAFDRIIVMDN 547
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpaLLVTHDEEDAPAAGRVLDLGN 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
338-559 |
2.83e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.90 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSY-PGQP--QPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYRE----A 410
Cdd:PRK13649 2 GINLQNVSYTYqAGTPfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 411 ALRATMSVVPQ--RVHLFSAT-LRD------NLLLAAPQADDAALGAvLARVGL-EKLLDDEGLnawlgeggrQLSGGEL 480
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETvLKDvafgpqNFGVSQEEAEALAREK-LALVGIsESLFEKNPF---------ELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 481 RRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKE 558
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGKPKD 231
|
.
gi 495163667 559 L 559
Cdd:PRK13649 232 I 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
334-559 |
2.83e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.96 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 334 PREASLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGD---VMLDGVSITGYREA 410
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 411 ALRATMSVVPQRvhlfsatlRDNLLLAAPQADDAALG----------------AVLARVGLEKLLDDEGLNawlgeggrq 474
Cdd:PRK13640 81 DIREKVGIVFQN--------PDNQFVGATVGDDVAFGlenravprpemikivrDVLADVGMLDYIDSEPAN--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 475 LSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTAFDRIIVMDNGQITE 552
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLA 223
|
....*..
gi 495163667 553 QGSHKEL 559
Cdd:PRK13640 224 QGSPVEI 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
339-562 |
3.41e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 106.31 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRN--VSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKS----TLLQLITRAWDPTSGDVMLDGVSITGYREAAL 412
Cdd:COG4172 7 LSVEDlsVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 413 RA------TM-------SVVPqrvhLFS------ATLRDNLLLAAPQADDAALgAVLARVGLEkllDDEG-LNAWlgegG 472
Cdd:COG4172 87 RRirgnriAMifqepmtSLNP----LHTigkqiaEVLRLHRGLSGAAARARAL-ELLERVGIP---DPERrLDAY----P 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 473 RQLSGGELRRLGIARALLhNAPMLLL-DEPTEGLDAETERQILALVKEVaVQKT---LLMVTHRLqGLTA--FDRIIVMD 546
Cdd:COG4172 155 HQLSGGQRQRVMIAMALA-NEPDLLIaDEPTTALDVTVQAQILDLLKDL-QRELgmaLLLITHDL-GVVRrfADRVAVMR 231
|
250
....*....|....*.
gi 495163667 547 NGQITEQGSHKELLAQ 562
Cdd:COG4172 232 QGEIVEQGPTAELFAA 247
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
343-563 |
4.47e-24 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 102.24 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 343 NVSFS-YPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGvsitgyreaalraTMSVVPQ 421
Cdd:cd03291 39 NLFFSnLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 422 RVHLFSATLRDNLLLAApQADDAALGAVLARVGLEKLLDD--EGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLD 499
Cdd:cd03291 106 FSWIMPGTIKENIIFGV-SYDEYRYKSVVKACQLEEDITKfpEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 500 EPTEGLDAETERQIL-ALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQ 563
Cdd:cd03291 185 SPFGYLDVFTEKEIFeSCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
338-562 |
5.72e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 101.24 E-value: 5.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYpgQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMS 417
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQrVHLF--SATLRD----------NLLLAAPQADDAALGAVLARVGL----EKLLDDeglnawlgeggrqLSGGELR 481
Cdd:PRK11231 80 LLPQ-HHLTpeGITVRElvaygrspwlSLWGRLSAEDNARVNQAMEQTRInhlaDRRLTD-------------LSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 482 RLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKEL 559
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEV 225
|
...
gi 495163667 560 LAQ 562
Cdd:PRK11231 226 MTP 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
345-554 |
5.73e-24 |
|
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: 100.13 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 345 SFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSiTGYREAALRATMSVVPQRVH 424
Cdd:cd03266 10 RFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-VVKEPAEARRRLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 425 LFS-ATLRDNLLLAAP---QADDAALGAVlarvglEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDE 500
Cdd:cd03266 89 LYDrLTARENLEYFAGlygLKGDELTARL------EELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 501 PTEGLDAETERQILALVKEV-AVQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQG 554
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
339-561 |
7.03e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.60 E-value: 7.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPgQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYRE-AALRATMS 417
Cdd:PRK13644 2 IRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQ--RVHLFSATLRDNLllaAPQADDAALGAVLARVGLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPM 495
Cdd:PRK13644 81 IVFQnpETQFVGRTVEEDL---AFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 496 LLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLA 561
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
339-552 |
1.22e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.53 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYP-------GQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAA 411
Cdd:PRK10419 4 LNVSGLSHHYAhgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 412 LRA-----------TMSVVPQRvHLFSATLRDNL--LLAAPQADDAA-LGAVLARVGleklLDDEGLNAWLGeggrQLSG 477
Cdd:PRK10419 84 RKAfrrdiqmvfqdSISAVNPR-KTVREIIREPLrhLLSLDKAERLArASEMLRAVD----LDDSVLDKRPP----QLSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 478 GELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ--KTLLMVTHRLQGLTAF-DRIIVMDNGQITE 552
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfgTACLFITHDLRLVERFcQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
338-563 |
1.24e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.06 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSY-PGQPQPA--LRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREA---- 410
Cdd:PRK13641 2 SIKFENVDYIYsPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 411 ALRATMSVVPQ--RVHLFSAT-LRD------NLLLAAPQADDAALgAVLARVGL-EKLLDDEGLnawlgeggrQLSGGEL 480
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTvLKDvefgpkNFGFSEDEAKEKAL-KWLKKVGLsEDLISKSPF---------ELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 481 RRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEvaVQK---TLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSH 556
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKD--YQKaghTVILVTHNMDDVAEYaDDVLVLEHGKLIKHASP 229
|
....*..
gi 495163667 557 KELLAQQ 563
Cdd:PRK13641 230 KEIFSDK 236
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
338-554 |
1.42e-23 |
|
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: 99.27 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYPGQPQPA--LRDITLDVAPGEHIAILGRTGCGKSTLLQLIT---RAWDPTSGDVMLDGVSITgyreaal 412
Cdd:cd03234 3 VLPWWDVGLKAKNWNKYAriLNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 413 RATM----SVVPQ----------RVHL-FSATLRDNLLLAAPQ----ADDAALGAV-LARVGLEKLlddeglnawlgegg 472
Cdd:cd03234 76 PDQFqkcvAYVRQddillpgltvRETLtYTAILRLPRKSSDAIrkkrVEDVLLRDLaLTRIGGNLV-------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 473 RQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVT-H--RLQGLTAFDRIIVMDNGQ 549
Cdd:cd03234 142 KGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTiHqpRSDLFRLFDRILLLSSGE 221
|
....*
gi 495163667 550 ITEQG 554
Cdd:cd03234 222 IVYSG 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
338-562 |
1.50e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 102.15 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLI----TrawdPTSGDVMLDGVSITGYREAALR 413
Cdd:COG1118 2 SIEVRNISKRFGSFT--LLDDVSLEIASGELVALLGPSGSGKTTLLRIIagleT----PDSGRIVLNGRDLFTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 414 AtMSVVPQ-----RvHLfsaTLRDNL---LLAAPQADDAALGAV---LARVGLEKLlddeglnawlgeGGR---QLSGGE 479
Cdd:COG1118 76 R-VGFVFQhyalfP-HM---TVAENIafgLRVRPPSKAEIRARVeelLELVQLEGL------------ADRypsQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 480 LRRLGIARALLHNAPMLLLDEPTEGLDA----ETERQILALVKEVAVqkTLLMVTH-RLQGLTAFDRIIVMDNGQITEQG 554
Cdd:COG1118 139 RQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDELGG--TTVFVTHdQEEALELADRVVVMNQGRIEQVG 216
|
....*...
gi 495163667 555 SHKELLAQ 562
Cdd:COG1118 217 TPDEVYDR 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
339-554 |
1.55e-23 |
|
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: 98.89 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYpGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSIT-------GY--RE 409
Cdd:cd03269 1 LEVENVTKRF-GRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiaarnriGYlpEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 410 AALRATMSVVPQRVHLfsATLRD-NLLLAAPQADDAalgavlarvgLEKLlddeGLNAWLGEGGRQLSGGELRRLGIARA 488
Cdd:cd03269 79 RGLYPKMKVIDQLVYL--AQLKGlKKEEARRRIDEW----------LERL----ELSEYANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 489 LLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQITEQG 554
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
339-567 |
1.78e-23 |
|
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: 99.15 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYpgQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITG---YREAalRAT 415
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmHKRA--RLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 416 MSVVPQRVHLF-SATLRDNLLLAAPQADDAA------LGAVLARVGLEKLLDDEGLnawlgeggrQLSGGELRRLGIARA 488
Cdd:cd03218 77 IGYLPQEASIFrKLTVEENILAVLEIRGLSKkereekLEELLEEFHITHLRKSKAS---------SLSGGERRRVEIARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 489 LLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVT-HRL-QGLTAFDRIIVMDNGQITEQGSHKELLAQQG-- 564
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAANELvr 227
|
...
gi 495163667 565 RYY 567
Cdd:cd03218 228 KVY 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
338-565 |
2.63e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 100.18 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSIT-------GY--R 408
Cdd:COG4152 1 MLELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDpedrrriGYlpE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 409 EAALRATMSVVPQRVHLfsATLRDnllLAAPQADDAAlgavlarvglEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARA 488
Cdd:COG4152 79 ERGLYPKMKVGEQLVYL--ARLKG---LSKAEAKRRA----------DEWLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 489 LLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQQGR 565
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
339-547 |
2.75e-23 |
|
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: 96.45 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVmldgvsitgyrEAALRATMSV 418
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSATLRDNLLLAapqaddaalgavlarvglekllddeglnaWlgegGRQLSGGELRRLGIARALLHNAPMLLL 498
Cdd:cd03223 69 LPQRPYLPLGTLREQLIYP-----------------------------W----DDVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495163667 499 DEPTEGLDAETERQILALVKEVAVqkTLLMVTHRLQGLTAFDRIIVMDN 547
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKELGI--TVISVGHRPSLWKFHDRVLDLDG 162
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
339-560 |
3.20e-23 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 99.49 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSY-------PGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSIT---GYR 408
Cdd:TIGR02769 3 LEVRDVTHTYrtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 409 EAALRATMSVVPQ-RVHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLDDEGLNA-WLGEGGRQLSGGELRRLGIA 486
Cdd:TIGR02769 83 RRAFRRDVQLVFQdSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 487 RALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTL--LMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELL 560
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQLL 239
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
336-562 |
4.39e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.42 E-value: 4.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 336 EASLSLRNVSFSY-PGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRA 414
Cdd:PRK13650 2 SNIIEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 415 TMSVVPQRvhlfsatlRDNLLLAAPQADDAALGavLARVGLEKLLDDEGLNAWLGEGGRQ---------LSGGELRRLGI 485
Cdd:PRK13650 82 KIGMVFQN--------PDNQFVGATVEDDVAFG--LENKGIPHEEMKERVNEALELVGMQdfkereparLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 486 ARALLHNAPMLLLDEPTEGLDAETERQILALVKEV--AVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQ 562
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrdDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
339-562 |
4.77e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.00 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITgYREAAL---RAT 415
Cdd:PRK13639 2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 416 MSVVPQRvhlfsatlRDNLLLAAPQADDAALGAV---LARVGLEKLLDDE----GLNAWLGEGGRQLSGGELRRLGIARA 488
Cdd:PRK13639 80 VGIVFQN--------PDDQLFAPTVEEDVAFGPLnlgLSKEEVEKRVKEAlkavGMEGFENKPPHHLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 489 LLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK-TLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQ 562
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGiTIIISTHDVDLVPVYaDKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
354-554 |
5.36e-23 |
|
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: 97.79 E-value: 5.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 354 PALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVsITGYREAALRATMSVV-PQRVHL-FSATLR 431
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVfGQKTQLwWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 432 DNLLLAAP--QADDAALGAVLARvgLEKLLDdegLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAET 509
Cdd:cd03267 114 DSFYLLAAiyDLPPARFKKRLDE--LSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495163667 510 ERQILALVKEVAVQK--TLLMVTHRLQGLTAF-DRIIVMDNGQITEQG 554
Cdd:cd03267 189 QENIRNFLKEYNRERgtTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
356-553 |
8.63e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.19 E-value: 8.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAA---LR-ATMSVVPQRVHL---FSA 428
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQKLGFIYQFHHLlpdFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 429 --TLRDNLLL---AAPQADDAALgAVLARVGLEKLLDDEglnawlgegGRQLSGGELRRLGIARALLHNAPMLLLDEPTE 503
Cdd:PRK11629 105 leNVAMPLLIgkkKPAEINSRAL-EMLAAVGLEHRANHR---------PSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495163667 504 GLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTAFDRIIVMDNGQITEQ 553
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
339-561 |
1.07e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 97.46 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSypgQPQPALRDITLDVAPGEHIAILGRTGCGKS----TLLQLITRAWDPTSGDVMLDGVSITGyreAALRA 414
Cdd:PRK10418 5 IELRNIALQ---AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP---CALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 415 -TMSVVPQR-------VHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLDDEGLNAWlgeggrQLSGGELRRLGIA 486
Cdd:PRK10418 79 rKIATIMQNprsafnpLHTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYPF------EMSGGMLQRMMIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 487 RALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTL--LMVTHRLqGLTA--FDRIIVMDNGQITEQGSHKELLA 561
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDM-GVVArlADDVAVMSHGRIVEQGDVETLFN 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
354-576 |
1.11e-22 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 103.07 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 354 PALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGvsitgyreaalraTMSVVPQRVHLFSATLRDN 433
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 434 LLLAApQADDAALGAVLARVGLEKLLD--DEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETER 511
Cdd:TIGR01271 507 IIFGL-SYDEYRYTSVIKACQLEEDIAlfPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 512 QIL-ALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYYQFRARSVHY 576
Cdd:TIGR01271 586 EIFeSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAF 651
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
356-554 |
1.13e-22 |
|
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: 96.21 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVA---PGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGvsiTGYREAALRATMSV-------VPQRVHL 425
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG---TVLFDSRKKINLPPqqrkiglVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 426 FS-ATLRDNLLLAAPQADDAALgavlaRVGLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEG 504
Cdd:cd03297 87 FPhLNVRENLAFGLKRKRNRED-----RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495163667 505 LDAETERQILALVKEVA--VQKTLLMVTHRLQGL-TAFDRIIVMDNGQITEQG 554
Cdd:cd03297 162 LDRALRLQLLPELKQIKknLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
339-531 |
1.89e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.69 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGyrEAALRAtmsV 418
Cdd:PRK11248 2 LQISHLYADYGGKP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--PGAERG---V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFS-ATLRDNL-----LLAAPQAD-DAALGAVLARVGLEkllddeglnawlGEGGR---QLSGGELRRLGIARA 488
Cdd:PRK11248 75 VFQNEGLLPwRNVQDNVafglqLAGVEKMQrLEIAHQMLKKVGLE------------GAEKRyiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495163667 489 LLHNAPMLLLDEPTEGLDAETERQILALVKEV--AVQKTLLMVTH 531
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITH 187
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
355-566 |
2.10e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 98.24 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVmldgvSITGY----REAALRATMSVV-PQRVHLF-SA 428
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV-----RVLGYvpfkRRKEFARRIGVVfGQRSQLWwDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 429 TLRDNL-LLAAP-QADDAALGAVLARvgLEKLLDDEGLnawLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLD 506
Cdd:COG4586 112 PAIDSFrLLKAIyRIPDAEYKKRLDE--LVELLDLGEL---LDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163667 507 AETERQILALVKEVAVQK--TLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQQGRY 566
Cdd:COG4586 187 VVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
336-550 |
2.18e-22 |
|
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: 94.42 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 336 EASLSLRNVSFSypgqpqPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYR-EAALRA 414
Cdd:cd03215 2 EPVLEVRGLSVK------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 415 TMSVVP---QRVHLF-SATLRDNLLLaapqaddaalgavlarvglekllddeglnawlgegGRQLSGGELRRLGIARALL 490
Cdd:cd03215 76 GIAYVPedrKREGLVlDLSVAENIAL-----------------------------------SSLLSGGNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163667 491 HNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQI 550
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
339-563 |
2.49e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 97.23 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREA--ALRATM 416
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVVPQRvhlfsatlRDNLLLAAPQADDAALGAV----------------LARVGLEKLLDdeglnawlgEGGRQLSGGEL 480
Cdd:PRK13636 85 GMVFQD--------PDNQLFSASVYQDVSFGAVnlklpedevrkrvdnaLKRTGIEHLKD---------KPTHCLSFGQK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 481 RRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVA--VQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHK 557
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQkeLGLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPK 227
|
....*.
gi 495163667 558 ELLAQQ 563
Cdd:PRK13636 228 EVFAEK 233
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
340-560 |
4.09e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.92 E-value: 4.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 340 SLRNVSFSYpgQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVV 419
Cdd:COG4604 3 EIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 420 PQRVHLFSA-TLRDnllLAA----P-------QADDAALGAVLARVGLEKL----LDdeglnawlgeggrQLSGGELRRL 483
Cdd:COG4604 81 RQENHINSRlTVRE---LVAfgrfPyskgrltAEDREIIDEAIAYLDLEDLadryLD-------------ELSGGQRQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 484 GIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVA--VQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELL 560
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINFASCYaDHIVAMKDGRVVAQGTPEEII 224
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
348-531 |
5.81e-22 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 93.64 E-value: 5.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 348 YPGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSItGYREAALRAtmsvVPQRVHLFS 427
Cdd:TIGR01166 1 YPGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLE----RRQRVGLVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 428 ATlRDNLLLAAPQADDAALGA---------VLARVG--LEKLlddeGLNAWLGEGGRQLSGGELRRLGIARALLHNAPML 496
Cdd:TIGR01166 75 QD-PDDQLFAADVDQDVAFGPlnlglseaeVERRVReaLTAV----GASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 495163667 497 LLDEPTEGLDAETERQILALVKE-VAVQKTLLMVTH 531
Cdd:TIGR01166 150 LLDEPTAGLDPAGREQMLAILRRlRAEGMTVVISTH 185
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
342-562 |
9.59e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.54 E-value: 9.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 342 RNVSFSY----PGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREA-ALRATM 416
Cdd:PRK13633 8 KNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVVPQRvhlfsatlRDNLLLAAPQADDAALGA---------VLARVglEKLLDDEGLNAWLGEGGRQLSGGELRRLGIAR 487
Cdd:PRK13633 88 GMVFQN--------PDNQIVATIVEEDVAFGPenlgippeeIRERV--DESLKKVGMYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 488 ALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLAQ 562
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
356-570 |
1.21e-21 |
|
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: 96.72 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVA---PGEHI-AILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREA----ALRATMSVVPQRVHLFS 427
Cdd:TIGR02142 9 LGDFSLDADftlPGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiflpPEKRRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 428 -ATLRDNLLLAAPQADDAalgavLARVGLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLD 506
Cdd:TIGR02142 89 hLSVRGNLRYGMKRARPS-----ERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 507 AETERQILALVKEVA--VQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQQGRYYQFR 570
Cdd:TIGR02142 164 DPRKYEILPYLERLHaeFGIPILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWASPDLPWLAR 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
337-550 |
6.34e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.72 E-value: 6.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 337 ASLSLRNVSFSYPGQPQP--ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAAL-- 412
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 413 --RATMSVVPQRVHLFSAtlrdnlLLAAPQADDAALGAVLARVglEKLLDDEGLNAWLGEGGR------QLSGGELRRLG 484
Cdd:PRK10535 83 lrREHFGFIFQRYHLLSH------LTAAQNVEVPAVYAGLERK--QRLLRAQELLQRLGLEDRveyqpsQLSGGQQQRVS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 485 IARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAFDRIIVMDNGQI 550
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
356-562 |
6.95e-21 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 94.40 E-value: 6.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDV---APGEHI-AILGRTGCGKSTLLQLITRAWDPTSGDVMLDGV----SITGYREAALRATMSVVPQRVHLFS 427
Cdd:COG4148 11 RGGFTLDVdftLPGRGVtALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 428 -ATLRDNLLL----AAPQADDAALGAVLARVGLEKLLDdeglnawlgeggR---QLSGGELRRLGIARALLHNAPMLLLD 499
Cdd:COG4148 91 hLSVRGNLLYgrkrAPRAERRISFDEVVELLGIGHLLD------------RrpaTLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 500 EPTEGLDAETERQIL----ALVKEVAVqkTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQ 562
Cdd:COG4148 159 EPLAALDLARKAEILpyleRLRDELDI--PILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
346-548 |
8.24e-21 |
|
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: 91.24 E-value: 8.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 346 FSYpGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRA----TMSVVPQ 421
Cdd:cd03290 8 FSW-GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSrnrySVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 422 RVHLFSATLRDNLLLAAPqADDAALGAVLARVGLEKLLD--DEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLD 499
Cdd:cd03290 87 KPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDllPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495163667 500 EPTEGLDAE-----TERQILALVKEvaVQKTLLMVTHRLQGLTAFDRIIVMDNG 548
Cdd:cd03290 166 DPFSALDIHlsdhlMQEGILKFLQD--DKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
356-569 |
8.56e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.95 E-value: 8.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREA-------------ALRATMSVVPQR 422
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 423 VHLFS-ATLRDNLLLAAPQAddAALGAVLARVGLEKLLDDEGLN-AWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDE 500
Cdd:PRK10619 101 FNLWShMTVLENVMEAPIQV--LGLSKQEARERAVKYLAKVGIDeRAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 501 PTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQgltaFDR-----IIVMDNGQITEQGSHKELLA--QQGRYYQF 569
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMG----FARhvsshVIFLHQGKIEEEGAPEQLFGnpQSPRLQQF 251
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
333-566 |
9.85e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.47 E-value: 9.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 333 APREASLslrNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSG-----DVMLDGVSITGY 407
Cdd:PRK14271 19 APAMAAV---NLTLGFAGKT--VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 408 REA-ALRATMSVVPQRVHLFSATLRDNLLLAA------PQADDAALG-AVLARVGLEKLLDDEglnawLGEGGRQLSGGE 479
Cdd:PRK14271 94 RDVlEFRRRVGMLFQRPNPFPMSIMDNVLAGVrahklvPRKEFRGVAqARLTEVGLWDAVKDR-----LSDSPFRLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 480 LRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKE 558
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQ 248
|
250
....*....|...
gi 495163667 559 LL-----AQQGRY 566
Cdd:PRK14271 249 LFsspkhAETARY 261
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
356-560 |
1.05e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.88 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLITrAWDPT----SGDVMLDGVSITGYReaaLRAtMSVVPQRVHLF--SAT 429
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKE---MRA-ISAYVQQDDLFipTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 430 LRDNLLLAAPQADDAALGAVLARVGLEKLLDDEGL----NAWLGEGGRQ--LSGGELRRLGIARALLHNAPMLLLDEPTE 503
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLrkcaNTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163667 504 GLDAETERQILALVKEVAVQ-KTLLMVTH----RLQGLtaFDRIIVMDNGQITEQGSHKELL 560
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKgKTIICTIHqpssELFEL--FDKIILMAEGRVAYLGSPDQAV 255
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
336-559 |
1.25e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.38 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 336 EASLSLRNVSFSYpgQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWD-----PTSGDVMLDGVSITGYR-- 408
Cdd:PRK14239 3 EPILQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 409 EAALRATMSVVPQRVHLFSATLRDNL---LLAAPQADDAALGAVLarvglEKLLddEGLNAW------LGEGGRQLSGGE 479
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFPMSIYENVvygLRLKGIKDKQVLDEAV-----EKSL--KGASIWdevkdrLHDSALGLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 480 LRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKE 558
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYNDTKQ 233
|
.
gi 495163667 559 L 559
Cdd:PRK14239 234 M 234
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
339-562 |
3.36e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 94.27 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:PRK10522 323 LELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSATLRDnlllAAPQADDAALGAVLARVGLEKLLDDeglnawlgEGGR----QLSGGELRRLGIARALLHNAP 494
Cdd:PRK10522 402 VFTDFHLFDQLLGP----EGKPANPALVEKWLERLKMAHKLEL--------EDGRisnlKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163667 495 MLLLDEPTEGLDAETER----QILALVKEVAvqKTLLMVTHRLQGLTAFDRIIVMDNGQITE-QGSHKELLAQ 562
Cdd:PRK10522 470 ILLLDEWAADQDPHFRRefyqVLLPLLQEMG--KTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
336-563 |
4.10e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.02 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 336 EASLSLRNVSFSYpgQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGyREAALRAT 415
Cdd:PRK13537 5 VAPIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 416 MSVVPQRVHL---FsaTLRDNLLLAAPQAddaALGAVLARVGLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHN 492
Cdd:PRK13537 82 VGVVPQFDNLdpdF--TVRENLLVFGRYF---GLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163667 493 APMLLLDEPTEGLDAETERQILALVKEV-AVQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQQ 563
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
336-570 |
4.56e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 89.70 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 336 EASLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITG---YREAal 412
Cdd:COG1137 1 MMTLEAENLVKSYGKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmHKRA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 413 RATMSVVPQRVHLF-SATLRDNLLlaapqaddaalgAVLARVG---------LEKLLDDEGLNAWLGEGGRQLSGGELRR 482
Cdd:COG1137 77 RLGIGYLPQEASIFrKLTVEDNIL------------AVLELRKlskkereerLEELLEEFGITHLRKSKAYSLSGGERRR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 483 LGIARALLHNAPMLLLDEPTEGLD----AE--------TERQILALVKEVAVQKTLlmvthrlqGLTafDRIIVMDNGQI 550
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDpiavADiqkiirhlKERGIGVLITDHNVRETL--------GIC--DRAYIISEGKV 214
|
250 260
....*....|....*....|....*
gi 495163667 551 TEQGSHKELLAQQG--RYY---QFR 570
Cdd:COG1137 215 LAEGTPEEILNNPLvrKVYlgeDFR 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
353-555 |
1.15e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 93.92 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 353 QPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAaLRATMSVVPQRVHLFS-ATLR 431
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDA-VRQSLGMCPQHNILFHhLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 432 DNLLLAAPQADDAALGAVLArvgLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETER 511
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQLE---MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495163667 512 QILALVKEVAVQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGS 555
Cdd:TIGR01257 1099 SIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
338-561 |
1.28e-19 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 88.10 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITG---YREAalRA 414
Cdd:TIGR04406 1 TLVAENLIKSYKKRK--VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlpmHERA--RL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 415 TMSVVPQRVHLFSA-TLRDNLLLAAPQADDAALGAVLARvgLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNA 493
Cdd:TIGR04406 77 GIGYLPQEASIFRKlTVEENIMAVLEIRKDLDRAEREER--LEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 494 PMLLLDEPTEGLDA------------ETERQILALVKEVAVQKTLLMVthrlqgltafDRIIVMDNGQITEQGSHKELLA 561
Cdd:TIGR04406 155 KFILLDEPFAGVDPiavgdikkiikhLKERGIGVLITDHNVRETLDIC----------DRAYIISDGKVLAEGTPAEIVA 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
339-562 |
1.32e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.41 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSY-PGQP--QPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYRE----AA 411
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 412 LRATMSVVPQ--RVHLFSAT-LRD------NLLLAAPQADDAAlGAVLARVGLEKllddeglnAWLGEGGRQLSGGELRR 482
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETvLKDvafgpqNFGIPKEKAEKIA-AEKLEMVGLAD--------EFWEKSPFELSGGQMRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 483 LGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEV-AVQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELL 560
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADYaDYVYLLEKGHIISCGTPSDVF 232
|
..
gi 495163667 561 AQ 562
Cdd:PRK13643 233 QE 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
355-567 |
1.34e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 91.25 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRAT----MSVVPQRVHLFS-AT 429
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 430 LRDNlllaapQADDAALGAVLARVGLEKLLD---DEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLD 506
Cdd:PRK10070 123 VLDN------TAFGMELAGINAEERREKALDalrQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 507 A--ETERQILALVKEVAVQKTLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKELLAQQGRYY 567
Cdd:PRK10070 197 PliRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
344-551 |
1.39e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.62 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 344 VSFSYPGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAA---LRATMSVVP 420
Cdd:PRK10908 7 VSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 421 QRVHLF-SATLRDN----LLLAAPQADDAA--LGAVLARVGLEklldDEGLNAWLgeggrQLSGGELRRLGIARALLHNA 493
Cdd:PRK10908 86 QDHHLLmDRTVYDNvaipLIIAGASGDDIRrrVSAALDKVGLL----DKAKNFPI-----QLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163667 494 PMLLLDEPTEGLDAETERQILALVKEV-AVQKTLLMVTHRLqGLTAFD--RIIVMDNGQIT 551
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDI-GLISRRsyRMLTLSDGHLH 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
338-573 |
1.66e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.83 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYPGQPQP--------------------ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDV 397
Cdd:COG1134 4 MIEVENVSKSYRLYHEPsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 398 MLDGvsitgyREAALRATMS-VVPQrvhlfsATLRDNLLLAApqaddAALGavLARVGLEKLLDD-----EglnawLGEG 471
Cdd:COG1134 84 EVNG------RVSALLELGAgFHPE------LTGRENIYLNG-----RLLG--LSRKEIDEKFDEivefaE-----LGDF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 472 G----RQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVM 545
Cdd:COG1134 140 IdqpvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRLcDRAIWL 219
|
250 260
....*....|....*....|....*...
gi 495163667 546 DNGQITEQGSHKELLAqqgRYYQFRARS 573
Cdd:COG1134 220 EKGRLVMDGDPEEVIA---AYEALLAGR 244
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
337-553 |
1.78e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 90.29 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 337 ASLSLRNVSFSYPGqPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREA------ 410
Cdd:PRK11650 2 AGLKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAdrdiam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 411 -----ALRATMSVvpqrvhlfsatlRDNLLLA-----APQADDAALGAVLAR-VGLEKLLDDEglnawlgegGRQLSGGE 479
Cdd:PRK11650 81 vfqnyALYPHMSV------------RENMAYGlkirgMPKAEIEERVAEAARiLELEPLLDRK---------PRELSGGQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 480 LRRLGIARALLHNAPMLLLDEPTEGLDAETERQ----ILALVKEVAVqkTLLMVTH-RLQGLTAFDRIIVMDNGQItEQ 553
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQmrleIQRLHRRLKT--TSLYVTHdQVEAMTLADRVVVMNGGVA-EQ 215
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
354-549 |
2.03e-19 |
|
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: 87.49 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 354 PALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDV-------MLDGVSITGYREAALRAT--------MSV 418
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggWVDLAQASPREILALRRRtigyvsqfLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPqRVhlfSAtlRD---NLLLAAPQADDAAL---GAVLARVGLEKLLddeglnaWlgeggrQL-----SGGELRRLGIAR 487
Cdd:COG4778 105 IP-RV---SA--LDvvaEPLLERGVDREEARaraRELLARLNLPERL-------W------DLppatfSGGEQQRVNIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 488 ALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKT-LLMVTHRLQGLTAF-DRIIVMDNGQ 549
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIGIFHDEEVREAVaDRVVDVTPFS 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
337-559 |
2.48e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.09 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 337 ASLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITgYREAALRAtM 416
Cdd:PRK11000 2 ASVTLRNVTKAYGDVV--ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAERG-V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVVPQrvhlfSATLRDNLLLaapqADDAALGAVLARVG----------------LEKLLDdeglnawlgeggRQ---LSG 477
Cdd:PRK11000 78 GMVFQ-----SYALYPHLSV----AENMSFGLKLAGAKkeeinqrvnqvaevlqLAHLLD------------RKpkaLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 478 GELRRLGIARALLHNAPMLLLDEPTEGLDAETERQ----ILALVKEvaVQKTLLMVTH-RLQGLTAFDRIIVMDNGQITE 552
Cdd:PRK11000 137 GQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQmrieISRLHKR--LGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQ 214
|
....*..
gi 495163667 553 QGSHKEL 559
Cdd:PRK11000 215 VGKPLEL 221
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
339-562 |
3.14e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.94 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRV--HLFSATLRDNLLLAAPQA--DDAALG----AVLARVGLEKLLDdeglnawlgEGGRQLSGGELRRLGIARALL 490
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIAFGPINLglDEETVAhrvsSALHMLGLEELRD---------RVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 491 HNAPMLLLDEPTEGLDAETERQILALVKEVAVQ--KTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQ 562
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
339-562 |
3.17e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.04 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLIT--RAWDPTSGDVMLDGVSITGyreaalratM 416
Cdd:COG0396 1 LEIKNLHVSVEGKE--ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILE---------L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVvPQRVH--LFSA----------TLRDNLLLAAPQADDAALGAVLARVGLEKLLDDEGLNA-----WLGEGgrqLSGGE 479
Cdd:COG0396 70 SP-DERARagIFLAfqypveipgvSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEdfldrYVNEG---FSGGE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 480 LRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKT-LLMVTH--RLQGLTAFDRIIVMDNGQITEQGSh 556
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRgILIITHyqRILDYIKPDFVHVLVDGRIVKSGG- 224
|
....*.
gi 495163667 557 KELLAQ 562
Cdd:COG0396 225 KELALE 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
339-559 |
3.81e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.50 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRvhlfsatlRDNLLLAAPQADDAALGAVLARVGLEKL-------LDDEGLNAWLGEGGRQLSGGELRRLGIARALLH 491
Cdd:PRK13648 88 VFQN--------PDNQFVGSIVKYDVAFGLENHAVPYDEMhrrvseaLKQVDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 492 NAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKEL 559
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
332-563 |
4.34e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.73 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 332 DAPREASLS-----LRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITG 406
Cdd:PRK13536 30 KASIPGSMStvaidLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 407 YREAAlRATMSVVPQRVHL-FSATLRDNLLL------AAPQADDAALGAVLARVGLEKLLDDEGlnawlgeggRQLSGGE 479
Cdd:PRK13536 108 RARLA-RARIGVVPQFDNLdLEFTVRENLLVfgryfgMSTREIEAVIPSLLEFARLESKADARV---------SDLSGGM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 480 LRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKE-VAVQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHK 557
Cdd:PRK13536 178 KRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPH 257
|
....*.
gi 495163667 558 ELLAQQ 563
Cdd:PRK13536 258 ALIDEH 263
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
339-560 |
5.82e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 5.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:PRK09536 4 IDVSDLSVEFGDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHL-FSATLRDNL----------LLAAPQADDAALGAVLARVGLEKLLDdeglnawlgEGGRQLSGGELRRLGIAR 487
Cdd:PRK09536 82 VPQDTSLsFEFDVRQVVemgrtphrsrFDTWTETDRAAVERAMERTGVAQFAD---------RPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 488 ALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELL 560
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADVL 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
337-560 |
6.23e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.51 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 337 ASLSLRNVSFSYpGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWD-----PTSGDVMLDGVSITGYREAA 411
Cdd:PRK14247 2 NKIEIRDLKVSF-GQVE-VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 412 LRATMSVVPQrvhlfsatlRDNLLLAAPQADDAALGAVLARV-------------GLEKLLDDEGLNAWLGEGGRQLSGG 478
Cdd:PRK14247 80 LRRRVQMVFQ---------IPNPIPNLSIFENVALGLKLNRLvkskkelqervrwALEKAQLWDEVKDRLDAPAGKLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 479 ELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVTH-RLQGLTAFDRIIVMDNGQITEQGSHK 557
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTR 230
|
...
gi 495163667 558 ELL 560
Cdd:PRK14247 231 EVF 233
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
331-560 |
7.10e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 86.77 E-value: 7.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 331 KDAPREASLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREA 410
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 411 ALRATMSVVPQRVHLFSATLRDNLLLAAPQADDAALG--AVLARVGLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARA 488
Cdd:PRK10575 82 AFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 489 LLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELL 560
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAELM 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
339-551 |
8.70e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.70 E-value: 8.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDG--VSITGYREaALRATM 416
Cdd:COG3845 6 LELRGITKRFGGVV--ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRD-AIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVVPQRVHLFSA-TLRDNLLLAAPQADDAALGAVLARVGLEKLLDDEGLN------AWlgeggrQLSGGELRRLGIARAL 489
Cdd:COG3845 83 GMVHQHFMLVPNlTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDvdpdakVE------DLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 490 LHNAPMLLLDEPTEGL-DAETER--QIL-ALVKEvavQKTLLMVTHRLQGLTAF-DRIIVMDNGQIT 551
Cdd:COG3845 157 YRGARILILDEPTAVLtPQEADElfEILrRLAAE---GKSIIFITHKLREVMAIaDRVTVLRRGKVV 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
339-561 |
1.79e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.91 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQ-PALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMS 417
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQRvhlfsatlRDNLLLAAPQADDAALGAVLARVGLEKLLD--DEGLNA--WLGEGGRQ---LSGGELRRLGIARALL 490
Cdd:PRK13642 85 MVFQN--------PDNQFVGATVEDDVAFGMENQGIPREEMIKrvDEALLAvnMLDFKTREparLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163667 491 HNAPMLLLDEPTEGLDAETERQILALVKEV--AVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLA 561
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIkeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
336-549 |
2.15e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 336 EASLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSIT-GYREAALRA 414
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 415 TMSVVPQRVHLF-SATLRDNLLLAA-PQA----DDAALGAVlARVGLEKLLDDEGLNAWLGEggrqLSGGELRRLGIARA 488
Cdd:PRK11288 80 GVAIIYQELHLVpEMTVAENLYLGQlPHKggivNRRLLNYE-AREQLEHLGVDIDPDTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163667 489 LLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQ 549
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEgRVILYVSHRMEEIFALcDAITVFKDGR 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
339-554 |
2.41e-18 |
|
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: 84.12 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYP--------------------GQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVM 398
Cdd:cd03220 1 IELENVSKSYPtykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 399 LDG-VSitgyreAALRATMSVVPqrvhlfSATLRDNLLLAA------PQADDAALGAVLARVGLEKLLDdeglnawlgEG 471
Cdd:cd03220 81 VRGrVS------SLLGLGGGFNP------ELTGRENIYLNGrllglsRKEIDEKIDEIIEFSELGDFID---------LP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 472 GRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKE-VAVQKTLLMVTHRLQGLTAF-DRIIVMDNGQ 549
Cdd:cd03220 140 VKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRElLKQGKTVILVSHDPSSIKRLcDRALVLEKGK 219
|
....*
gi 495163667 550 ITEQG 554
Cdd:cd03220 220 IRFDG 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
358-562 |
2.95e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 86.31 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 358 DITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITgyREAALRATMSVVPQRVHLFS-ATLRDNL-- 434
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRDICMVFQSYALFPhMSLGENVgy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 435 ---LLAAPQADdaalgaVLARV--GLEkLLDDEGLnawlgeGGR---QLSGGELRRLGIARALLHNAPMLLLDEPTEGLD 506
Cdd:PRK11432 102 glkMLGVPKEE------RKQRVkeALE-LVDLAGF------EDRyvdQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 507 AETERQILALVKEVAVQ--KTLLMVTH-RLQGLTAFDRIIVMDNGQITEQGSHKELLAQ 562
Cdd:PRK11432 169 ANLRRSMREKIRELQQQfnITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
355-555 |
3.52e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.45 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVaPGEHI-AILGRTGCGKSTLLQLITRAWD--PT---SGDVMLDGVSITGYR--EAALRATMSVVPQRVHLF 426
Cdd:PRK14243 25 AVKNVWLDI-PKNQItAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDvdPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 427 SATLRDNLLLAAP----QADdaaLGAVLARVGLEKLLDDEgLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPT 502
Cdd:PRK14243 104 PKSIYDNIAYGARingyKGD---MDELVERSLRQAALWDE-VKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495163667 503 EGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGS 555
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
339-550 |
5.69e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.96 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYRE--------A 410
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREdtrlmfqdA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 411 ALRATMSVVpqrvhlfsatlrDNLLLA-APQADDAALGAvLARVGLEkllddEGLNAWLGeggrQLSGGELRRLGIARAL 489
Cdd:PRK11247 91 RLLPWKKVI------------DNVGLGlKGQWRDAALQA-LAAVGLA-----DRANEWPA----ALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 490 LHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTAF-DRIIVMDNGQI 550
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
351-561 |
6.41e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 87.91 E-value: 6.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 351 QPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMldgvsitgyreaALRaTMSVVPQRVHLFSATL 430
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW------------AER-SIAYVPQQAWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 431 RDNLLLAAPQaDDAALGAVLARVGLEKLLDD--EGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAE 508
Cdd:PTZ00243 738 RGNILFFDEE-DAARLADAVRVSQLEADLAQlgGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495163667 509 T-ERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVMDNGQITEQGSHKELLA 561
Cdd:PTZ00243 817 VgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
339-568 |
6.54e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVS--FSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKS-TLLQLITRAWDP----TSGDVMLDGVSITGYREAA 411
Cdd:PRK15134 6 LAIENLSvaFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 412 LRAT----MSVVPQR-------VHLFSATLRDNLLLAAPQADDAALGAVLA---RVGLEKLLDDeglnawLGEGGRQLSG 477
Cdd:PRK15134 86 LRGVrgnkIAMIFQEpmvslnpLHTLEKQLYEVLSLHRGMRREAARGEILNcldRVGIRQAAKR------LTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 478 GELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEV--AVQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQG 554
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqqELNMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQN 239
|
250
....*....|....*
gi 495163667 555 SHKELLAQ-QGRYYQ 568
Cdd:PRK15134 240 RAATLFSApTHPYTQ 254
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
339-554 |
8.94e-18 |
|
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: 81.93 E-value: 8.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSF--SYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPT---SGDVMLDGVSITGYREAALR 413
Cdd:cd03233 4 LSWRNISFttGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 414 ATMSVVPQRVHLFSATLRDNLllaapqadDAALgavlarvgleKLLDDEGLnawlgeggRQLSGGELRRLGIARALLHNA 493
Cdd:cd03233 84 EIIYVSEEDVHFPTLTVRETL--------DFAL----------RCKGNEFV--------RGISGGERKRVSIAEALVSRA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 494 PMLLLDEPTEGLDAETERQILALVKEVA-VQKTLLMVThRLQ---GLTA-FDRIIVMDNGQITEQG 554
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCIRTMAdVLKTTTFVS-LYQasdEIYDlFDKVLVLYEGRQIYYG 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
337-563 |
1.13e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.62 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 337 ASLSLRNVSFSYpGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAA-LRAT 415
Cdd:PRK11614 4 VMLSFDKVSAHY-GKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 416 MSVVPQRVHLFS-ATLRDNLLLAAPQADDAALGAVLARVglekllddEGLNAWLGEGGRQ----LSGGELRRLGIARALL 490
Cdd:PRK11614 82 VAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV--------YELFPRLHERRIQragtMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 491 HNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKELLAQQ 563
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
339-533 |
2.40e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.08 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYpGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMldgvsitgyREAALRatMSV 418
Cdd:PRK09544 5 VSLENVSVSF-GQRR-VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR--IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLfSATLR---DNLLLAAPQADDAALGAVLARVGLEKLLDdeglnawlgEGGRQLSGGELRRLGIARALLHNAPM 495
Cdd:PRK09544 72 VPQKLYL-DTTLPltvNRFLRLRPGTKKEDILPALKRVQAGHLID---------APMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495163667 496 LLLDEPTEGLDAETERQILALVKEV--AVQKTLLMVTHRL 533
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLrrELDCAVLMVSHDL 181
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
316-547 |
2.85e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.85 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 316 DVIDQPADITFAESGKDAPREASLSLRNVSFSYPGQPQPAL-RDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTS 394
Cdd:PTZ00265 360 EIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 395 GDVML-DGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLA--------------------------------APQA 441
Cdd:PTZ00265 440 GDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrAKCA 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 442 DDAAL--------GAVLARVGLEKLLDDEGLN-------------------AWLGEGGRQLSGGELRRLGIARALLHNAP 494
Cdd:PTZ00265 520 GDLNDmsnttdsnELIEMRKNYQTIKDSEVVDvskkvlihdfvsalpdkyeTLVGSNASKLSGGQKQRISIARAIIRNPK 599
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 495 MLLLDEPTEGLDAETerqilalvkEVAVQKTL-----------LMVTHRLQGLTAFDRIIVMDN 547
Cdd:PTZ00265 600 ILILDEATSSLDNKS---------EYLVQKTInnlkgnenritIIIAHRLSTIRYANTIFVLSN 654
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
355-563 |
3.95e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 82.59 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAA----------------LRATMSV 418
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHelitnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQ--RVHLFSATLRDNLLLAApqaddAALG------AVLARVGLEKL-LDDeglnAWLGEGGRQLSGGELRRLGIARAL 489
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMFGP-----VALGvkkseaKKLAKFYLNKMgLDD----SYLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 490 LHNAPMLLLDEPTEGLDAETERQILALVKEV-AVQKTLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKELLAQQ 563
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-560 |
5.03e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.24 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYpgQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTS-----GDVMLDGVSITGYREAA- 411
Cdd:PRK14258 7 AIKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 412 -LRATMSVVPQRVHLFSATLRDNLLLAAP--------QADDAALGAVLArvglEKLLDDegLNAWLGEGGRQLSGGELRR 482
Cdd:PRK14258 85 rLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpklEIDDIVESALKD----ADLWDE--IKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 483 LGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTH------RLQGLTAF-----DRIivmdnGQ 549
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSelTMVIVSHnlhqvsRLSDFTAFfkgneNRI-----GQ 233
|
250
....*....|.
gi 495163667 550 ITEQGSHKELL 560
Cdd:PRK14258 234 LVEFGLTKKIF 244
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
338-559 |
5.11e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.82 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSYpGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITgyREAALRATMS 417
Cdd:PRK10851 2 SIEIANIKKSF-GRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQRVHLFS-ATLRDNL---LLAAPQADDAALGAVLARVglEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNA 493
Cdd:PRK10851 78 FVFQHYALFRhMTVFDNIafgLTVLPRRERPNAAAIKAKV--TQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163667 494 PMLLLDEPTEGLDA----ETERQILALVKEVAVqkTLLMVTH-RLQGLTAFDRIIVMDNGQITEQGSHKEL 559
Cdd:PRK10851 156 QILLLDEPFGALDAqvrkELRRWLRQLHEELKF--TSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
357-560 |
5.41e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.19 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 357 RDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGY------REAALRATMSVVPQRVHLFSATL 430
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYaskevaRRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 431 RDN-----LLLAAPQADDAALGAVLARVGLEKLLDdeglnawlgEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGL 505
Cdd:PRK10253 104 RGRyphqpLFTRWRKEDEEAVTKAMQATGITHLAD---------QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 506 DAETERQILALVKEVAVQK--TLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKELL 560
Cdd:PRK10253 175 DISHQIDLLELLSELNREKgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
356-574 |
5.55e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 81.41 E-value: 5.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQliTRAWDPT----------SGDVMLDG---VSITGYREAALRATMSVVPQR 422
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLK--ALAGDLTgggaprgarvTGDVTLNGeplAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 423 VHLFSAtlRDNLLLAA-PQADDAALGAVLARVGLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARAL--LHNAP----- 494
Cdd:PRK13547 95 AFAFSA--REIVLLGRyPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqLWPPHdaaqp 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 495 --MLLLDEPTEGLDAETERQILALVKEVAVQKTL--LMVTH--RLQGLTAfDRIIVMDNGQITEQGSHKELL--AQQGRY 566
Cdd:PRK13547 173 prYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgvLAIVHdpNLAARHA-DRIAMLADGAIVAHGAPADVLtpAHIARC 251
|
....*...
gi 495163667 567 YQFRARSV 574
Cdd:PRK13547 252 YGFAVRLV 259
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
356-560 |
5.58e-17 |
|
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: 79.49 E-value: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLIT--RAWDPTSGDVMLDGVSITgyreaalratmsvvpqrvhlfsatlrdn 433
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDIT---------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 434 lllAAPQADDAALGAVLA--------RVGLEKLLDDeglnawLGEGgrqLSGGELRRLGIARALLHNAPMLLLDEPTEGL 505
Cdd:cd03217 68 ---DLPPEERARLGIFLAfqyppeipGVKNADFLRY------VNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 506 DAETERQILALVKEVAVQKT-LLMVTH--RLQGLTAFDRIIVMDNGQITEQGShKELL 560
Cdd:cd03217 136 DIDALRLVAEVINKLREEGKsVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELA 192
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-560 |
9.29e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.48 E-value: 9.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWD------PTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFS-A 428
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPhL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 429 TLRDNLL-------LAAPQADDAALGAVLARVGLEKLLDDEglnawLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEP 501
Cdd:PRK14246 106 SIYDNIAyplkshgIKEKREIKKIVEECLRKVGLWKEVYDR-----LNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 502 TEGLDAETERQILALVKEVAVQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELL 560
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIF 240
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
340-509 |
9.61e-17 |
|
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: 83.45 E-value: 9.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 340 SLRNVSFSYPGQpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVML-DGVSItGY--REAALRATM 416
Cdd:TIGR03719 6 TMNRVSKVVPPK-KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKV-GYlpQEPQLDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SV-------VPQRVHLFSATLRDNLLLAAPQADDAALGAVLARvgLEKLLDdeGLNAWlgEGGRQ--------------- 474
Cdd:TIGR03719 84 TVrenveegVAEIKDALDRFNEISAKYAEPDADFDKLAAEQAE--LQEIID--AADAW--DLDSQleiamdalrcppwda 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 495163667 475 ----LSGGELRRLGIARALLHNAPMLLLDEPTEGLDAET 509
Cdd:TIGR03719 158 dvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
355-559 |
1.21e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.03 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALrATMSVVP--QRVHLF-SATLR 431
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 432 DNLLLAAPQ------------------ADDAALGAV---LARVGLEKLLDDEGLNawlgeggrqLSGGELRRLGIARALL 490
Cdd:PRK11300 99 ENLLVAQHQqlktglfsgllktpafrrAESEALDRAatwLERVGLLEHANRQAGN---------LAYGQQRRLEIARCMV 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 491 HNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQ---GLTafDRIIVMDNGQITEQGSHKEL 559
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKlvmGIS--DRIYVVNQGTPLANGTPEEI 241
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
355-554 |
2.24e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.54 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSItgyREAALRATMSVVPQRVHL---FSATLR 431
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNLVAYVPQSEEVdwsFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 432 DNLLLA----------APQADDAALGAVLARVGLEKLLDDEglnawLGEggrqLSGGELRRLGIARALLHNAPMLLLDEP 501
Cdd:PRK15056 99 DVVMMGryghmgwlrrAKKRDRQIVTAALARVDMVEFRHRQ-----IGE----LSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495163667 502 TEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAFDRIIVMDNGQITEQG 554
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
356-553 |
3.51e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.90 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYRE---AALRA-TMSVVPQRVHLF-SATL 430
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAkHVGFVFQSFMLIpTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 431 RDNLLLAA-------PQADDAALgAVLARVGLEKLLDDegLNAwlgeggrQLSGGELRRLGIARALLHNAPMLLLDEPTE 503
Cdd:PRK10584 106 LENVELPAllrgessRQSRNGAK-ALLEQLGLGKRLDH--LPA-------QLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495163667 504 GLDAETERQI----LALVKEVAVqkTLLMVTHRLQGLTAFDRIIVMDNGQITEQ 553
Cdd:PRK10584 176 NLDRQTGDKIadllFSLNREHGT--TLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
339-561 |
4.09e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.90 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYpgQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREA--ALRATM 416
Cdd:PRK13638 2 LATSDLWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SVVPQ--RVHLFSATLRDNLL-----LAAPQADdaalgaVLARVgleklldDEGLNAWLGEGGRQ-----LSGGELRRLG 484
Cdd:PRK13638 80 ATVFQdpEQQIFYTDIDSDIAfslrnLGVPEAE------ITRRV-------DEALTLVDAQHFRHqpiqcLSHGQKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 485 IARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLA 561
Cdd:PRK13638 147 IAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgNHVIISSHDIDLIYEIsDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
339-548 |
5.08e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPgqPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLD---------------GVS 403
Cdd:PRK09700 6 ISMAGIGKSFG--PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINninynkldhklaaqlGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 404 ITgYREAALRATMSVVPqrvHLFSATLRDNLLLAAPQADDAALgavlaRVGLEKLLDDEGLNAWLGEGGRQLSGGELRRL 483
Cdd:PRK09700 84 II-YQELSVIDELTVLE---NLYIGRHLTKKVCGVNIIDWREM-----RVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 484 GIARALLHNAPMLLLDEPTEGL-DAETErQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNG 548
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLtNKEVD-YLFLIMNQLRKEgTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
339-561 |
5.19e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREA-ALRATMS 417
Cdd:PRK15439 12 LCARSISKQYSGVE--VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQRVHLF-SATLRDNLL--LAAPQADDAALGAVLARVGLEklLDDEGLNAWLGEGGRQLsggelrrLGIARALLHNAP 494
Cdd:PRK15439 90 LVPQEPLLFpNLSVKENILfgLPKRQASMQKMKQLLAALGCQ--LDLDSSAGSLEVADRQI-------VEILRGLMRDSR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 495 MLLLDEPTEGLD-AETER---QILALVKE-VAVqktlLMVTHRLQGLTAF-DRIIVMDNGQI-----TEQGSHKELLA 561
Cdd:PRK15439 161 ILILDEPTASLTpAETERlfsRIRELLAQgVGI----VFISHKLPEIRQLaDRISVMRDGTIalsgkTADLSTDDIIQ 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
347-559 |
5.43e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 79.37 E-value: 5.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 347 SYPGQPQPALR---DITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVpQRV 423
Cdd:PRK15079 25 QWFWQPPKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDI-QMI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 424 H---LFSATLRDNL--LLAAP----------QADDAALGAVLARVGLEKLLddegLNAWLGEggrqLSGGELRRLGIARA 488
Cdd:PRK15079 104 FqdpLASLNPRMTIgeIIAEPlrtyhpklsrQEVKDRVKAMMLKVGLLPNL----INRYPHE----FSGGQCQRIGIARA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 489 LLHNAPMLLLDEPTEGLDAETERQILALVKEvaVQK----TLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKEL 559
Cdd:PRK15079 176 LILEPKLIICDEPVSALDVSIQAQVVNLLQQ--LQRemglSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
341-561 |
8.18e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.59 E-value: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 341 LRNVSFSY-PGQPQ--PALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDV------------------ML 399
Cdd:PRK13651 5 VKNIVKIFnKKLPTelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 400 DGVSI--TGYRE----AALRATMSVVPQ--RVHLFSATLRDNLLLAA-----PQADDAALGA-VLARVGL-EKLLDDEGL 464
Cdd:PRK13651 85 EKLVIqkTRFKKikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPvsmgvSKEEAKKRAAkYIELVGLdESYLQRSPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 465 NawlgeggrqLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRI 542
Cdd:PRK13651 165 E---------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWtKRT 235
|
250
....*....|....*....
gi 495163667 543 IVMDNGQITEQGSHKELLA 561
Cdd:PRK13651 236 IFFKDGKIIKDGDTYDILS 254
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
339-554 |
1.25e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.89 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYpgQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGvsitgyREAALR--ATM 416
Cdd:PRK11701 7 LSVRGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM------RDGQLRdlYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SvVPQRVHLfsatLRDNLLLAAPQADDAALGAVLA--RVGlEKLLD----------DEGLNaWLGE----------GGRQ 474
Cdd:PRK11701 79 S-EAERRRL----LRTEWGFVHQHPRDGLRMQVSAggNIG-ERLMAvgarhygdirATAGD-WLERveidaariddLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 475 LSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTL--LMVTHRL--QGLTAfDRIIVMDNGQI 550
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLavVIVTHDLavARLLA-HRLLVMKQGRV 230
|
....
gi 495163667 551 TEQG 554
Cdd:PRK11701 231 VESG 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
341-569 |
1.35e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.11 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 341 LRNVSFSYpGQpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAAL---RATMS 417
Cdd:PRK11831 10 MRGVSFTR-GN-RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQRVHLFS-ATLRDNllLAAPQADDAALGAVLARVGLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPML 496
Cdd:PRK11831 88 MLFQSGALFTdMNVFDN--VAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 497 LLDEPTEGLDAETERQILALVKEV--AVQKTLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKELLAQQG-RYYQF 569
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQALQANPDpRVRQF 242
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
339-560 |
1.47e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.42 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSypgqpqPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWdPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:COG4138 1 LQLNDVAVA------GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQR-VHLFSATLRDNLLLAAP-----QADDAALGAVLARVGLEKLLddeglnawlgegGR---QLSGGELRRLGIARAL 489
Cdd:COG4138 74 LSQQqSPPFAMPVFQYLALHQPagassEAVEQLLAQLAEALGLEDKL------------SRpltQLSGGEWQRVRLAAVL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 490 LH-------NAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQgLTAF--DRIIVMDNGQITEQGSHKEL 559
Cdd:COG4138 142 LQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQgITVVMSSHDLN-HTLRhaDRVWLLKQGKLVASGETAEV 220
|
.
gi 495163667 560 L 560
Cdd:COG4138 221 M 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
341-563 |
1.67e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.36 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 341 LRNVSFSYpGQPQP----ALRDITLDVAPGEHIAILGRTGCGKSTLLQL-----ITRAWDPTSGDVMLDGvSITGYREAA 411
Cdd:PRK13645 9 LDNVSYTY-AKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliISETGQTIVGDYAIPA-NLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 412 -LRATMSVVPQ--RVHLFSATLRDNLLLAApqaddAALGAVLARV--GLEKLLDDEGL-NAWLGEGGRQLSGGELRRLGI 485
Cdd:PRK13645 87 rLRKEIGLVFQfpEYQLFQETIEKDIAFGP-----VNLGENKQEAykKVPELLKLVQLpEDYVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 486 ARALLHNAPMLLLDEPTEGLDAETERQILALVKEV--AVQKTLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKELLAQ 562
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
.
gi 495163667 563 Q 563
Cdd:PRK13645 242 Q 242
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
336-561 |
1.78e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.75 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 336 EASLSLRNVS--FSYPG-----QPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSIT--- 405
Cdd:PRK15112 2 ETLLEVRNLSktFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 406 -GYREAALR-----ATMSVVP-QRV-HLFSATLRDNLLLaAPQADDAALGAVLARVGLekllddegLNAWLGEGGRQLSG 477
Cdd:PRK15112 82 ySYRSQRIRmifqdPSTSLNPrQRIsQILDFPLRLNTDL-EPEQREKQIIETLRQVGL--------LPDHASYYPHMLAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 478 GELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTL--LMVTHRLqGLTAF--DRIIVMDNGQITEQ 553
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHL-GMMKHisDQVLVMHQGEVVER 231
|
....*...
gi 495163667 554 GSHKELLA 561
Cdd:PRK15112 232 GSTADVLA 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
339-567 |
1.95e-15 |
|
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: 80.06 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSI-TGYREaaLRATMS 417
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISD--VHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 418 VVPQrvhlFSA-----TLRDNLLLAapqaddAALGAVLARvGLEKL----LDDEGLNAWLGEGGRQLSGGELRRLGIARA 488
Cdd:TIGR01257 2016 YCPQ----FDAiddllTGREHLYLY------ARLRGVPAE-EIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 489 LLHNAPMLLLDEPTEGLDAETERQ----ILALVKEvavQKTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQQ 563
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMlwntIVSIIRE---GRAVVLTSHSMEECEALcTRLAIMVKGAFQCLGTIQHLKSKF 2161
|
....
gi 495163667 564 GRYY 567
Cdd:TIGR01257 2162 GDGY 2165
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
333-551 |
2.73e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 333 APREASLSLRNVSFSyPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAAL 412
Cdd:COG3845 252 EPGEVVLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 413 RAT-MSVVP---QRVHLF-SATLRDNLLLAAPQADDAALGAVLARVGL----EKLLD-------DEGLNAwlgeggRQLS 476
Cdd:COG3845 331 RRLgVAYIPedrLGRGLVpDMSVAENLILGRYRRPPFSRGGFLDRKAIrafaEELIEefdvrtpGPDTPA------RSLS 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 477 GGELRRLGIARALLHNAPMLLLDEPTEGLD----AETERQILALVKE-VAVqktlLMVTHRLQGLTAF-DRIIVMDNGQI 550
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLELRDAgAAV----LLISEDLDEILALsDRIAVMYEGRI 480
|
.
gi 495163667 551 T 551
Cdd:COG3845 481 V 481
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
346-562 |
3.06e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.93 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 346 FSYPGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAA---LRATMSVVPQ- 421
Cdd:PRK11308 22 FKPERLVK-ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 422 -------RvHLFSATLRDNLL----LAAPQADDAALgAVLARVGLEKllddeglnawlGEGGR---QLSGGELRRLGIAR 487
Cdd:PRK11308 101 pygslnpR-KKVGQILEEPLLintsLSAAERREKAL-AMMAKVGLRP-----------EHYDRyphMFSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 488 ALLHNAPMLLLDEPTEGLDAETERQILALVKEvaVQKTL----LMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQ 562
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMD--LQQELglsyVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
356-519 |
7.93e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.37 E-value: 7.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSIT--GYREA--------ALRATMSVvpqrvhl 425
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdpDVAEAchylghrnAMKPALTV------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 426 fsatlRDNLLLAAP--QADDAALGAVLARVGLEKLLDDEGlnawlgeggRQLSGGELRRLGIARALLHNAPMLLLDEPTE 503
Cdd:PRK13539 91 -----AENLEFWAAflGGEELDIAAALEAVGLAPLAHLPF---------GYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170
....*....|....*.
gi 495163667 504 GLDAETERQILALVKE 519
Cdd:PRK13539 157 ALDAAAVALFAELIRA 172
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
333-551 |
9.25e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.98 E-value: 9.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 333 APREASLSLRNVSFsypgqpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDG--VSITGYREA 410
Cdd:COG1129 251 APGEVVLEVEGLSV------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 411 aLRATMSVVP---QRVHLF-SATLRDNLLLAapqaddaalgaVLARVGLEKLLDDEGLNAWLGEGGRQ------------ 474
Cdd:COG1129 325 -IRAGIAYVPedrKGEGLVlDLSIRENITLA-----------SLDRLSRGGLLDRRRERALAEEYIKRlriktpspeqpv 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 475 --LSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQ---GLTafDRIIVMDNG 548
Cdd:COG1129 393 gnLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVISSELPellGLS--DRILVMREG 470
|
...
gi 495163667 549 QIT 551
Cdd:COG1129 471 RIV 473
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
341-561 |
9.47e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.77 E-value: 9.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 341 LRNVSFSYPGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVP 420
Cdd:PRK13647 7 VEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 421 QRV--HLFSATLRD-------NLLLAAPQADDAAlGAVLARVGLEKLLDdeglnawlgEGGRQLSGGELRRLGIARALLH 491
Cdd:PRK13647 86 QDPddQVFSSTVWDdvafgpvNMGLDKDEVERRV-EEALKAVRMWDFRD---------KPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163667 492 NAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQ-GLTAFDRIIVMDNGQITEQGShKELLA 561
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLT 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
332-567 |
1.07e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.05 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 332 DAPREASLSLRNVSFSYPGQ---------PQPALRDITLDVAPGEHIAILGRTGCGKST----LLQLItrawdPTSGDVM 398
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFPIRkgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 399 LDGVSITGYREAAL---RATMSVVPQ--------------------RVHlfsatlrdNLLLAAPQADDAALgAVLARVGL 455
Cdd:PRK15134 344 FDGQPLHNLNRRQLlpvRHRIQVVFQdpnsslnprlnvlqiieeglRVH--------QPTLSAAQREQQVI-AVMEEVGL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 456 ekllDDEGLNAWLGEggrqLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTL--LMVTHRL 533
Cdd:PRK15134 415 ----DPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDL 486
|
250 260 270
....*....|....*....|....*....|....*
gi 495163667 534 QGLTAF-DRIIVMDNGQITEQGSHKELLAQQGRYY 567
Cdd:PRK15134 487 HVVRALcHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
339-561 |
1.29e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 76.76 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLI--TRAWDPTSGDVMLDgVSIT---GYRE---- 409
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYH-VALCekcGYVErpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 410 ---------------------------AALRATMSVVPQRVHLF--SATLRDNLLLAAPQADDAALGAVLARVgleKLLD 460
Cdd:TIGR03269 78 vgepcpvcggtlepeevdfwnlsdklrRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAV---DLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 461 DEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMV--THRLQGLTA 538
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVltSHWPEVIED 234
|
250 260
....*....|....*....|....
gi 495163667 539 F-DRIIVMDNGQITEQGSHKELLA 561
Cdd:TIGR03269 235 LsDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
358-554 |
1.32e-14 |
|
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: 73.60 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 358 DITLDVAPG-----EHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSItgyreaalratmSVVPQRVHL-FSATLR 431
Cdd:cd03237 12 EFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKAdYEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 432 DnllLAAPQADDAALGA-----VLARVGLEKLLDDEGLNawlgeggrqLSGGELRRLGIARALLHNAPMLLLDEPTEGLD 506
Cdd:cd03237 80 D---LLSSITKDFYTHPyfkteIAKPLQIEQILDREVPE---------LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495163667 507 AETERQILALVKEVAV--QKTLLMVTHRLQGLTAF-DRIIVMDnGQITEQG 554
Cdd:cd03237 148 VEQRLMASKVIRRFAEnnEKTAFVVEHDIIMIDYLaDRLIVFE-GEPSVNG 197
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
353-554 |
2.03e-14 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 73.06 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 353 QPALRDITLDVAPGEHIAILGRTGCGKSTLLQLItrAWDP----TSGDVMLDGVSITGYR--EAAlRATMSVVPQRVHLF 426
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTI--AGHPsyevTSGTILFKGQDLLELEpdERA-RAGLFLAFQYPEEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 427 SATLRDNLLLAAPQADDAALG-AVLARVGLEKLLDD---------EGLNAWLGEGgrqLSGGELRRLGIARALLHNAPML 496
Cdd:TIGR01978 90 PGVSNLEFLRSALNARRSARGeEPLDLLDFEKLLKEklalldmdeEFLNRSVNEG---FSGGEKKRNEILQMALLEPKLA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163667 497 LLDEPTEGLDAETERQILALVKEVAVQKT-LLMVTH--RLQGLTAFDRIIVMDNGQITEQG 554
Cdd:TIGR01978 167 ILDEIDSGLDIDALKIVAEGINRLREPDRsFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
340-509 |
2.07e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.93 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 340 SLRNVSFSYPGQpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVML-DGVSItGY--REAALRATM 416
Cdd:PRK11819 8 TMNRVSKVVPPK-KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKV-GYlpQEPQLDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 SV---VPQRVHLFSATLRD----NLLLAAPQADDAALGAVLARvgLEKLLDdeGLNAWlgEGGRQ--------------- 474
Cdd:PRK11819 86 TVrenVEEGVAEVKAALDRfneiYAAYAEPDADFDALAAEQGE--LQEIID--AADAW--DLDSQleiamdalrcppwda 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 495163667 475 ----LSGGELRRLGIARALLHNAPMLLLDEPTEGLDAET 509
Cdd:PRK11819 160 kvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
358-532 |
2.41e-14 |
|
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: 75.94 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 358 DITLDVAPGEHIAILGRTGCGKSTLLQLITRAWdPTSGdvmldgvsitGYREAALRATMSVVPQRVHLFSATLRDNLLLA 437
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYG----------GRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 438 APQAD-------DAALGAVLARVGLEKLLDDEG----LNAWLGEggrqLSGGELRRLGIARALLHNAPMLLLDEPTEGLD 506
Cdd:TIGR00954 539 DSSEDmkrrglsDKDLEQILDNVQLTHILEREGgwsaVQDWMDV----LSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180
....*....|....*....|....*.
gi 495163667 507 AETERQILALVKEVAVqkTLLMVTHR 532
Cdd:TIGR00954 615 VDVEGYMYRLCREFGI--TLFSVSHR 638
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
339-531 |
3.30e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 71.62 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREaalratmsv 418
Cdd:TIGR01189 1 LAARNLACSRGERM--LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLFSA---------TLRDNLLLAAP--QADDAALGAVLARVGLeklLDDEGLNAwlgeggRQLSGGELRRLGIAR 487
Cdd:TIGR01189 70 EPHENILYLGhlpglkpelSALENLHFWAAihGGAQRTIEDALAAVGL---TGFEDLPA------AQLSAGQQRRLALAR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495163667 488 ALLHNAPMLLLDEPTEGLDAETERQILALVKE-VAVQKTLLMVTH 531
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
357-508 |
4.00e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.37 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 357 RDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVvpqrVHL------FSATl 430
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYL----GHQpgikteLTAL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 431 rDNLLLAAP---QADDAALGAVLARVGLEKLLDdegLNAwlgeggRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDA 507
Cdd:PRK13538 93 -ENLRFYQRlhgPGDDEALWEALAQVGLAGFED---VPV------RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
.
gi 495163667 508 E 508
Cdd:PRK13538 163 Q 163
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
337-563 |
4.06e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.23 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 337 ASLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLD--GVSITGYREAALRA 414
Cdd:PRK10895 2 ATLTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdeDISLLPLHARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 415 tMSVVPQRVHLFSA-TLRDNLLLAAPQADDaaLGAVLARVGLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNA 493
Cdd:PRK10895 80 -IGYLPQEASIFRRlSVYDNLMAVLQIRDD--LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163667 494 PMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMVT-HRL-QGLTAFDRIIVMDNGQITEQGSHKELLAQQ 563
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
356-555 |
4.13e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.76 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVA---PGEHI-AILGRTGCGKSTLLQLITRAWDPTSGDVMLD---------GVSIT------GYreaalratm 416
Cdd:PRK11144 10 LGDLCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNgrvlfdaekGICLPpekrriGY--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 svVPQRVHLFSA-TLRDNLLLAAPQADDAALGAVLARVGLEKLLDdeglnawlgeggR---QLSGGELRRLGIARALLHN 492
Cdd:PRK11144 81 --VFQDARLFPHyKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLD------------RypgSLSGGEKQRVAIGRALLTA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495163667 493 APMLLLDEPTEGLDAETERQILALVKEVA--VQKTLLMVTHRLQG-LTAFDRIIVMDNGQITEQGS 555
Cdd:PRK11144 147 PELLLMDEPLASLDLPRKRELLPYLERLAreINIPILYVSHSLDEiLRLADRVVVLEQGKVKAFGP 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
358-546 |
4.94e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.84 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 358 DITLDVAPG-----EHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDgVSItgyreaalratmSVVPQRV-HLFSATLR 431
Cdd:PRK13409 352 DFSLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKI------------SYKPQYIkPDYDGTVE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 432 DNLLLAAPQADDAALGA-VLARVGLEKLLDDEglnawLGEggrqLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAEtE 510
Cdd:PRK13409 419 DLLRSITDDLGSSYYKSeIIKPLQLERLLDKN-----VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE-Q 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495163667 511 RQILALV-KEVA--VQKTLLMVTHR--LQGLTAfDRIIVMD 546
Cdd:PRK13409 489 RLAVAKAiRRIAeeREATALVVDHDiyMIDYIS-DRLMVFE 528
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
341-571 |
2.56e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.68 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 341 LRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDV----MLDGVSITGYREAalratm 416
Cdd:PRK11147 322 MENVNYQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtKLEVAYFDQHRAE------ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 417 sVVPQRvhlfsaTLRDNLllaAPQADDAALGAVLARVgLEKLLDdeglnaWLGEGGRQ------LSGGELRRLGIARALL 490
Cdd:PRK11147 394 -LDPEK------TVMDNL---AEGKQEVMVNGRPRHV-LGYLQD------FLFHPKRAmtpvkaLSGGERNRLLLARLFL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 491 HNAPMLLLDEPTEGLDAETerqiLALVKEV--AVQKTLLMVTHRLQGL--TAFDRIIVMDNGQITEQ-GSHKELLAQQGR 565
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVET----LELLEELldSYQGTVLLVSHDRQFVdnTVTECWIFEGNGKIGRYvGGYHDARQQQAQ 532
|
....*.
gi 495163667 566 YYQFRA 571
Cdd:PRK11147 533 YLALKQ 538
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
22-314 |
2.64e-13 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 70.66 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 22 VVLAIVTLLASIGLLTLSGWFLS-ASAVVGMAGLYSFNYMLPAAGVrGAAIIRTAGRYFERLVSHEGTFRVLEHLRVYTF 100
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKlLIDDVIPAGDLSLLLWIALLLL-LLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 101 SRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLDVTLALtlggIMLATLLLLPPL 180
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTL----VALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 181 FYRAGRpvgealtMLRASYR--QQLTGWLQGQAELSI--------FGAAGRYREQLDTTEQVWHEAQRRQAGLTALSQAM 250
Cdd:cd07346 156 LRYFRR-------RIRKASRevRESLAELSAFLQESLsgirvvkaFAAEEREIERFREANRDLRDANLRAARLSALFSPL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 251 MTLISGMTVVLILWMAAGGV-GGNSTPGSLIALFVFCALAAF--EALAPVGGAFQhlgQVIASARRV 314
Cdd:cd07346 229 IGLLTALGTALVLLYGGYLVlQGSLTIGELVAFLAYLGMLFGpiQRLANLYNQLQ---QALASLERI 292
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
359-531 |
3.45e-13 |
|
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: 68.67 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 359 ITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLFSATLRDNLLLAA 438
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 439 PQADDAALGAVLARVGLEKLLDdeglnawlgEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVK 518
Cdd:cd03231 99 ADHSDEQVEEALARVGLNGFED---------RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....
gi 495163667 519 EVAVQ-KTLLMVTH 531
Cdd:cd03231 170 GHCARgGMVVLTTH 183
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
358-546 |
4.97e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 71.74 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 358 DITLDVAPG-----EHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDgvsitgyreaalrATMSVVPQRV-HLFSATLR 431
Cdd:COG1245 353 GFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-------------LKISYKPQYIsPDYDGTVE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 432 DNLLLAAPQADDAAL--GAVLARVGLEKLLDDEglnawLGEggrqLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAEt 509
Cdd:COG1245 420 EFLRSANTDDFGSSYykTEIIKPLGLEKLLDKN-----VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE- 489
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495163667 510 ERQILA-LVKEVAVQ--KTLLMVTHRLQGL-TAFDRIIVMD 546
Cdd:COG1245 490 QRLAVAkAIRRFAENrgKTAMVVDHDIYLIdYISDRLMVFE 530
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
338-548 |
7.04e-13 |
|
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: 67.27 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 338 SLSLRNVSFSY--PGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLIT-RAWDPT-SGDVMLDGVSITgyrEAALR 413
Cdd:cd03232 3 VLTWKNLNYTVpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgRKTAGViTGEILINGRPLD---KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 414 ATMSVVPQRVHLFSATLRDNLLLAApqaddaalgavlarvglekllddeglnaWLgeggRQLSGGELRRLGIARALLHNA 493
Cdd:cd03232 80 STGYVEQQDVHSPNLTVREALRFSA----------------------------LL----RGLSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 494 PMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLT--AFDRIIVMDNG 548
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLADSgQAILCTIHQPSASIfeKFDRLLLLKRG 185
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
324-564 |
1.57e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.92 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 324 ITFaESGKDAPREAsLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVS 403
Cdd:PRK15064 307 IRF-EQDKKLHRNA-LEVENLTKGFDNGP--LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 404 ITGYreaalratmsvVPQ-RVHLFSATLrdNLL-----LAAPQADDAALGAVLARvglekLL---DDEGLNAwlgeggRQ 474
Cdd:PRK15064 383 NIGY-----------YAQdHAYDFENDL--TLFdwmsqWRQEGDDEQAVRGTLGR-----LLfsqDDIKKSV------KV 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 475 LSGGELRRLGIARALLHNAPMLLLDEPTEGLDAET-ERQILALVKevaVQKTLLMVTHRLQGLTAF-DRII-VMDNGQIT 551
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESiESLNMALEK---YEGTLIFVSHDREFVSSLaTRIIeITPDGVVD 515
|
250
....*....|...
gi 495163667 552 EQGSHKELLAQQG 564
Cdd:PRK15064 516 FSGTYEEYLRSQG 528
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
314-551 |
1.64e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 70.27 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 314 VSDVIDQPaDITFA-ESGKDAPREASLSLRNVSFSYPGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDP 392
Cdd:PLN03073 484 VDAVVNDP-DYKFEfPTPDDRPGPPIISFSDASFGYPGGPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQP 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 393 TSGDVmldgvsitgYREAALRatMSVVPQRvHLFSATLRDNLLL----AAPQADDAALGAVLARVGLEKLLDDEGLNAwl 468
Cdd:PLN03073 562 SSGTV---------FRSAKVR--MAVFSQH-HVDGLDLSSNPLLymmrCFPGVPEQKLRAHLGSFGVTGNLALQPMYT-- 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 469 geggrqLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETerqILALVKEVAV-QKTLLMVTHRLQGLT-AFDRIIVMD 546
Cdd:PLN03073 628 ------LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLfQGGVLMVSHDEHLISgSVDELWVVS 698
|
....*
gi 495163667 547 NGQIT 551
Cdd:PLN03073 699 EGKVT 703
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
355-559 |
1.73e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.73 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVAPGEHIAILGRTGCGKSTLLQ----LITRAWDPTSgDVMLDGVSITgyREAAL-------RATMSVVPQRV 423
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGS-HIELLGRTVQ--REGRLardirksRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 424 HLFSA-TLRDNLLLAA---------------PQADDAALGAvLARVGLEKLLDDEGlnawlgeggRQLSGGELRRLGIAR 487
Cdd:PRK09984 96 NLVNRlSVLENVLIGAlgstpfwrtcfswftREQKQRALQA-LTRVGMVHFAHQRV---------STLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 488 ALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQ-GLTAFDRIIVMDNGQITEQGSHKEL 559
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
332-531 |
2.15e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 69.27 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 332 DAPReasLSLRNVSFSYpgQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLIT------RAWDPT-------SGDVM 398
Cdd:PRK10938 257 NEPR---IVLNNGVVSY--NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgYSNDLTlfgrrrgSGETI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 399 LDGVSITGYreaalratmsvVPQRVHL---FSATLRDNLL----------LAAPQADDAALGAVLARVGLEKLLDDEGLn 465
Cdd:PRK10938 332 WDIKKHIGY-----------VSSSLHLdyrVSTSVRNVILsgffdsigiyQAVSDRQQKLAQQWLDILGIDKRTADAPF- 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163667 466 awlgeggRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAeTERQ-----ILALVKEVAVQktLLMVTH 531
Cdd:PRK10938 400 -------HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP-LNRQlvrrfVDVLISEGETQ--LLFVSH 460
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
340-564 |
2.27e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.15 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 340 SLRNVSFSYpGQPQpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVM-LDG-VSITGYREAA------ 411
Cdd:NF033858 3 RLEGVSHRY-GKTV-ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGdMADARHRRAVcpriay 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 412 --------LRATMSVvpqrvhlfsatlRDNL-----LLAAPQADDAAlgavlaRVglEKLLDDEGLNAWLGEGGRQLSGG 478
Cdd:NF033858 81 mpqglgknLYPTLSV------------FENLdffgrLFGQDAAERRR------RI--DELLRATGLAPFADRPAGKLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 479 ELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK---TLLMVTHRLQGLTAFDRIIVMDNGQITEQGS 555
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAERFDWLVAMDAGRVLATGT 220
|
....*....
gi 495163667 556 HKELLAQQG 564
Cdd:NF033858 221 PAELLARTG 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
365-533 |
2.67e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 365 PGEHIAILGRTGCGKSTLLQLIT--------RAWDPTSGDVMLD---GVSITGY----REAALRAtmSVVPQRVHL---- 425
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSgelipnlgDYEEEPSWDEVLKrfrGTELQNYfkklYNGEIKV--VHKPQYVDLipkv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 426 FSATLRDnlLLAapQADDA-ALGAVLARVGLEKLLDDEGlnawlgeggRQLSGGELRRLGIARALLHNAPMLLLDEPTEG 504
Cdd:PRK13409 176 FKGKVRE--LLK--KVDERgKLDEVVERLGLENILDRDI---------SELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190
....*....|....*....|....*....|
gi 495163667 505 LDAeTERQILA-LVKEVAVQKTLLMVTHRL 533
Cdd:PRK13409 243 LDI-RQRLNVArLIRELAEGKYVLVVEHDL 271
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
356-555 |
2.95e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.97 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLIT--RAWDPTSGDVMLDGVSITgYREAALRATMSVV-----PqrVHLFSA 428
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESIL-DLEPEERAHLGIFlafqyP--IEIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 429 TLRDNLLLA---------APQADDAALGAVLArvglEKL----LDDEGLNAWLGEGgrqLSGGELRRLGIARALLHNAPM 495
Cdd:CHL00131 100 SNADFLRLAynskrkfqgLPELDPLEFLEIIN----EKLklvgMDPSFLSRNVNEG---FSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163667 496 LLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTH--RLQGLTAFDRIIVMDNGQITEQGS 555
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMTSeNSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
351-561 |
3.97e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.14 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 351 QPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTS--GDVMLDGVSITgyrEAALRATMSVVPQRVHLFSA 428
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT---KQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 429 TLRDNL----LLAAPQA---DDAALGA--VLARVGLEKLLDDEGLNAWLgeggRQLSGGELRRLGIARALLHNAPMLLLD 499
Cdd:PLN03211 156 TVRETLvfcsLLRLPKSltkQEKILVAesVISELGLTKCENTIIGNSFI----RGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 500 EPTEGLDAETE-RQILALVKEVAVQKTLLMVTHRLQG--LTAFDRIIVMDNGQITEQGSHKELLA 561
Cdd:PLN03211 232 EPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
355-562 |
4.16e-12 |
|
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: 68.68 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVML----DGVSIT--GYREAAlRAT--MSVVPQRVHLF 426
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTkpGPDGRG-RAKryIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 427 S-ATLRDNLL----LAAPQaDDAALGAV--LARVGleklLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLD 499
Cdd:TIGR03269 378 PhRTVLDNLTeaigLELPD-ELARMKAVitLKMVG----FDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 500 EPTEGLDAETERQ----ILALVKEvaVQKTLLMVTHRLQG-LTAFDRIIVMDNGQITEQGSHKELLAQ 562
Cdd:TIGR03269 453 EPTGTMDPITKVDvthsILKAREE--MEQTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-560 |
4.23e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.40 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWD-----PTSGDVMLDGVSItgYREAA----LRATMSVVPQRVHLF 426
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNI--YSPDVdpieVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 427 S-ATLRDNL--------LLAAPQADDAALGAVLARVGLEKLLDDEgLNAWLGeggrQLSGGELRRLGIARALLHNAPMLL 497
Cdd:PRK14267 98 PhLTIYDNVaigvklngLVKSKKELDERVEWALKKAALWDEVKDR-LNDYPS----NLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 498 LDEPTEGLDAETERQILALVKEVAVQKTLLMVTHR-LQGLTAFDRIIVMDNGQITEQGSHKELL 560
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
343-559 |
8.24e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 8.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 343 NVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKS----TLLQLITRAWDPTSGDVML------DGVSITGYREAAL 412
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLlrrrsrQVIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 413 R----ATMSVVPQR-------VHLFSATLRDNLLLAAPQADDAALGAvlARVGLEKLLDDEGlNAWLGEGGRQLSGGELR 481
Cdd:PRK10261 99 RhvrgADMAMIFQEpmtslnpVFTVGEQIAESIRLHQGASREEAMVE--AKRMLDQVRIPEA-QTILSRYPHQLSGGMRQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 482 RLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKevAVQKTLLM----VTHRLqGLTA--FDRIIVMDNGQITEQGS 555
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK--VLQKEMSMgvifITHDM-GVVAeiADRVLVMYQGEAVETGS 252
|
....
gi 495163667 556 HKEL 559
Cdd:PRK10261 253 VEQI 256
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
363-533 |
8.46e-12 |
|
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: 65.47 E-value: 8.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 363 VAPGEHIAILGRTGCGKSTLLQLIT--------RAWDPTSGDVMLD---GVSITGYREAALRATMSVV--PQRVHLFSAT 429
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIvkPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 430 LRDNLLLAAPQADD-AALGAVLARVGLEKLLDDEGlnawlgeggRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAE 508
Cdd:cd03236 103 VKGKVGELLKKKDErGKLDELVDQLELRHVLDRNI---------DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180
....*....|....*....|....*.
gi 495163667 509 TERQILALVKEVAVQ-KTLLMVTHRL 533
Cdd:cd03236 174 QRLNAARLIRELAEDdNYVLVVEHDL 199
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
332-532 |
1.63e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 332 DAPREASLSLRNVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRA--WDPTSGDVMLDGVSItgYRE 409
Cdd:COG2401 22 DLSERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDVPDNQF--GRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 410 aalratmsvvpqrvhlfsATLRDNLLLAAPqADDAAlgAVLARVGLEkllddeglNAWLGEGG-RQLSGGELRRLGIARA 488
Cdd:COG2401 100 ------------------ASLIDAIGRKGD-FKDAV--ELLNAVGLS--------DAVLWLRRfKELSTGQKFRFRLALL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495163667 489 LLHNAPMLLLDEPTEGLDAETERQILALVKEVA--VQKTLLMVTHR 532
Cdd:COG2401 151 LAERPKLLVIDEFCSHLDRQTAKRVARNLQKLArrAGITLVVATHH 196
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
334-566 |
1.79e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 334 PREASLSLRNVSfsypGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYR--EAA 411
Cdd:PRK10982 246 PGEVILEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNanEAI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 412 LRATMSVVPQRVhlfSATLRDNLllaapqadDAALGAVLARVGLEK----LLDDEGLNA---WLGEGGR----------- 473
Cdd:PRK10982 322 NHGFALVTEERR---STGIYAYL--------DIGFNSLISNIRNYKnkvgLLDNSRMKSdtqWVIDSMRvktpghrtqig 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 474 QLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTH---RLQGLTafDRIIVMDNGQ 549
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGIIIISSempELLGIT--DRILVMSNGL 468
|
250 260
....*....|....*....|..
gi 495163667 550 I-----TEQGSHKELLAQQGRY 566
Cdd:PRK10982 469 VagivdTKTTTQNEILRLASLH 490
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
339-535 |
1.83e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYpgQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYReAALRATMSV 418
Cdd:PRK13540 2 LDVIELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDL-CTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLF-SATLRDNLLLAAPQADDAALGAVLARV-GLEKLLDDE-GLnawlgeggrqLSGGELRRLGIARALLHNAPM 495
Cdd:PRK13540 79 VGHRSGINpYLTLRENCLYDIHFSPGAVGITELCRLfSLEHLIDYPcGL----------LSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495163667 496 LLLDEPTEGLDaetERQILALVKEVAvqktllmvTHRLQG 535
Cdd:PRK13540 149 WLLDEPLVALD---ELSLLTIITKIQ--------EHRAKG 177
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
22-281 |
2.31e-11 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 64.72 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 22 VVLAIVTLLASIGLlTLSGWFLSASAV--VGMAGLYSFNYMLPAAGVR-GAAIIRTAGRYFERLVSHEGTFRVLEHLRVY 98
Cdd:cd18544 1 FILALLLLLLATAL-ELLGPLLIKRAIddYIVPGQGDLQGLLLLALLYlGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 99 TFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLDVTLALtlggIMLATLlllp 178
Cdd:cd18544 80 LFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLAL----ISLLVL---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 179 plfyragrPVGEALTML-----RASYRQ------QLTGWLQ----GQAELSIFGAAGRYREQLDTTEQVWHEAQRRQAGL 243
Cdd:cd18544 152 --------PLLLLATYLfrkksRKAYREvreklsRLNAFLQesisGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKL 223
|
250 260 270
....*....|....*....|....*....|....*....
gi 495163667 244 TALSQAMMTLISGMTVVLILWMAAGGV-GGNSTPGSLIA 281
Cdd:cd18544 224 FALFRPLVELLSSLALALVLWYGGGQVlSGAVTLGVLYA 262
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
363-548 |
2.97e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.67 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 363 VAPGEHIAILGRTGCGKSTLLQLITRAWDP---TSGDVMLDGVSItgyREAALRATMSVVPQRVHLFSATLRDNLLLAA- 438
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPL---DSSFQRSIGYVQQQDLHLPTSTVRESLRFSAy 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 439 ---PQA-----DDAALGAVLARVGLEKLLDdeglnAWLGEGGRQLSGGELRRLGIARALLHNAPMLL-LDEPTEGLDAET 509
Cdd:TIGR00956 863 lrqPKSvskseKMEYVEEVIKLLEMESYAD-----AVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495163667 510 ERQILALVKEVAVQ-KTLLMVTHRLQG--LTAFDRIIVMDNG 548
Cdd:TIGR00956 938 AWSICKLMRKLADHgQAILCTIHQPSAilFEEFDRLLLLQKG 979
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
339-560 |
1.36e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSypgqpqPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITrAWDPTSGDVMLDGVSITGYREAAL---RAT 415
Cdd:PRK03695 1 MQLNDVAVS------TRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMA-GLLPGSGSIQFAGQPLEAWSAAELarhRAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 416 MS---VVPQRVHLFSATLRDNLLLAAPQADDAALGAVLARVGLEKLLddeglnawlgegGR---QLSGGELRRLGIARAL 489
Cdd:PRK03695 74 LSqqqTPPFAMPVFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKL------------GRsvnQLSGGEWQRVRLAAVV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 490 LH-------NAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKELL 560
Cdd:PRK03695 142 LQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQgIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
22-281 |
1.65e-10 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 62.06 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 22 VVLAIVTLLASIGLLTLSGWFLSaSAV--VGMAGLYSfNYMLPAAGVRGAAIIRTAGRYFERLVSHEGTFRVLEHLRVYT 99
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIR-RIIdsVIGGGLRE-LLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 100 FSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLDVTLALtlggIMLATLLLLPP 179
Cdd:cd18542 79 YDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTL----ISLAIIPFIAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 180 LFYRAGRPVGEALTMLRASYrqqltgwlqgqAELS------IFG-------AAGRY-REQLDTTEQVWHEAQRRQAGLTA 245
Cdd:cd18542 155 FSYVFFKKVRPAFEEIREQE-----------GELNtvlqenLTGvrvvkafAREDYeIEKFDKENEEYRDLNIKLAKLLA 223
|
250 260 270
....*....|....*....|....*....|....*....
gi 495163667 246 LSQAMMTLISGMTVVLILWmaAGG---VGGNSTPGSLIA 281
Cdd:cd18542 224 KYWPLMDFLSGLQIVLVLW--VGGylvINGEITLGELVA 260
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
18-314 |
3.74e-10 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 61.28 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 18 LSLGVVLAIVTLLASIGLLTLSGWFLSasaVVGMAGLYSFNYMLPAAGVrGAAIIRTAGRYFERLVSHEGTFRVLEHLRV 97
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLD---DIFVEKDLEALLLVPLAII-GLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 98 YTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLDVTLALtlggIMLATLLLL 177
Cdd:cd18552 77 DLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTL----IALVVLPLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 178 PPLFYRAGRpvgealTMLRASYRQQ-----LTGWLQ----GQAELSIFGAAGRYREQLDTTEQVWHEAQRRQAGLTALSQ 248
Cdd:cd18552 153 ALPIRRIGK------RLRKISRRSQesmgdLTSVLQetlsGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSS 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 249 AMMTLISGMTVVLILWMAAGGV-GGNSTPGSLIAlFVFCALAAFEALAPVGGAFQHLGQVIASARRV 314
Cdd:cd18552 227 PLMELLGAIAIALVLWYGGYQViSGELTPGEFIS-FITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
336-553 |
6.08e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 336 EASLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDG--VSITGYREAAlR 413
Cdd:PRK10762 2 QALLQLKGIDKAFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkeVTFNGPKSSQ-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 414 ATMSVVPQRVHLFSA-TLRDNLLLAA---------------PQADdaalgAVLARVGLE---KLLddeglnawLGEggrq 474
Cdd:PRK10762 79 AGIGIIHQELNLIPQlTIAENIFLGRefvnrfgridwkkmyAEAD-----KLLARLNLRfssDKL--------VGE---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 475 LSGGELRRLGIARALLHNAPMLLLDEPTEGL-DAETErQILALVKEVAVQKT-LLMVTHRLQGL-TAFDRIIVMDNGQ-I 550
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETE-SLFRVIRELKSQGRgIVYISHRLKEIfEICDDVTVFRDGQfI 220
|
...
gi 495163667 551 TEQ 553
Cdd:PRK10762 221 AER 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
361-562 |
7.04e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 361 LDVAPGEHIAILGRTGCGKSTLlqliTRAwdpTSGDVMLdgvsITGYREAAL-RATMSVVPQRVHLFSAT-LRDNLLLAA 438
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSAL----ARA---LAGELPL----LSGERQSQFsHITRLSFEQLQKLVSDEwQRNNTDMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 439 PQADDAalGAVLARVGLEKLLDDE---------GLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAET 509
Cdd:PRK10938 93 PGEDDT--GRTTAEIIQDEVKDPArceqlaqqfGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 510 ERQILALVKEVAVQK-TLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQ 562
Cdd:PRK10938 171 RQQLAELLASLHQSGiTLVLVLNRFDEIPDFvQFAGVLADCTLAETGEREEILQQ 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
365-533 |
8.60e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 61.34 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 365 PGEHIAILGRTGCGKSTLL-----QLIT---RAWDPTSGDVMLD---GVSITGYREAALRATMSVV--PQRVHL----FS 427
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALkilsgELKPnlgDYDEEPSWDEVLKrfrGTELQDYFKKLANGEIKVAhkPQYVDLipkvFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 428 ATLRDnlLLAapQADD-AALGAVLARVGLEKLLDDEGlnawlgeggRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLD 506
Cdd:COG1245 178 GTVRE--LLE--KVDErGKLDELAEKLGLENILDRDI---------SELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180
....*....|....*....|....*....
gi 495163667 507 AeTERQILA-LVKEVAVQ-KTLLMVTHRL 533
Cdd:COG1245 245 I-YQRLNVArLIRELAEEgKYVLVVEHDL 272
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
357-551 |
1.02e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 357 RDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAA-LRATMSVVP---QRVHLF------ 426
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYldapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 427 ----SATLRDNLLLAAPQADDAALGAVLARVGLeKLLDDEglnawlgEGGRQLSGGELRRLGIARALLHNAPMLLLDEPT 502
Cdd:PRK15439 360 wnvcALTHNRRGFWIKPARENAVLERYRRALNI-KFNHAE-------QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495163667 503 EGLDAETERQILALVKEVAVQKT-LLMVT---HRLQGLTafDRIIVMDNGQIT 551
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVaVLFISsdlEEIEQMA--DRVLVMHQGEIS 482
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
474-562 |
1.08e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 60.30 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 474 QLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTAF-DRIIVMDNGQI 550
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQgtSILLISHDLESISQWaDTITVLYCGQT 237
|
90
....*....|..
gi 495163667 551 TEQGSHKELLAQ 562
Cdd:COG4170 238 VESGPTEQILKS 249
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
474-559 |
1.37e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.76 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 474 QLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLT-AFDRIIVMDNGQI 550
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVAeAAHKIIVMYAGQV 232
|
....*....
gi 495163667 551 TEQGSHKEL 559
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
355-554 |
1.95e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.25 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSI---TGYREAALRATM---------SVVPQR 422
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIqfifqdpyaSLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 423 VHLFS--ATLRDNLLLAApQADDAALGAVLARVGLEKllddegLNAWlgEGGRQLSGGELRRLGIARALLHNAPMLLLDE 500
Cdd:PRK10261 419 TVGDSimEPLRVHGLLPG-KAAAARVAWLLERVGLLP------EHAW--RYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495163667 501 PTEGLDAETERQILALVKEvaVQKTL----LMVTHRLQGLTAFD-RIIVMDNGQITEQG 554
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLD--LQRDFgiayLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
362-544 |
2.06e-09 |
|
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: 57.20 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 362 DVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVsitgyreaalraTMSVVPQRVhlfsatlrdnlllaapqa 441
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------TPVYKPQYI------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 442 ddaalgavlarvglekllddeglnawlgeggrQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVA 521
Cdd:cd03222 71 --------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*.
gi 495163667 522 V--QKTLLMVTHRLQGLTAF-DRIIV 544
Cdd:cd03222 119 EegKKTALVVEHDLAVLDYLsDRIHV 144
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
343-562 |
2.17e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.35 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 343 NVSFSYPGQPQPALRDITLDVAPGEHIAILGRTGCGKS----TLLQLITRAwDPTSGDVMLDGVSITGYREAALRATmsv 418
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAAN-GRIGGSATFNGREILNLPEKELNKL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 vpqRVHLFSATLRDNLLLAAPqaddaalgavLARVG---LEKLLDDEGLN---AWLgEGGRQL----------------- 475
Cdd:PRK09473 95 ---RAEQISMIFQDPMTSLNP----------YMRVGeqlMEVLMLHKGMSkaeAFE-ESVRMLdavkmpearkrmkmyph 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 476 --SGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVA--VQKTLLMVTHRLqGLTA--FDRIIVMDNGQ 549
Cdd:PRK09473 161 efSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKreFNTAIIMITHDL-GVVAgiCDKVLVMYAGR 239
|
250
....*....|...
gi 495163667 550 ITEQGSHKELLAQ 562
Cdd:PRK09473 240 TMEYGNARDVFYQ 252
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
339-509 |
2.84e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRN--VSFSYpgqpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLItrawdptSGDVMLDG----------VS--- 403
Cdd:PRK11147 4 ISIHGawLSFSD----APLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDgriiyeqdliVArlq 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 404 ------ITG----YREAALRATMSVVP---QRVHLFSATLRDNLL--LAAPQAD---------DAALGAVLARVGLEKll 459
Cdd:PRK11147 73 qdpprnVEGtvydFVAEGIEEQAEYLKryhDISHLVETDPSEKNLneLAKLQEQldhhnlwqlENRINEVLAQLGLDP-- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495163667 460 dDEGLNAwlgeggrqLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAET 509
Cdd:PRK11147 151 -DAALSS--------LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
341-549 |
2.93e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 341 LRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDG--VSITGYREaALRATMSV 418
Cdd:PRK10982 1 MSNISKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSKE-ALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLF-SATLRDNLLLA-----APQADDAALgavlaRVGLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHN 492
Cdd:PRK10982 78 VHQELNLVlQRSVMDNMWLGryptkGMFVDQDKM-----YRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163667 493 APMLLLDEPTEGLdaeTERQILALVKEVAVQKT----LLMVTHRLQGLTAF-DRIIVMDNGQ 549
Cdd:PRK10982 153 AKIVIMDEPTSSL---TEKEVNHLFTIIRKLKErgcgIVYISHKMEEIFQLcDEITILRDGQ 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
357-552 |
4.31e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 357 RDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYRE-AALRATMSVVPQR------VHLFSat 429
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITESrrdngfFPNFS-- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 430 LRDNLLLAaPQADDAALGAVLarvGL------EKLLDDE---------GLNAWLGEggrqLSGGELRRLGIARALLHNAP 494
Cdd:PRK09700 358 IAQNMAIS-RSLKDGGYKGAM---GLfhevdeQRTAENQrellalkchSVNQNITE----LSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 495 MLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQITE 552
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
365-548 |
5.41e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 365 PGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLdgVSITGYREAALratmsvvpqrvhlfsatlrdnlllaapqadda 444
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVL-------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 445 algavlarvgleklldDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALV------- 517
Cdd:smart00382 47 ----------------DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllll 110
|
170 180 190
....*....|....*....|....*....|....*..
gi 495163667 518 KEVAVQKTLLMVTHRLQGL------TAFDRIIVMDNG 548
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLgpallrRRFDRRIVLLLI 147
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
302-563 |
1.09e-08 |
|
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: 57.91 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 302 QHLGQVIASARRVSDVIDQPADITFAESGKDAPREAS---LSLRNVSFSYPGQPQ-PALRDITLDVAPGEHIAILGRTGC 377
Cdd:TIGR02633 218 QHVATKDMSTMSEDDIITMMVGREITSLYPHEPHEIGdviLEARNLTCWDVINPHrKRVDDVSFSLRRGEILGVAGLVGA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 378 GKSTLLQLITRAWDPT-SGDVMLDGVSITGYREA-ALRATMSVVPQ--RVHLFSATLR--DNLLLAAPQA-------DDA 444
Cdd:TIGR02633 298 GRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAqAIRAGIAMVPEdrKRHGIVPILGvgKNITLSVLKSfcfkmriDAA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 445 A-LGAVLARVgleKLLDDEGLNAWLGEGGrqLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ 523
Cdd:TIGR02633 378 AeLQIIGSAI---QRLKVKTASPFLPIGR--LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE 452
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 495163667 524 K-TLLMVTHRL-QGLTAFDRIIVMDNGQITEQGSHKELLAQQ 563
Cdd:TIGR02633 453 GvAIIVVSSELaEVLGLSDRVLVIGEGKLKGDFVNHALTQEQ 494
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
356-531 |
1.29e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.87 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVML-DGVSItGY----REAALRATMSVVPQRVHLfsatl 430
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKL-GYfaqhQLEFLRADESPLQHLARL----- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 431 rdnlllaAPQADDAALGAVLARVGLEkllDDEglnawLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETe 510
Cdd:PRK10636 402 -------APQELEQKLRDYLGGFGFQ---GDK-----VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM- 465
|
170 180
....*....|....*....|...
gi 495163667 511 RQIL--ALVKevaVQKTLLMVTH 531
Cdd:PRK10636 466 RQALteALID---FEGALVVVSH 485
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
356-558 |
1.94e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWD----PTSGDVMLDGVSItgyREAALRATMSVV---PQRVHLFSA 428
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITP---EEIKKHYRGDVVynaETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 429 TLRDNLLLAA----PQ---------ADDAALGAVLARV-GLEKLLDDEGLNAWLgeggRQLSGGELRRLGIARALLHNAP 494
Cdd:TIGR00956 154 TVGETLDFAArcktPQnrpdgvsreEYAKHIADVYMATyGLSHTRNTKVGNDFV----RGVSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 495 MLLLDEPTEGLDAETERQILALVKEVA--VQKTLLMVTHRL--QGLTAFDRIIVMDNGQITEQGSHKE 558
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRALKTSAniLDTTPLVAIYQCsqDAYELFDKVIVLYEGYQIYFGPADK 297
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
358-551 |
2.26e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 358 DITLDVAPGEHIAILGRTGCGKSTLLQLITRAWD-PTSGDVMLDG--VSITGYREAaLRATMSVVPQ-RVhlfsatlRDN 433
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRNPQQA-IAQGIAMVPEdRK-------RDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 434 LLLAAPQADDAALgAVLARVGLEKLLDDEG-LNAWLGEGGR-------------QLSGGELRRLGIARALLHNAPMLLLD 499
Cdd:PRK13549 352 IVPVMGVGKNITL-AALDRFTGGSRIDDAAeLKTILESIQRlkvktaspelaiaRLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 500 EPTEGLD----AETERQILALVKE-VAVqktlLMVTHRLQ---GLTafDRIIVMDNGQIT 551
Cdd:PRK13549 431 EPTRGIDvgakYEIYKLINQLVQQgVAI----IVISSELPevlGLS--DRVLVMHEGKLK 484
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
339-552 |
2.67e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLITrAWDPT---SGDVMLDG-------------- 401
Cdd:NF040905 2 LEMRGITKTFPGVK--ALDDVNLSVREGEIHALCGENGAGKSTLMKVLS-GVYPHgsyEGEILFDGevcrfkdirdseal 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 402 --VSItgYREAALRATMSVVpqrvhlfsatlrDNLLLAAPQA-------DDAALGAV--LARVGLEK----LLDDeglna 466
Cdd:NF040905 79 giVII--HQELALIPYLSIA------------ENIFLGNERAkrgvidwNETNRRARelLAKVGLDEspdtLVTD----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 467 wLGEGGRQLsggelrrLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK-TLLMVTHRLQGLTAF-DRIIV 544
Cdd:NF040905 140 -IGVGKQQL-------VEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGiTSIIISHKLNEIRRVaDSITV 211
|
....*...
gi 495163667 545 MDNGQITE 552
Cdd:NF040905 212 LRDGRTIE 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
333-558 |
4.44e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 333 APR---EASLSLRNVSfsYPGQPQPalrdITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDG--VSITGY 407
Cdd:PRK11288 249 RPRplgEVRLRLDGLK--GPGLREP----ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSP 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 408 REAaLRATMSVVPQR------VHLfsATLRDNLLLAAPQAddaalgavLARVGLekLLDD--EGLNAWL--------GEG 471
Cdd:PRK11288 323 RDA-IRAGIMLCPEDrkaegiIPV--HSVADNINISARRH--------HLRAGC--LINNrwEAENADRfirslnikTPS 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 472 GRQ----LSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK-TLLMVTHRLQ---GLTafDRII 543
Cdd:PRK11288 390 REQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGvAVLFVSSDLPevlGVA--DRIV 467
|
250
....*....|....*
gi 495163667 544 VMDNGQITEQGSHKE 558
Cdd:PRK11288 468 VMREGRIAGELAREQ 482
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
333-561 |
4.67e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 333 APREASLSLRNVSfsypgqpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITgyreaal 412
Cdd:PRK10762 252 APGEVRLKVDNLS-------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV------- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 413 ratmSVVPQR------VHLFSATLRDNLLLAAPQADDAALGAV--LARVGLEKLLDDE----------------GLNAWL 468
Cdd:PRK10762 318 ----TRSPQDglangiVYISEDRKRDGLVLGMSVKENMSLTALryFSRAGGSLKHADEqqavsdfirlfniktpSMEQAI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 469 GEggrqLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK-TLLMVTHRL-QGLTAFDRIIVMD 546
Cdd:PRK10762 394 GL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGlSIILVSSEMpEVLGMSDRILVMH 469
|
250 260
....*....|....*....|
gi 495163667 547 NGQIT-----EQGSHKELLA 561
Cdd:PRK10762 470 EGRISgeftrEQATQEKLMA 489
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
355-506 |
5.45e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSIT----------GYreaalratMSvvpQRVH 424
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDagdiatrrrvGY--------MS---QAFS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 425 LFSA-TLRDNLLLAA-----PQAD-DAALGAVLARVGLEKLLDDegLNAWLGEGGRQlsggelrRLGIARALLHNAPMLL 497
Cdd:NF033858 350 LYGElTVRQNLELHArlfhlPAAEiAARVAEMLERFDLADVADA--LPDSLPLGIRQ-------RLSLAVAVIHKPELLI 420
|
....*....
gi 495163667 498 LDEPTEGLD 506
Cdd:NF033858 421 LDEPTSGVD 429
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
474-561 |
5.66e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.81 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 474 QLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK--TLLMVTHRLQGLTAF-DRIIVMDNGQI 550
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQWaDKINVLYCGQT 237
|
90
....*....|.
gi 495163667 551 TEQGSHKELLA 561
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
355-570 |
6.87e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.74 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVAPGEHIAILGRTGCGKSTLlQLITRAWDPTSGDVMLDGVSITGYREAaLRATMS----VVPQRVHLFSAtl 430
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRA-LRRTIG*hrpVR*GRRESFSG-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 431 RDNLLLAAPQADdaaLGAVLARVGLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETE 510
Cdd:NF000106 104 RENLYMIGR*LD---LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163667 511 RQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQ-QGRYYQFR 570
Cdd:NF000106 181 NEVWDEVRSMVRDgATVLLTTQYMEEAEQLaHELTVIDRGRVIADGKVDELKTKvGGRTLQIR 243
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
347-508 |
8.31e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 347 SYPGQPQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSVVPQRVHLF 426
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 427 SaTLRDNLLLAAPQADDAAL--GAVLARVGLEKLLDDEglnawlgegGRQLSGGELRRLGIARALLHNAPMLLLDEPTEG 504
Cdd:PRK13543 98 S-TLENLHFLCGLHGRRAKQmpGSALAIVGLAGYEDTL---------VRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
....
gi 495163667 505 LDAE 508
Cdd:PRK13543 168 LDLE 171
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-314 |
8.75e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 54.08 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 18 LSLGVVLAIVTLLASIGLLTLSGWFLSASAVVGMAGLYSFNYMLPAAGvrgAAIIRTAGRYFERLVSHEGTFRVLEHLRV 97
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLG---AYLLRALLNFLRIYLNHVAEQKVVADLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 98 YTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLDVTLALtlggIMLAT---L 174
Cdd:cd18778 78 DLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLAL----LTLIPipfL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 175 LLLPPLFYRAGRP----VGEALTMLRASYRQQLTGWLQGQAelsiFGAAGRYREQLDTTEQVWHEAQRRQAGLTALSQAM 250
Cdd:cd18778 154 ALGAWLYSKKVRPryrkVREALGELNALLQDNLSGIREIQA----FGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 251 MTLISGMTVVLILWMAAGGV-GGNSTPGSLIALFVFCALaAFEALAPVGGAFQHLGQVIASARRV 314
Cdd:cd18778 230 MEFLTSLGTVLVLGFGGRLVlAGELTIGDLVAFLLYLGL-FYEPITSLHGLNEMLQRALAGAERV 293
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
356-557 |
9.72e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.24 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLIT--RAWDPTSGDVMLDG--------VSITGYREAALRATMSVVPQRVHL 425
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGfpkkqetfARISGYCEQNDIHSPQVTVRESLI 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 426 FSATLRdnllLAAPQADDAAL---GAVLARVGLEKLLDD-EGLNAWLGeggrqLSGGELRRLGIARALLHNAPMLLLDEP 501
Cdd:PLN03140 976 YSAFLR----LPKEVSKEEKMmfvDEVMELVELDNLKDAiVGLPGVTG-----LSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 502 TEGLDAETERQILALVKE-VAVQKTLLMVTHR--LQGLTAFDRIIVMD-NGQITEQG-----SHK 557
Cdd:PLN03140 1047 TSGLDARAAAIVMRTVRNtVDTGRTVVCTIHQpsIDIFEAFDELLLMKrGGQVIYSGplgrnSHK 1111
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
355-549 |
1.21e-07 |
|
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: 54.45 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITR-----AWDptsGDVMLDGVSI--TGYREAAlRATMSVVPQRVHLF- 426
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgTWD---GEIYWSGSPLkaSNIRDTE-RAGIVIIHQELTLVp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 427 SATLRDNLLLA------APQADDAALGAVLARVGLEKLLDDEGLNAWLGeggrQLSGGELRRLGIARALLHNAPMLLLDE 500
Cdd:TIGR02633 92 ELSVAENIFLGneitlpGGRMAYNAMYLRAKNLLRELQLDADNVTRPVG----DYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495163667 501 PTEGLDAETERQILALVKEVAVQK-TLLMVTHRLQGLTAF-DRIIVMDNGQ 549
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAHGvACVYISHKLNEVKAVcDTICVIRDGQ 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
339-549 |
2.04e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.78 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLIT--RAWDPTSGDVMLD---------------G 401
Cdd:PRK13549 6 LEMKNITKTFGGVK--ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvYPHGTYEGEIIFEgeelqasnirdteraG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 402 VSITgYREAALRATMSVvpqrvhlfsatlrdnlllaapqADDAALGAVLARVGL----------EKLLDDEGLNAWLGEG 471
Cdd:PRK13549 84 IAII-HQELALVKELSV----------------------LENIFLGNEITPGGImdydamylraQKLLAQLKLDINPATP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 472 GRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQK-TLLMVTHRLQGLTAF-DRIIVMDNGQ 549
Cdd:PRK13549 141 VGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGiACIYISHKLNEVKAIsDTICVIRDGR 220
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
70-314 |
2.05e-07 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 52.81 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 70 AIIRTAGRYFERLVSHEGTFRVLEHLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVD-TLDHLYLRVISPLIGALAVI 148
Cdd:cd18554 56 LILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEqTKDFITTGLMNIWLDMITII 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 149 AVVTLGLsLLDVTLALtLGGIMLATLLLLPPLFYRAGRpvgeALTMLRASYRQQLTGWL----QGQAELSIFGAAGRYRE 224
Cdd:cd18554 136 IAICIML-VLNPKLTF-VSLVIFPFYILAVKYFFGRLR----KLTKERSQALAEVQGFLheriQGMSVIKSFALEKHEQK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 225 QLDTTEQVWHEAQRRQAGLTALSQAMMTLISGMTVVLILWMAAGGV-GGNSTPGSLIALFVFCALaAFEALAPVGGAFQH 303
Cdd:cd18554 210 QFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLViEGNLTVGTLVAFVGYMER-MYSPLRRLVNSFTT 288
|
250
....*....|.
gi 495163667 304 LGQVIASARRV 314
Cdd:cd18554 289 LTQSFASMDRV 299
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
25-314 |
2.12e-07 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 52.87 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 25 AIVTLLASIGLLTLSGWFLSASAVVGMAGLYSFNYMLPAAGVRGAAIIRTAGRYFERLVSHEGTFRVLEHLRVYTFSRLL 104
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 105 PLSPSGLARFRQGELLNRLVADVDTLDHL-------YLRVISPLIGALAVIAVVTLGLSLLdvtLALTLGGIMLATllll 177
Cdd:cd18576 81 RLPLSFFHERRVGELTSRLSNDVTQIQDTltttlaeFLRQILTLIGGVVLLFFISWKLTLL---MLATVPVVVLVA---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 178 pPLFYRAGRP--------VGEALTMLRASyrqqltgwLQGQAELSIFGA----AGRYREQLDTTEQVWHEAQRRQAGLTA 245
Cdd:cd18576 154 -VLFGRRIRKlskkvqdeLAEANTIVEET--------LQGIRVVKAFTRedyeIERYRKALERVVKLALKRARIRALFSS 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495163667 246 LsqaMMTLISGmTVVLILWMAAGGV-GGNSTPGSLIALFVFCAL--AAFEALAPVGGAFQhlgQVIASARRV 314
Cdd:cd18576 225 F---IIFLLFG-AIVAVLWYGGRLVlAGELTAGDLVAFLLYTLFiaGSIGSLADLYGQLQ---KALGASERV 289
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
13-281 |
3.33e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 52.13 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 13 RHKWLLSLGVVLAIVTLLAsiglltlsgwfLSASAVVGMAGLysfnymlpaagvrgAAIIRTAGRYFERLVSHegtfRVL 92
Cdd:cd18564 36 PGLLGLAPLLGPDPLALLL-----------LAAAALVGIALL--------------RGLASYAGTYLTALVGQ----RVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 93 EHLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLDVTLALtlggIMLA 172
Cdd:cd18564 87 LDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLAL----IALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 173 TLLLLPPLFYRAGRPVGEALTMLRASyrqqlTGWLQGQAELSI--------FGAAGRYREQLDTTEQVWHEAQRRQAGLT 244
Cdd:cd18564 163 VAPLLLLAARRFSRRIKEASREQRRR-----EGALASVAQESLsairvvqaFGREEHEERRFARENRKSLRAGLRAARLQ 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 495163667 245 ALSQAMMTLISGMTVVLILWMAAGGV-GGNSTPGSLIA 281
Cdd:cd18564 238 ALLSPVVDVLVAVGTALVLWFGAWLVlAGRLTPGDLLV 275
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
358-511 |
6.80e-07 |
|
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: 52.24 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 358 DITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVML-DGVSItGYreaalratmsvVPQRvhlfsatlRDNLll 436
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKL-AY-----------VDQS--------RDAL-- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 437 aapqaDDAAlgAVLARV--GLEKL-LDDEGLN--AWLG----EGGRQ------LSGGELRRLGIARALLHNAPMLLLDEP 501
Cdd:TIGR03719 398 -----DPNK--TVWEEIsgGLDIIkLGKREIPsrAYVGrfnfKGSDQqkkvgqLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
170
....*....|
gi 495163667 502 TEGLDAETER 511
Cdd:TIGR03719 471 TNDLDVETLR 480
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
18-314 |
1.08e-06 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 50.51 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 18 LSLGVVLAIVTLLASIGLLTLSGWFLSAsavVGMAGLYSFNYMLPAAGVRGAAIIRTAGRYFERLVSHegtfRVLEHLRV 97
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDA---LSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGE----RVVLDLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 98 YTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLI-GALAVIAVVTLgLSLLDVTLALtlggIMLATLLL 176
Cdd:cd18551 74 RLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVtGVLTVVGAVVL-MFLLDWVLTL----VTLAVVPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 177 LPPLFYRAGRPVGealtmlRASYR-QQLTGWLQGQAE--LS------IFGAAGRYREQLDTTEQVWHEAQRRQAGLTALS 247
Cdd:cd18551 149 AFLIILPLGRRIR------KASKRaQDALGELSAALEraLSairtvkASNAEERETKRGGEAAERLYRAGLKAAKIEALI 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 248 QAMMTLIsgMTVVLILWMAAGGV---GGNSTPGSLIAlFVFCALAAFEALAPVGGAFQHLGQVIASARRV 314
Cdd:cd18551 223 GPLMGLA--VQLALLVVLGVGGArvaSGALTVGTLVA-FLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
18-285 |
4.74e-06 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 48.41 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 18 LSLGVVLAIVTLLASIGLLTLSGWFLSASAVVGMAGLYSFNYMlpAAGVRGAAIIRTAGRYF-ERLVSHEGTfRVLEHLR 96
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVY--SLALLLLGLAQFILSFLqSYLLNHTGE-RLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 97 VYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLDVTLALtlggIMLATLLL 176
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTL----VLLAVLPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 177 LPPLFYRAGRPVGEALTMLRASYR---QQLTGWLQGQAELSIFGAAGRYREQLDTTEQVWHEAQRRQAGLTALSQAMMTL 253
Cdd:pfam00664 154 YILVSAVFAKILRKLSRKEQKAVAkasSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQF 233
|
250 260 270
....*....|....*....|....*....|...
gi 495163667 254 ISGMTVVLILWMAAGGVG-GNSTPGSLIALFVF 285
Cdd:pfam00664 234 IGYLSYALALWFGAYLVIsGELSVGDLVAFLSL 266
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
356-561 |
6.41e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPT---SGDVMLDGvsiTGYREAALRATMSVVPQR-VHLFSATLR 431
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNG---YRLNEFVPRKTSAYISQNdVHVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 432 DNLLLAA-------------------------PQAD-DAALGAVLARVGLEKLLDDEGLNAwLG-----------EGGRQ 474
Cdd:PLN03140 258 ETLDFSArcqgvgtrydllselarrekdagifPEAEvDLFMKATAMEGVKSSLITDYTLKI-LGldickdtivgdEMIRG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 475 LSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVA--VQKTLLMVThrLQ----GLTAFDRIIVMDNG 548
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVhlTEATVLMSL--LQpapeTFDLFDDIILLSEG 414
|
250
....*....|...
gi 495163667 549 QITEQGSHKELLA 561
Cdd:PLN03140 415 QIVYQGPRDHILE 427
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
21-314 |
6.92e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 47.94 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 21 GVVLAIVTLLASIGLLTLSGWFLSA-----------SAVVGMAGLYSFNymLPAAGVRgAAIIRTAGryfERLVSHegtf 89
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTiikggdldvlnELALILLAIYLLQ--SVFTFVR-YYLFNIAG---ERIVAR---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 90 rvlehLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLDVTLALTLGGI 169
Cdd:cd18557 71 -----LRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 170 MLATLLllpplfyrAGRPVGEALTMLRASYRQQltgwlqgQAELS--------------IFGA----AGRYREQLDTTeq 231
Cdd:cd18557 146 IPLLLI--------ASKIYGRYIRKLSKEVQDA-------LAKAGqvaeeslsnirtvrSFSAeekeIRRYSEALDRS-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 232 vwHEAQRRQAGLTALSQAMMTLISGMTVVLILWMAAGGVG-GNSTPGSLIAlFVFCALAAFEALAPVGGAFQHLGQVIAS 310
Cdd:cd18557 209 --YRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLsGQLTVGELTS-FILYTIMVASSVGGLSSLLADIMKALGA 285
|
....
gi 495163667 311 ARRV 314
Cdd:cd18557 286 SERV 289
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
370-531 |
1.08e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.45 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 370 AILGRTGCGKSTLLQLITRA--WD-PTSGDVMLDGVSITgyREAALRAtmsvvpqRVHL-FSatLRDNLLLAAPQADDAA 445
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYAltGElPPNSKGGAHDPKLI--REGEVRA-------QVKLaFE--NANGKKYTITRSLAIL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 446 LGAVLARVG-LEKLLDDEglnawLGeggrQLSGGE------LRRLGIARALLHNAPMLLLDEPTEGLDAET-ERQILALV 517
Cdd:cd03240 95 ENVIFCHQGeSNWPLLDM-----RG----RCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENiEESLAEII 165
|
170
....*....|....*.
gi 495163667 518 KEVAVQKT--LLMVTH 531
Cdd:cd03240 166 EERKSQKNfqLIVITH 181
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
475-556 |
1.41e-05 |
|
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: 45.78 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 475 LSGGELRRLGIARALLHNAP--MLLLDEPTEGLDAETERQILALVKEVAVQK-TLLMVTHRLQGLTAFDRIIVMDNGQiT 551
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGnTVILIEHNLDVLSSADWIIDFGPGS-G 166
|
....*
gi 495163667 552 EQGSH 556
Cdd:cd03238 167 KSGGK 171
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
474-545 |
2.12e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.04 E-value: 2.12e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 474 QLSGGELRRLGIARAL----LHNAPMLLLDEPTEGLDAETERQILALVKEVAVQKTLLMV-THRLQGLTAFDRIIVM 545
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIViTHLPELAELADKLIHI 153
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
356-568 |
3.31e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDG--------------------VSITGYRE-AALRA 414
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpalpqpaleYVIDGDREyRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 415 TMSVVPQRvhlfsatlRDNLLLAAPQADDAALGAVLARVGLEKLLDDEGL-NAWLGEGGRQLSGGELRRLGIARALLHNA 493
Cdd:PRK10636 97 QLHDANER--------NDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 494 PMLLLDEPTEGLDAETerqILALVKEV-AVQKTLLMVTHRLQGLTAF-DRIIVMDNGQITE-QGSHKEL-------LAQQ 563
Cdd:PRK10636 169 DLLLLDEPTNHLDLDA---VIWLEKWLkSYQGTLILISHDRDFLDPIvDKIIHIEQQSLFEyTGNYSSFevqratrLAQQ 245
|
....*
gi 495163667 564 GRYYQ 568
Cdd:PRK10636 246 QAMYE 250
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
474-511 |
3.50e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 3.50e-05
10 20 30
....*....|....*....|....*....|....*...
gi 495163667 474 QLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETER 511
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLR 482
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
90-283 |
4.15e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 45.56 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 90 RVLEHLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLIGALAVIAVVTLGLSLLDVTLALTLGGI 169
Cdd:cd18546 69 RLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 170 M----LATL--LLLPPLFYRAGRpvgEALTMLRASYRQQLTGWLQGQAelsiFGAAGRYREQLDTTEQVWHEAQRRQAGL 243
Cdd:cd18546 149 LpplaLATRwfRRRSSRAYRRAR---ERIAAVNADLQETLAGIRVVQA----FRRERRNAERFAELSDDYRDARLRAQRL 221
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495163667 244 TALSQAMMTLISGMTVVLILWMAAGGV-GGNSTPGSLIALF 283
Cdd:cd18546 222 VAIYFPGVELLGNLATAAVLLVGAWRVaAGTLTVGVLVAFL 262
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
74-302 |
6.53e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 45.17 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 74 TAGRYFerLVSHEGTfRVLEHLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLY-------LRVISPLIGALA 146
Cdd:cd18575 53 SALRFY--LVSWLGE-RVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVgsslsiaLRNLLLLIGGLV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 147 VIAVVTLGLSLLDV-TLALTLGGIMLatllllpplfyrAGRPVGealtmlRASYRQQLTgwlqgQAELSIFGA------- 218
Cdd:cd18575 130 MLFITSPKLTLLVLlVIPLVVLPIIL------------FGRRVR------RLSRASQDR-----LADLSAFAEetlsaik 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 219 -----------AGRYREQLDTTEQVwheAQRR---QAGLTALSqamMTLISGmTVVLILWMAAGGV-GGNSTPGSLIAlF 283
Cdd:cd18575 187 tvqaftredaeRQRFATAVEAAFAA---ALRRiraRALLTALV---IFLVFG-AIVFVLWLGAHDVlAGRMSAGELSQ-F 258
|
250 260
....*....|....*....|..
gi 495163667 284 VFCAL---AAFEALAPVGGAFQ 302
Cdd:cd18575 259 VFYAVlaaGSVGALSEVWGDLQ 280
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
355-569 |
1.82e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.65 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 355 ALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDG-VSITGYrEAALRATMSVVpqrvhlfsatlrDN 433
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAI-SAGLSGQLTGI------------EN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 434 -----LLLAAPQADDAALgavlarvgLEKLLDDEGLNAWLGEGGRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAE 508
Cdd:PRK13546 106 iefkmLCMGFKRKEIKAM--------TPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495163667 509 TERQILALVKEVAVQ-KTLLMVTHRLQGLTAF-DRIIVMDNGQITEQGSHKELLAQqgrYYQF 569
Cdd:PRK13546 178 FAQKCLDKIYEFKEQnKTIFFVSHNLGQVRQFcTKIAWIEGGKLKDYGELDDVLPK---YEAF 237
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
339-508 |
2.92e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.17 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 339 LSLRNVSFSYPgqpQPALRDITLDVAPGEHIAILGRTGCGKSTLLQLITRAWDPTSGDVMLDGVSITGYREAALRATMSV 418
Cdd:PRK13541 2 LSLHQLQFNIE---QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 419 VPQRVHLfsaTLRDNLLLAAPQADDAALgaVLARVGLEKLLDdeglnaWLGEGGRQLSGGELRRLGIARALLHNAPMLLL 498
Cdd:PRK13541 79 LGLKLEM---TVFENLKFWSEIYNSAET--LYAAIHYFKLHD------LLDEKCYSLSSGMQKIVAIARLIACQSDLWLL 147
|
170
....*....|
gi 495163667 499 DEPTEGLDAE 508
Cdd:PRK13541 148 DEVETNLSKE 157
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
95-314 |
3.52e-04 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 42.77 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 95 LRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLY---LR--VISPLIGALAVIAVVTLglsllDVTLALTLGGI 169
Cdd:cd18548 74 LRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVmmlLRmlVRAPIMLIGAIIMAFRI-----NPKLALILLVA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 170 MLATLLLLPPLFYRAG---RPVGEALTMLRASYRQQLTGwlqgqaelsI-----FGAAGRYREQLDTTEQVWHEAQRRQA 241
Cdd:cd18548 149 IPILALVVFLIMKKAIplfKKVQKKLDRLNRVVRENLTG---------IrviraFNREDYEEERFDKANDDLTDTSLKAG 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495163667 242 GLTALSQAMMTLISGMTVVLILWMAAGGV-GGNSTPGSLIALFVFCALAAFeALAPVGGAFQHLGQVIASARRV 314
Cdd:cd18548 220 RLMALLNPLMMLIMNLAIVAILWFGGHLInAGSLQVGDLVAFINYLMQILM-SLMMLSMVFVMLPRASASAKRI 292
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
328-575 |
3.60e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 328 ESGKDAPREASLSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQ-LITRAWD--PTSGDVMLDGVSI 404
Cdd:PLN03073 167 DGNGGGPAIKDIHMENFSISVGGRD--LIVDASVTLAFGRHYGLVGRNGTGKTTFLRyMAMHAIDgiPKNCQILHVEQEV 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 405 TGYREAALRATMSVVPQRVHLfsatLRDNLLLAAPQADDAALGAVLARVGLEKLLDD---------------EGLNAWLG 469
Cdd:PLN03073 245 VGDDTTALQCVLNTDIERTQL----LEEEAQLVAQQRELEFETETGKGKGANKDGVDkdavsqrleeiykrlELIDAYTA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 470 EG-------------------GRQLSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETerqILALVKE-VAVQKTLLMV 529
Cdd:PLN03073 321 EAraasilaglsftpemqvkaTKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYlLKWPKTFIVV 397
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 495163667 530 THRLQGLTAFDRIIVMDNGQiteqgshkELLAQQGRYYQF-RARSVH 575
Cdd:PLN03073 398 SHAREFLNTVVTDILHLHGQ--------KLVTYKGDYDTFeRTREEQ 436
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
18-269 |
6.80e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 41.70 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 18 LSLGVVLAIVTLLASIGLLTLSGWFL-SASAVVGMAGLYsfnymLPAAGVRGAAIIRTAGRYFERLVSHEGTFRVLEHLR 96
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIdGPIAHGDRSALW-----PLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 97 VYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLdHLYLRVISPLIGALAVIAVVTLGLSLLDVTLALtlggIMLATLLL 176
Cdd:cd18543 76 TDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLGNLLTLVVGLVVMLVLSPPLAL----VALASLPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 177 LPPLFYRAGRpvgealTMLRASYR-QQLTGWLQGQAELSI--------FGAAGRYREQLDTTEQVWHEAQRRQAGLTALS 247
Cdd:cd18543 151 LVLVARRFRR------RYFPASRRaQDQAGDLATVVEESVtgirvvkaFGRERRELDRFEAAARRLRATRLRAARLRARF 224
|
250 260
....*....|....*....|....*.
gi 495163667 248 QAMMTLISGMTVVLIL----WMAAGG 269
Cdd:cd18543 225 WPLLEALPELGLAAVLalggWLVANG 250
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
457-559 |
9.55e-04 |
|
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: 42.31 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 457 KLLDDEGLN-AWLGEGGRQLSGGELRRLGIARALLHNA---PMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTH 531
Cdd:TIGR00630 811 QTLCDVGLGyIRLGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgNTVVVIEH 890
|
90 100 110
....*....|....*....|....*....|....
gi 495163667 532 RLQGLTAFDRIIVM------DNGQITEQGSHKEL 559
Cdd:TIGR00630 891 NLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
356-545 |
1.77e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 356 LRDITLDVAPGEHIAILGRTGCGKSTLlqlitrAWDptsgdvmldgvsiTGYREAALRATMSVVP---QRVHLFSATLRD 432
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL------AFD-------------TIYAEGQRRYVESLSAyarQFLGQMDKPDVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 433 NLLLAAP----------QADDAALGAV----------LARVGLE---KLLDDEGLNAW-LGEGGRQLSGGELRRLGIARA 488
Cdd:cd03270 72 SIEGLSPaiaidqkttsRNPRSTVGTVteiydylrllFARVGIRerlGFLVDVGLGYLtLSRSAPTLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 489 LLHNAPMLL--LDEPTEGL-DAETERQILALVKEVAVQKTLLMVTHRLQGLTAFDRIIVM 545
Cdd:cd03270 152 IGSGLTGVLyvLDEPSIGLhPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
468-543 |
1.80e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 40.29 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 468 LGEGGRQLSGGELRRLGIARALLHNAP---MLLLDEPTEGLDAETERQIL-ALVKEVAVQKTLLMVTHRLQGLTAFDRII 543
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLeVLQRLVDKGNTVVVIEHNLDVIKCADWII 242
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
448-561 |
2.03e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 448 AVLARVGLEKLLDDEGLNAwlgeggrqLSGGELRRLGIARALLHN--APMLLLDEPTEGLDAETERQILALVKEVAVQ-K 524
Cdd:PRK00635 458 SILIDLGLPYLTPERALAT--------LSGGEQERTALAKHLGAEliGITYILDEPSIGLHPQDTHKLINVIKKLRDQgN 529
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 495163667 525 TLLMVTHRLQGLTAFDRIIVMD------NGQITEQGSHKELLA 561
Cdd:PRK00635 530 TVLLVEHDEQMISLADRIIDIGpgagifGGEVLFNGSPREFLA 572
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
475-551 |
2.48e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 475 LSGGELRRLGIARALLHNAPMLLLDEPTEGLDAETERQILALVKEVAVQ-KTLLMVTHRLQ---GLTafDRIIVMDNGQI 550
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEgKGVIVISSELPellGMC--DRIYVMNEGRI 482
|
.
gi 495163667 551 T 551
Cdd:NF040905 483 T 483
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
63-282 |
5.32e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 39.00 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 63 AAGVRGAAIIRTAGRYFERLVSHEGTFRVLEHLRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDHLYLRVISPLI 142
Cdd:cd18550 42 ALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 143 GALAVIAVVTLGLSLLDVTLALtLGGIMLAtllllppLFYRAGRPVGEALTMLRASyRQQLTGWLQGQAE--LSIFGAA- 219
Cdd:cd18550 122 SNVVTLVATLVAMLALDWRLAL-LSLVLLP-------LFVLPTRRVGRRRRKLTRE-QQEKLAELNSIMQetLSVSGALl 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495163667 220 ----GRYREQLDTTEQVWHE---AQRRQAGLTALSQAMMTLISGMTVVLILWMAAGGVGGNS-TPGSLIAL 282
Cdd:cd18550 193 vklfGREDDEAARFARRSRElrdLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGlTIGTLVAF 263
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
470-540 |
5.52e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 470 EGGRQLSGGELR------RLGIARALLHNAPMLLLDEPTEGLDaETERQILALVKEVAVQKT-----LLMVTHRLQGLTA 538
Cdd:PRK01156 797 EGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLD-EDRRTNLKDIIEYSLKDSsdipqVIMISHHRELLSV 875
|
..
gi 495163667 539 FD 540
Cdd:PRK01156 876 AD 877
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|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
25-151 |
5.58e-03 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 38.93 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 25 AIVTLLASIGLLTLSGWFLS---ASAVVGMAGLYSFnyMLPAAGVRGAAIIRTAGRYFERLVSHEGTFRVLEHLRVYTFS 101
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLAriiAGVFLEGAGLAAL--LPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLA 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 495163667 102 RLLPLSPSGLARFRQGELLNRLVADVDTLD--------HLYLRVISPLIgALAVIAVV 151
Cdd:cd18584 79 RLLALGPALLRRQSSGELATLLTEGVDALDgyfarylpQLVLAAIVPLL-ILVAVFPL 135
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|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
339-401 |
6.88e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 38.62 E-value: 6.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495163667 339 LSLRNVSFSYPGQPqpALRDITLDVAPGEHIAILGRTGCGKSTLLQLIT--RAWDPTSGDVMLDG 401
Cdd:PRK09580 2 LSIKDLHVSVEDKA--ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKG 64
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|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
68-284 |
8.23e-03 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 38.55 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 68 GAAIIRTAGRYFERLVSHeGTFRVLEH-LRVYTFSRLLPLSPSGLARFRQGELLNRLVADVDTLDhlylRVISPliGALA 146
Cdd:cd18541 48 LLALLIGIFRFLWRYLIF-GASRRIEYdLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVR----MALGP--GILY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495163667 147 VI-AVVTLGLSL-----LDVTLALtlggIMLATLLLLPPLFYRAGRpvgealtMLRASYRQ------QLTGWLQ----GQ 210
Cdd:cd18541 121 LVdALFLGVLVLvmmftISPKLTL----IALLPLPLLALLVYRLGK-------KIHKRFRKvqeafsDLSDRVQesfsGI 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495163667 211 AELSIFGAAGRYREQLDTTEQVWHEAQRRQAGLTALSQAMMTLISGMTVVLILWMaaGG---VGGNSTPGSLIALFV 284
Cdd:cd18541 190 RVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWY--GGrlvIRGTITLGDLVAFNS 264
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
368-405 |
8.88e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.44 E-value: 8.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 495163667 368 HIAILGRTGCGKSTLLQLITRAW-----------DPTSGDVMLDGVSIT 405
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKaivsdypgttrDPNEGRLELKGKQII 49
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