|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-527 |
1.94e-146 |
|
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: 432.64 E-value: 1.94e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 2 KKLTKMVLSYKLYPTLMLIMSVFLSFTVVAQNISISHFLNHLLYYQQQSLLLLLSVI--FISLILRATFNMLIQFLGDHL 79
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGllLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 80 AFKVKHMLREQVILK---------KSVRSiGEEINILTESIDGIGPFFQSYLPQVFKSMLIPIVIIITMCFVHLPTAIIM 150
Cdd:COG4988 86 AARVKRRLRRRLLEKllalgpawlRGKST-GELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 151 IVTAPFIPLFYVIFGLKTRDESKDQMTYLNQFSQRFLNTAKGLITFKLLNQTKQSEQQLYKDSTRFRDLTMRILKSAFLS 230
Cdd:COG4988 165 LVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 231 GLMLEFISMLGIGLVALEAALSLvVFNHINFVTAAIAIILAPEFYNAIKDLGQAFHTGKQSEGASDVVFSFLESEDKADS 310
Cdd:COG4988 245 SAVLEFFASLSIALVAVYIGFRL-LGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 311 P-TLKVDEQQFEQVLIKHVDFQYANSNHmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL- 388
Cdd:COG4988 324 AgTAPLPAAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLs 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 389 ---------NIGFLSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRI 459
Cdd:COG4988 403 dldpaswrrQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRL 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386603 460 ELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLI 527
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIV 550
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
57-513 |
3.24e-112 |
|
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: 343.88 E-value: 3.24e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 57 VIFISLILRATFNMLIQFLGDHLAFKVKHMLREQVILK--------KSVRSIGEEINILTESIDGIGPFFQSYLPQVFKS 128
Cdd:TIGR02857 49 ALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAvaalgprwLQGRPSGELATLALEGVEALDGYFARYLPQLVLA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 129 MLIPIVIIITMCFVHLPTAIIMIVTAPFIPLFYVIFGLKTRDESKDQMTYLNQFSQRFLNTAKGLITFKLLNQTKQSEQQ 208
Cdd:TIGR02857 129 VIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 209 LYKDSTRFRDLTMRILKSAFLSGLMLEFISMLGIGLVALEAALSLvVFNHINFVTAAIAIILAPEFYNAIKDLGQAFHTG 288
Cdd:TIGR02857 209 IRRSSEEYRERTMRVLRIAFLSSAVLELFATLSVALVAVYIGFRL-LAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHAR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 289 KQSEGASDVVFSFLESEDKADSPTLKVDEQQFEQVLIKHVDFQYANSNHmALKNISFSVNKGEKVAIVGPSGAGKSTLAK 368
Cdd:TIGR02857 288 ADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLN 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 369 LLSQSVTPTHGTLSFNQASL----------NIGFLSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKY 438
Cdd:TIGR02857 367 LLLGFVDPTEGSIAVNGVPLadadadswrdQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQ 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488386603 439 GIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIR 513
Cdd:TIGR02857 447 GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA 521
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-527 |
3.42e-94 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 298.62 E-value: 3.42e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 1 MKKLTKMVLSYKLYPTLMLIMSVFLSFTVVAQNISISHFLNHLLYYQQQSLLLLLSVIFISL-ILRATFNMLIQFLGDHL 79
Cdd:COG1132 9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLaLLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 80 AFKVKHMLREQV---ILKKSV-----RSIGEEINILTESIDGIGPFFQSYLPQVFKSMLIPIVIIITMCFVHLPTAIIMI 151
Cdd:COG1132 89 AQRVVADLRRDLfehLLRLPLsffdrRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 152 VTAPFIPLFYVIFGLKTRDESKDQMTYLNQFSQRFLNTAKGLITFKLLNQTKQSEQQLYKDSTRFRDLTMRILKSAFLSG 231
Cdd:COG1132 169 LVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 232 LMLEFISMLGIGLVALeAALSLVVFNHINFVTAAIAIILAPEFYNAIKDLGQAFHTGKQSEGASDVVFSFLESE----DK 307
Cdd:COG1132 249 PLMELLGNLGLALVLL-VGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPpeipDP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 308 ADSPTLKVDEQQFEqvlIKHVDFQYaNSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTL------ 381
Cdd:COG1132 328 PGAVPLPPVRGEIE---FENVSFSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvd 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 382 --SFNQASL--NIGFLSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMR 457
Cdd:COG1132 404 irDLTLESLrrQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQ 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386603 458 RIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRsSARRIY-IESGHLI 527
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIR-NADRILvLDDGRIV 553
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-508 |
4.81e-77 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 254.00 E-value: 4.81e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 29 VVAQNISISHFLNHllyyqqqslllllsviFISLILRATFNMLIQFLGDHLAFK----VKHMLREQV-----------IL 93
Cdd:PRK11174 52 LIIENIPREALLPP----------------FILLILLFVLRALLAWLRERVGFKagqhIRQQIRQQVldklqqlgpawIQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 94 KKSVRSIgeeINILTESIDGIGPFFQSYLPQVFKSMLIPIVIIITMCFVHLPTAIIMIVTAPFIPLFYVIFGLKTRDESK 173
Cdd:PRK11174 116 GKPAGSW---ATLVLEQVEDMHDFYARYLPQMALAVLVPLLILIAVFPINWAAGLILLGTAPLIPLFMALVGMGAADANR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 174 DQMTYLNQFSQRFLNTAKGLITFKLLNQTKQSEQQLYKDSTRFRDLTMRILKSAFLSGLMLEFISMLGIGLVAleaalsl 253
Cdd:PRK11174 193 RNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLSSAVLEFFASISIALVA------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 254 VVF-----NHINF------VTAAI---AIILAPEFYNAIKDLGQAFHTGKQSEGASDVVFSFLESEDkADSPTLKVDEQQ 319
Cdd:PRK11174 266 VYFgfsylGELNFghygtgVTLFAgffVLILAPEFYQPLRDLGTFYHAKAQAVGAAESLVTFLETPL-AHPQQGEKELAS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 320 FEQVLIKHVDFQ-YANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSqSVTPTHGTLSFNQASLN--------- 389
Cdd:PRK11174 345 NDPVTIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL-GFLPYQGSLKINGIELReldpeswrk 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 -IGFLSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLK 468
Cdd:PRK11174 424 hLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQP 503
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 488386603 469 PDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHR 508
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQ 543
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
57-529 |
1.29e-75 |
|
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: 253.22 E-value: 1.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 57 VIFISLILRATFNMLIQFLGDHLAFKV---------KHMLReqviLKKS---VRSIGEEINILTEsIDGIGPFFQSYLPQ 124
Cdd:COG2274 201 GLLLALLFEGLLRLLRSYLLLRLGQRIdlrlssrffRHLLR----LPLSffeSRSVGDLASRFRD-VESIREFLTGSLLT 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 125 VFKSMLIPIVIIITMCFVHLPTAIIMIVTAPFIPLFYVIFGLKTRDESKDQMTYLNQFSQRFLNTAKGLITFKLLNQTKQ 204
Cdd:COG2274 276 ALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESR 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 205 SEQQLYKDSTRFRDLTMRILKSAFLSGLMLEFISMLG-IGLVALEAalSLVVFNHINfVTAAIAI-ILAPEFYNAIKDLG 282
Cdd:COG2274 356 FRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLAtVALLWLGA--YLVIDGQLT-LGQLIAFnILSGRFLAPVAQLI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 283 QAFHTGKQSEGASDVVFSFLESEDKADSPTLKVDEQQFE-QVLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGA 361
Cdd:COG2274 433 GLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKgDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 362 GKSTLAKLLSQSVTPTHGTLSFNQASL----------NIGFLSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKE 431
Cdd:COG2274 513 GKSTLLKLLLGLYEPTSGRILIDGIDLrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHD 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 432 KVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDST 511
Cdd:COG2274 593 FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLST 672
|
490
....*....|....*...
gi 488386603 512 IRSSARRIYIESGHLIKD 529
Cdd:COG2274 673 IRLADRIIVLDKGRIVED 690
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
20-296 |
7.41e-73 |
|
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: 233.84 E-value: 7.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 20 IMSVFLSFTVVAQNISISHFLNHLLYYQQQSLLLLLSVI--FISLILRATFNMLIQFLGDHLAFKVKHMLREQVI----- 92
Cdd:cd18584 3 LLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLllLAALLLRALLAWAQERLAARAAARVKAELRRRLLarlla 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 93 ---LKKSVRSIGEEINILTESIDGIGPFFQSYLPQVFKSMLIPIVIIITMCFVHLPTAIIMIVTAPFIPLFYVIFGLKTR 169
Cdd:cd18584 83 lgpALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKAAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 170 DESKDQMTYLNQFSQRFLNTAKGLITFKLLNQTKQSEQQLYKDSTRFRDLTMRILKSAFLSGLMLEFISMLGIGLVALEA 249
Cdd:cd18584 163 AASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAVYI 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 488386603 250 ALSLvVFNHINFVTAAIAIILAPEFYNAIKDLGQAFHTGKQSEGASD 296
Cdd:cd18584 243 GFRL-LGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAE 288
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
133-531 |
5.73e-71 |
|
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: 237.36 E-value: 5.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 133 IVIIITMCFVHLPTAII----MIVTAPFIPLFyviFGLKTRDESKDQMTYLNQFSQRFLNTAKGLITFKLLNQTKQSEQQ 208
Cdd:COG4987 144 LAAVAFLAFFSPALALVlalgLLLAGLLLPLL---AARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALAR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 209 LYKDSTRFRDLTMRILKSAFLSGLMLEFISMLGIGLVALeAALSLVVFNHINFVTAAiAIILAP----EfynAIKDLGQA 284
Cdd:COG4987 221 LDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLW-LAAPLVAAGALSGPLLA-LLVLAAlalfE---ALAPLPAA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 285 FHTGKQSEGASDVVFSFLESEDKADSPTLKVDEQQFEQVLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKS 364
Cdd:COG4987 296 AQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKS 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 365 TLAKLLSQSVTPTHGTLSFNQASL----------NIGFLSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVL 434
Cdd:COG4987 376 TLLALLLRFLDPQSGSITLGGVDLrdldeddlrrRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLA 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 435 SLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRS 514
Cdd:COG4987 456 ALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLER 535
|
410
....*....|....*..
gi 488386603 515 SARRIYIESGHLIKDDS 531
Cdd:COG4987 536 MDRILVLEDGRIVEQGT 552
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
325-525 |
1.04e-53 |
|
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: 179.50 E-value: 1.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------NIGFLS 394
Cdd:cd03228 3 FKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLrdldleslrkNIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 395 QRPHIFADSIKNNIamyddeicdeqviqvldevglkekvlslkygiytsigeggemLSGGQMRRIELSRLLLLKPDIVIF 474
Cdd:cd03228 83 QDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488386603 475 DEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGH 525
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
323-527 |
3.07e-51 |
|
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: 175.11 E-value: 3.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 323 VLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQ--------ASL--NIGF 392
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlASLrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 393 LSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIV 472
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488386603 473 IFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLI 527
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIV 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
197-527 |
1.69e-50 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 182.33 E-value: 1.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 197 KLLNQTKQSEQQLYKDSTRFRDLT-----MRILKSAFLSGLMLeFISMLGIGLVALEAAL-SLVVFnhinfvtAAIAI-- 268
Cdd:PRK11160 221 RYRQQLEQTEQQWLAAQRRQANLTglsqaLMILANGLTVVLML-WLAAGGVGGNAQPGALiALFVF-------AALAAfe 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 269 ILAPefynaikdLGQAF-HTGKQSEGA----------SDVVFSfLESEDKADSPTLKvdeqqfeqvlIKHVDFQYANSNH 337
Cdd:PRK11160 293 ALMP--------VAGAFqHLGQVIASArrineiteqkPEVTFP-TTSTAAADQVSLT----------LNNVSFTYPDQPQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 338 MALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFLSQRPHIFADSIKNN 407
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdyseaalrqaISVVSQRVHLFSATLRDN 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 408 IAMYDDEICDEQVIQVLDEVGLkEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEK 487
Cdd:PRK11160 434 LLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETER 512
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 488386603 488 VIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLI 527
Cdd:PRK11160 513 QILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQII 552
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
325-527 |
3.03e-48 |
|
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: 167.02 E-value: 3.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYaNSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTL--------SFNQASL--NIGFLS 394
Cdd:cd03254 5 FENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirDISRKSLrsMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 395 QRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIF 474
Cdd:cd03254 84 QDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488386603 475 DEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLI 527
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKII 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
323-527 |
4.75e-46 |
|
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: 161.55 E-value: 4.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 323 VLIKHVDFQYAN-SNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IG 391
Cdd:cd03249 1 IEFKNVSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlnlrwlrsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 392 FLSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDI 471
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 472 VIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLI 527
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVV 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
326-529 |
2.06e-44 |
|
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: 156.60 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 326 KHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------NIGFLSQ 395
Cdd:cd03245 6 RNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrqldpadlrrNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 396 RPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFD 475
Cdd:cd03245 86 DVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488386603 476 EPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKD 529
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
322-531 |
9.63e-44 |
|
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: 154.57 E-value: 9.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 322 QVLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IG 391
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkiglhdlrsrIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 392 FLSQRPHIFADSIKNNIAMYDdEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDI 471
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 472 VIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDS 531
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
326-527 |
3.93e-43 |
|
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: 153.54 E-value: 3.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 326 KHVDFQYaNSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN--------QASL--NIGFLSQ 395
Cdd:cd03253 4 ENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdirevtLDSLrrAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 396 RPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFD 475
Cdd:cd03253 83 DTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488386603 476 EPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLI 527
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
63-508 |
3.47e-42 |
|
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: 158.68 E-value: 3.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 63 ILRATFNMLIQFLGDHLAFKVKHMLREQVILKKSVRSI--------GEEINILTESIDGIgpffQSYLPQVFKSMLIPIV 134
Cdd:TIGR02868 64 IGRAVFRYLERLVGHDAALRSLGALRVRVYERLARQALagrrrlrrGDLLGRLGADVDAL----QDLYVRVIVPAGVALV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 135 IIITMC----FVHLPTAIIMIVTApFIPLFYV--IFGLKTRDESKDQMTYLNQFSQRFLNTAKG---LITFKLLNQTKQS 205
Cdd:TIGR02868 140 VGAAAVaaiaVLSVPAALILAAGL-LLAGFVAplVSLRAARAAEQALARLRGELAAQLTDALDGaaeLVASGALPAALAQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 206 EQQLYKDSTRFRDltmrilKSAFLSGLMlEFISMLGIGLV---ALEAALSLVVFNHINFVTAAIAIILAPEFYNAIKDLG 282
Cdd:TIGR02868 219 VEEADRELTRAER------RAAAATALG-AALTLLAAGLAvlgALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALP 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 283 QAFHTGKQSEGASDVVFSFLESE---DKADSPTLKVDEQQFEQVLIKHVDFQYANSNhMALKNISFSVNKGEKVAIVGPS 359
Cdd:TIGR02868 292 AAAQQLTRVRAAAERIVEVLDAAgpvAEGSAPAAGAVGLGKPTLELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPS 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 360 GAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFLSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGL 429
Cdd:TIGR02868 371 GSGKSTLLATLAGLLDPLQGEVTLDGVPVSsldqdevrrrVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 430 KEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKviqQVLEHHFSTT---TVFIIA 506
Cdd:TIGR02868 451 ADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETAD---ELLEDLLAALsgrTVVLIT 527
|
..
gi 488386603 507 HR 508
Cdd:TIGR02868 528 HH 529
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
326-529 |
2.14e-41 |
|
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: 158.49 E-value: 2.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 326 KHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------NIGFLSQ 395
Cdd:TIGR03375 467 RNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIrqidpadlrrNIGYVPQ 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 396 RPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFD 475
Cdd:TIGR03375 547 DPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLD 626
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488386603 476 EPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKD 529
Cdd:TIGR03375 627 EPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVAD 680
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
128-527 |
4.52e-40 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 153.25 E-value: 4.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 128 SMLIPIV----IIITMCFVHLPT----AIIMIVTAPFIPLFYVIFGLKTRDESK---DQMTYLNQFSQRFLNTAKGLITF 196
Cdd:PRK11176 141 GALITVVregaSIIGLFIMMFYYswqlSLILIVIAPIVSIAIRVVSKRFRNISKnmqNTMGQVTTSAEQMLKGHKEVLIF 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 197 kllNQTKQSEQQLYKDSTRFRDLTMRILKSAFLSGLMLEFISMLGIGLVALEAALSLVVFN----HINFVTAAIAIILAP 272
Cdd:PRK11176 221 ---GGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTltagTITVVFSSMIALMRP 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 273 efYNAIKDLGQAFHTGKqseGASDVVFSFLESEDKADSPTLKVDEQQFEqVLIKHVDFQYANSNHMALKNISFSVNKGEK 352
Cdd:PRK11176 298 --LKSLTNVNAQFQRGM---AACQTLFAILDLEQEKDEGKRVIERAKGD-IEFRNVTFTYPGKEVPALRNINFKIPAGKT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 353 VAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------NIGFLSQRPHIFADSIKNNIAmY--DDEICDEQV 420
Cdd:PRK11176 372 VALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdytlaslrnQVALVSQNVHLFNDTIANNIA-YarTEQYSREQI 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 421 IQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTT 500
Cdd:PRK11176 451 EEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR 530
|
410 420
....*....|....*....|....*..
gi 488386603 501 TVFIIAHRDSTIRSSARRIYIESGHLI 527
Cdd:PRK11176 531 TSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
323-531 |
9.88e-40 |
|
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: 144.55 E-value: 9.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 323 VLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHG----------TLSFNQASLNIGF 392
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghdlaLADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 393 LSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIV 472
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488386603 473 IFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDS 531
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGS 219
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
227-521 |
1.81e-39 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 150.96 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 227 AFLSGLMLEFISMLGIGLVALEAALslVVFNHI---NFVTAAIAI--ILAPeFYNAIKDLGQaFHTGKQSEGASDVVFSF 301
Cdd:TIGR01842 225 GMLSNLSKYFRIVLQSLVLGLGAYL--AIDGEItpgMMIAGSILVgrALAP-IDGAIGGWKQ-FSGARQAYKRLNELLAN 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 302 LESEDkadsPTLKVDEQQFEqVLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTL 381
Cdd:TIGR01842 301 YPSRD----PAMPLPEPEGH-LSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 382 SFNQASLN----------IGFLSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEML 451
Cdd:TIGR01842 376 RLDGADLKqwdretfgkhIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATL 455
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386603 452 SGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEH-HFSTTTVFIIAHRDSTIrSSARRIYI 521
Cdd:TIGR01842 456 SGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAlKARGITVVVITHRPSLL-GCVDKILV 525
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
303-527 |
7.52e-38 |
|
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: 147.27 E-value: 7.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 303 ESEDKADSPTLKVD--EQQFEqvlikHVDFQYaNSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGT 380
Cdd:COG5265 341 EVADAPDAPPLVVGggEVRFE-----NVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 381 LSFN--------QASL--NIGFLSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEM 450
Cdd:COG5265 415 ILIDgqdirdvtQASLraAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLK 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 451 LSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLI 527
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIV 571
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
323-526 |
1.72e-37 |
|
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: 137.99 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 323 VLIKHVDFQYAN-SNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IG 391
Cdd:cd03248 12 VKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyehkylhskVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 392 FLSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDI 471
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488386603 472 VIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHL 526
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
328-514 |
3.64e-37 |
|
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: 144.89 E-value: 3.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 328 VDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------NIGFLSQRP 397
Cdd:COG4618 336 LTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwdreelgrHIGYLPQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 398 HIFADSIKNNIAMYDDeICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEP 477
Cdd:COG4618 416 ELFDGTIAENIARFGD-ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 488386603 478 AIGLDIETEKVIQQVLEHHFST-TTVFIIAHRDSTIRS 514
Cdd:COG4618 495 NSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAA 532
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
296-527 |
2.83e-36 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 142.41 E-value: 2.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 296 DVVFSFLESEDKADSPTLKvDEQQFEqvlikHVDFQYANSNHmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVT 375
Cdd:PRK13657 314 DAVPDVRDPPGAIDLGRVK-GAVEFD-----DVSFSYDNSRQ-GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 376 PTHGTL--------SFNQASL--NIGFLSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIG 445
Cdd:PRK13657 387 PQSGRIlidgtdirTVTRASLrrNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 446 EGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGH 525
Cdd:PRK13657 467 ERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGR 546
|
..
gi 488386603 526 LI 527
Cdd:PRK13657 547 VV 548
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
325-527 |
7.14e-36 |
|
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: 132.05 E-value: 7.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN---------IGFLSQ 395
Cdd:cd03247 3 INNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSdlekalsslISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 396 RPHIFADSIKNNIamyddeicdeqviqvldevglkekvlslkygiytsigegGEMLSGGQMRRIELSRLLLLKPDIVIFD 475
Cdd:cd03247 83 RPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488386603 476 EPAIGLDIETEkviQQVLEHHFSTT---TVFIIAHRDSTIRSSARRIYIESGHLI 527
Cdd:cd03247 124 EPTVGLDPITE---RQLLSLIFEVLkdkTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
130-524 |
4.52e-35 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 139.88 E-value: 4.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 130 LIPIVIIITMCFVHLPT-AIIMIVTAPFIPLFYVIFG--LKTRDESKDQMtylNQFSQRFLNTA-KGLITFKLLNQTKQS 205
Cdd:TIGR01846 263 LLFVVVFLAVMFFYSPTlTGVVIGSLVCYALLSVFVGpiLRKRVEDKFER---SAAATSFLVESvTGIETIKATATEPQF 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 206 EQQLYKDSTRFRDLTMRILKSAFLSGLMLEFISML--------GIGLVaLEAALS---LVVFNHI-NFVTAAIaIILApe 273
Cdd:TIGR01846 340 QNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLtfaillwfGAHLV-IGGALSpgqLVAFNMLaGRVTQPV-LRLA-- 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 274 fynaikDLGQAF-HTGKQSEGASDVVFSFLE--SEDKADSPTLKVDeqqfeqVLIKHVDFQYANSNHMALKNISFSVNKG 350
Cdd:TIGR01846 416 ------QLWQDFqQTGIALERLGDILNSPTEprSAGLAALPELRGA------ITFENIRFRYAPDSPEVLSNLNLDIKPG 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 351 EKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------NIGFLSQRPHIFADSIKNNIAMYDDEICDEQV 420
Cdd:TIGR01846 484 EFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLaiadpawlrrQMGVVLQENVLFSRSIRDNIALCNPGAPFEHV 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 421 IQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTT 500
Cdd:TIGR01846 564 IHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGR 643
|
410 420
....*....|....*....|....
gi 488386603 501 TVFIIAHRDSTIRSSARRIYIESG 524
Cdd:TIGR01846 644 TVIIIAHRLSTVRACDRIIVLEKG 667
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
273-528 |
1.11e-34 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 138.70 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 273 EFYNAIKDLGQAFHTGKQSEGASDVVFSFLESEDKADSPTLKVDEQQFEQVLIKHVDFQYAN-SNHMALKNISFSVNKGE 351
Cdd:TIGR00958 429 QLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNrPDVPVLKGLTFTLHPGE 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 352 KVAIVGPSGAGKSTLAKLLSQSVTPTHGTL--------SFNQASLN--IGFLSQRPHIFADSIKNNIAMYDDEICDEQVI 421
Cdd:TIGR00958 509 VVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgvplvQYDHHYLHrqVALVGQEPVLFSGSVRENIAYGLTDTPDEEIM 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 422 QVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEhhFSTTT 501
Cdd:TIGR00958 589 AAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRT 666
|
250 260
....*....|....*....|....*..
gi 488386603 502 VFIIAHRDSTIRSSARRIYIESGHLIK 528
Cdd:TIGR00958 667 VLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
340-477 |
1.43e-34 |
|
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: 127.38 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------NIGFLSQRPHIFAD-SIKNNI 408
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488386603 409 AM------YDDEICDEQVIQVLDEVGLKEKvlslkygIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEP 477
Cdd:pfam00005 81 RLglllkgLSKREKDARAEEALEKLGLGDL-------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
329-526 |
2.00e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.17 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 329 DFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFLSQRPH 398
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSampppewrrqVAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 399 IFADSIKNNIA----MYDDEICDEQVIQVLDEVGLKEKVLSlkygiyTSIGEggemLSGGQMRRIELSRLLLLKPDIVIF 474
Cdd:COG4619 85 LWGGTVRDNLPfpfqLRERKFDRERALELLERLGLPPDILD------KPVER----LSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 475 DEPAIGLDIET----EKVIQQVLEHHfsTTTVFIIAHRDSTI-RSSARRIYIESGHL 526
Cdd:COG4619 155 DEPTSALDPENtrrvEELLREYLAEE--GRAVLWVSHDPEQIeRVADRVLTLEAGRL 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
325-525 |
2.04e-34 |
|
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: 129.12 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN----------QASLNIGFLS 394
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdltklslkELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 395 QRPH--IFADSIK-------NNIAMYDDEIcDEQVIQVLDEVGLKEKvlsLKYGIYTsigeggemLSGGQMRRIELSRLL 465
Cdd:cd03225 82 QNPDdqFFGPTVEeevafglENLGLPEEEI-EERVEEALELVGLEGL---RDRSPFT--------LSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386603 466 LLKPDIVIFDEPAIGLDIETEKVIQQVLEH-HFSTTTVFIIAHRDSTIRSSA-RRIYIESGH 525
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELAdRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
325-531 |
9.51e-34 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 127.83 E-value: 9.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSnHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN----------QASLNIGFLS 394
Cdd:COG1122 3 LENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkditkknlrELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 395 QRPH--IFADSIKNNIA-------MYDDEIcDEQVIQVLDEVGLKEKvlsLKYGIYTsigeggemLSGGQMRRIELSRLL 465
Cdd:COG1122 82 QNPDdqLFAPTVEEDVAfgpenlgLPREEI-RERVEEALELVGLEHL---ADRPPHE--------LSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386603 466 LLKPDIVIFDEPAIGLDIE-TEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYI-ESGHLIKDDS 531
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRgRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVlDDGRIVADGT 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
325-524 |
1.66e-33 |
|
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: 125.41 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFLS 394
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwdpnelgdhVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 395 QRPHIFADSIKNNIamyddeicdeqviqvldevglkekvlslkygiytsigeggemLSGGQMRRIELSRLLLLKPDIVIF 474
Cdd:cd03246 83 QDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488386603 475 DEPAIGLDIETEKVIQQVLEH-HFSTTTVFIIAHRDSTIRSSARRIYIESG 524
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
323-524 |
6.49e-32 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 130.45 E-value: 6.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 323 VLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGF 392
Cdd:TIGR03796 478 VELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREeiprevlansVAM 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 393 LSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIV 472
Cdd:TIGR03796 558 VDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSIL 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488386603 473 IFDEPAIGLDIETEKVIQQVLEHHFSTTtvFIIAHRDSTIRSSARRIYIESG 524
Cdd:TIGR03796 638 ILDEATSALDPETEKIIDDNLRRRGCTC--IIVAHRLSTIRDCDEIIVLERG 687
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
325-512 |
2.16e-31 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 128.30 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYaNSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTL--------SFNQASL--NIGFLS 394
Cdd:PRK10790 343 IDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplsSLSHSVLrqGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 395 QRPHIFADSIKNNIAMYDDeICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIF 474
Cdd:PRK10790 422 QDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILIL 500
|
170 180 190
....*....|....*....|....*....|....*...
gi 488386603 475 DEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTI 512
Cdd:PRK10790 501 DEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTI 538
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
325-521 |
3.94e-31 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 128.15 E-value: 3.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQ---ASLNI-------GFLS 394
Cdd:TIGR03797 454 VDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGqdlAGLDVqavrrqlGVVL 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 395 QRPHIFADSIKNNIAMyDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIF 474
Cdd:TIGR03797 534 QNGRLMSGSIFENIAG-GAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLF 612
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488386603 475 DEPAIGLDIETEKVIQQVLEHHFSTTTVfiIAHRDSTIRsSARRIYI 521
Cdd:TIGR03797 613 DEATSALDNRTQAIVSESLERLKVTRIV--IAHRLSTIR-NADRIYV 656
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
319-531 |
1.26e-30 |
|
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: 118.67 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 319 QFEQVLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN--------- 389
Cdd:cd03369 3 EHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIStipledlrs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 -IGFLSQRPHIFADSIKNNIAMYDdEICDEQVIQVLdevglkekvlslkygiytSIGEGGEMLSGGQMRRIELSRLLLLK 468
Cdd:cd03369 83 sLTIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386603 469 PDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDS 531
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
325-526 |
4.21e-30 |
|
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: 117.21 E-value: 4.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANS--NHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-----------QASL--- 388
Cdd:cd03255 3 LKNLSKTYGGGgeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklsekeLAAFrrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 389 NIGFLSQRPHIFAD-SIKNNIAM------YDDEICDEQVIQVLDEVGLKEKvlslkygIYTSIGEggemLSGGQMRRIEL 461
Cdd:cd03255 83 HIGFVFQSFNLLPDlTALENVELplllagVPKKERRERAEELLERVGLGDR-------LNHYPSE----LSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 462 SRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLE--HHFSTTTVFIIAHRDSTIRSSARRIYIESGHL 526
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
325-532 |
1.28e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 116.32 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYanSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN---------QASLNIGFLSQ 395
Cdd:COG1131 3 VRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgedvardpaEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 396 RPHIFAD-SIKNNIAMY------DDEICDEQVIQVLDEVGLKEKvlslkygIYTSIGEggemLSGGQMRRIELSRLLLLK 468
Cdd:COG1131 81 EPALYPDlTVRENLRFFarlyglPRKEARERIDELLELFGLTDA-------ADRKVGT----LSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 469 PDIVIFDEPAIGLDIETEKVIQQVLEHHFST-TTVFIIAHRDSTIRSSARRI-YIESGHLIKDDSI 532
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVaIIDKGRIVADGTP 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
325-530 |
1.64e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.92 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANsNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL-------------NIG 391
Cdd:COG2884 4 FENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlkrreipylrrRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 392 FlsqrphIFAD-------SIKNNIAM------YDDEICDEQVIQVLDEVGLKEKVLSLKygiytsigeggEMLSGGQMRR 458
Cdd:COG2884 83 V------VFQDfrllpdrTVYENVALplrvtgKSRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386603 459 IELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEH-HFSTTTVFIIAHRDSTIRSS-ARRIYIESGHLIKDD 530
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEiNRRGTTVLIATHDLELVDRMpKRVLELEDGRLVRDE 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
323-524 |
2.13e-29 |
|
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: 114.87 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 323 VLIKHVDFQY---ANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNqasLNIGFLSQRPHI 399
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP---GSIAYVSQEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 400 FADSIKNNIAM---YDDEICDEqviqVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDE 476
Cdd:cd03250 78 QNGTIRENILFgkpFDEERYEK----VIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488386603 477 PAIGLDIET-----EKVIQQVLEHHfstTTVFIIAHRDSTIRSSARRIYIESG 524
Cdd:cd03250 154 PLSAVDAHVgrhifENCILGLLLNN---KTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
325-507 |
4.26e-29 |
|
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: 114.55 E-value: 4.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYanSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-----QASLNIGFLSQRPHI 399
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkpleKERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 400 ---FADSIKNNIAM----------YDDEICDEQVIQVLDEVGLKEKVLSlkygiytSIGEggemLSGGQMRRIELSRLLL 466
Cdd:cd03235 80 drdFPISVRDVVLMglyghkglfrRLSKADKAKVDEALERVGLSELADR-------QIGE----LSGGQQQRVLLARALV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488386603 467 LKPDIVIFDEPAIGLDIETEKVIQQVLEH-HFSTTTVFIIAH 507
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTH 190
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
325-540 |
9.32e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.42 E-value: 9.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYanSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-----QASLNIGFLSQRPHI 399
Cdd:COG1121 9 LENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFgkpprRARRRIGYVPQRAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 400 FAD---SIKNNIAMY--------------DDEICDEqviqVLDEVGLKEKvlslkygIYTSIGEggemLSGGQMRRIELS 462
Cdd:COG1121 87 DWDfpiTVRDVVLMGrygrrglfrrpsraDREAVDE----ALERVGLEDL-------ADRPIGE----LSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386603 463 RLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEH-HFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDSIISVTRSEV 540
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPEN 230
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
322-528 |
1.04e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 120.20 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 322 QVLIKHvdFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------NIG 391
Cdd:PRK10789 315 DVNIRQ--FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtklqldswrsRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 392 FLSQRPHIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDI 471
Cdd:PRK10789 393 VVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 472 VIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIK 528
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
323-504 |
1.23e-28 |
|
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: 113.34 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 323 VLIKHVDFQYANSN--HMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN-----IGFLSQ 395
Cdd:cd03293 1 LEVRNVSKTYGGGGgaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTgpgpdRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 396 RPHIFA-DSIKNNIA-------MYDDEIcDEQVIQVLDEVGLKEkvlSLKYgiYTSigeggeMLSGGQMRRIELSRLLLL 467
Cdd:cd03293 81 QDALLPwLTVLDNVAlglelqgVPKAEA-RERAEELLELVGLSG---FENA--YPH------QLSGGMRQRVALARALAV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488386603 468 KPDIVIFDEPAIGLDIETEKVIQQVLE---HHFSTTTVFI 504
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLdiwRETGKTVLLV 188
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
325-531 |
1.06e-27 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 112.16 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYA---NSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN------------ 389
Cdd:TIGR04521 3 LKNVSYIYQpgtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkklkdlrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 -IGFLSQRP--HIFADSIKNNIA-------MYDDEIcDEQVIQVLDEVGLKEKVLSLkygiytSIGEggemLSGGQMRRI 459
Cdd:TIGR04521 83 kVGLVFQFPehQLFEETVYKDIAfgpknlgLSEEEA-EERVKEALELVGLDEEYLER------SPFE----LSGGQMRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488386603 460 ELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLE--HHFSTTTVFIIAHRDSTIRSSARRIYI-ESGHLIKDDS 531
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKrlHKEKGLTVILVTHSMEDVAEYADRVIVmHKGKIVLDGT 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
325-521 |
1.29e-27 |
|
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: 108.49 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNhmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIGFLSQRphifadsi 404
Cdd:cd00267 2 IENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 405 KNNIAMyddeicdeqVIQvldevglkekvlslkygiytsigeggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIE 484
Cdd:cd00267 72 RRRIGY---------VPQ----------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190
....*....|....*....|....*....|....*...
gi 488386603 485 T-EKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYI 521
Cdd:cd00267 115 SrERLLELLRELAEEGRTVIIVTHDPELAELAADRVIV 152
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
339-529 |
2.54e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 109.75 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL--------------NIGFLSQRPHIFAD-S 403
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslserelarlrrrHIGFVFQFFNLLPElT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 404 IKNNIAM------YDDEICDEQVIQVLDEVGLKEKvlslkygIYTSIGEggemLSGGQMRRIELSRLLLLKPDIVIFDEP 477
Cdd:COG1136 103 ALENVALplllagVSRKERRERARELLERVGLGDR-------LDHRPSQ----LSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488386603 478 AIGLDIET-EKVIQQVLEHHFST-TTVFIIAHrDSTIRSSARRIY-IESGHLIKD 529
Cdd:COG1136 172 TGNLDSKTgEEVLELLRELNRELgTTIVMVTH-DPELAARADRVIrLRDGRIVSD 225
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
325-531 |
2.93e-27 |
|
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: 116.38 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYA-NSNhmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFL 393
Cdd:TIGR01193 476 INDVSYSYGyGSN--ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdidrhtlrqfINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 394 SQRPHIFADSIKNNIAMYDDE-ICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIV 472
Cdd:TIGR01193 554 PQEPYIFSGSILENLLLGAKEnVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488386603 473 IFDEPAIGLDIETEKVIQQVLEHHFSTTTVFiIAHRDSTIRSSARRIYIESGHLIKDDS 531
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQDKTIIF-VAHRLSVAKQSDKIIVLDHGKIIEQGS 691
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
63-296 |
6.57e-27 |
|
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: 110.45 E-value: 6.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 63 ILRATFNMLIQFLGDHLAFKVKHMLREQVILK--------KSVRSIGEEINILTESIDGIGPFFQSYLPQVFKSMLIPIV 134
Cdd:cd18561 47 VLRAALLWLRERVAHRAAQRVKQHLRRRLFAKllklgpgyLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 135 IIITMCFVHLPTAIIMIVTAPFIPLFYVIFGLKTRDESKDQMTYLNQFSQRFLNTAKGLITFKLLNQTKQSEQQLYKDST 214
Cdd:cd18561 127 ILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 215 RFRDLTMRILKSAFLSGLMLEFISMLGIGLVALEAALSLVVfNHINFVTAAIAIILAPEFYNAIKDLGQAFHTGKQSEGA 294
Cdd:cd18561 207 DLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLG-GQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISA 285
|
..
gi 488386603 295 SD 296
Cdd:cd18561 286 AD 287
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
340-532 |
7.52e-27 |
|
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: 108.74 E-value: 7.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL-------------NIGFLSQRPHIFAD-SIK 405
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglseaelyrlrrRMGMLFQSGALFDSlTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 406 NNIAM-------YDDEICDEQVIQVLDEVGLKEKVLSLKygiytsiGEggemLSGGQMRRIELSRLLLLKPDIVIFDEPA 478
Cdd:cd03261 96 ENVAFplrehtrLSEEEIREIVLEKLEAVGLRGAEDLYP-------AE----LSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 479 IGLD-IETEKVIQQVLEHHFST-TTVFIIAHRDSTIRSSARRIY-IESGHLIKDDSI 532
Cdd:cd03261 165 AGLDpIASGVIDDLIRSLKKELgLTSIMVTHDLDTAFAIADRIAvLYDGKIVAEGTP 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
340-522 |
9.13e-27 |
|
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: 107.56 E-value: 9.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL---------NIGFLSQRPHIFAD-SIKNNI- 408
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrdaredyrrRLAYLGHADGLKPElTVRENLr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 409 ---AMYDDEICDEQVIQVLDEVGLkEKVLSLKYGiytsigeggeMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIET 485
Cdd:COG4133 98 fwaALYGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 488386603 486 EKVIQQVLEHHFSTTTVFIIA-HRDSTIRsSARRIYIE 522
Cdd:COG4133 167 VALLAELIAAHLARGGAVLLTtHQPLELA-AARVLDLG 203
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
327-521 |
3.78e-26 |
|
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: 106.44 E-value: 3.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 327 HVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN-------------IGFL 393
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsrrlrkirrkeIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 394 SQRP-----------HIFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEKVLSlKYgiytsIGEggemLSGGQMRRIELS 462
Cdd:cd03257 88 FQDPmsslnprmtigEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLN-RY-----PHE----LSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386603 463 RLLLLKPDIVIFDEPAIGLDIETEKVIQQVL-----EHHfstTTVFIIAHRDSTIRSSARRIYI 521
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLkklqeELG---LTLLFITHDLGVVAKIADRVAV 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
325-508 |
8.28e-26 |
|
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: 110.76 E-value: 8.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSN---HMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL------------- 388
Cdd:COG1123 263 VRNLSKRYPVRGkggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklsrrslrelrr 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 389 NIGFLSQRP-----------HIFADSIKNNiAMYDDEICDEQVIQVLDEVGLKEKVLSlKYgiytsIGEggemLSGGQMR 457
Cdd:COG1123 343 RVQMVFQDPysslnprmtvgDIIAEPLRLH-GLLSRAERRERVAELLERVGLPPDLAD-RY-----PHE----LSGGQRQ 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 458 RIELSRLLLLKPDIVIFDEPAIGLDIeteKVIQQVLE------HHFSTTTVFI---------IAHR 508
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDV---SVQAQILNllrdlqRELGLTYLFIshdlavvryIADR 474
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
327-507 |
8.64e-26 |
|
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: 106.04 E-value: 8.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 327 HVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------NIGFLSQR 396
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtrrrrkafrrRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 397 P-------HIFADSIKN--NIAMYDDEicDEQVIQVLDEVGLKEKVLSlKYGiytsigeggEMLSGGQMRRIELSRLLLL 467
Cdd:COG1124 88 PyaslhprHTVDRILAEplRIHGLPDR--EERIAELLEQVGLPPSFLD-RYP---------HQLSGGQRQRVAIARALIL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488386603 468 KPDIVIFDEPAIGLDIETEKVIQQVL-----EHHFsttTVFIIAH 507
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLkdlreERGL---TYLFVSH 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
325-532 |
2.69e-25 |
|
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: 104.55 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYanSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN---------QASLNIGFLSQ 395
Cdd:COG4555 4 VENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgedvrkeprEARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 396 RPHIFAD-SIKNNIAMY------DDEICDEQVIQVLDEVGLkEKVLSLKYGiytsigeggeMLSGGQMRRIELSRLLLLK 468
Cdd:COG4555 82 ERGLYDRlTVRENIRYFaelyglFDEELKKRIEELIELLGL-EEFLDRRVG----------ELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 469 PDIVIFDEPAIGLDIE-TEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYI-ESGHLIKDDSI 532
Cdd:COG4555 151 PKVLLLDEPTNGLDVMaRRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVIlHKGKVVAQGSL 216
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
322-532 |
3.63e-25 |
|
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: 104.94 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 322 QVLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTpTHGTLSFNQASLN----------IG 391
Cdd:cd03289 2 QMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNsvplqkwrkaFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 392 FLSQRPHIFADSIKNNIAMYDdEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDI 471
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYG-KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386603 472 VIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDSI 532
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSI 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
302-513 |
4.52e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.13 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 302 LESEDKADSPTLKVDEQQFEQVLIKHVDFQYANSNHMaLKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTL 381
Cdd:COG4178 342 LEAADALPEAASRIETSEDGALALEDLTLRTPDGRPL-LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 382 SFNQASlNIGFLSQRPHIFADSIKNNIAmY---DDEICDEQVIQVLDEVGLKEKVlslkygiyTSIGEG---GEMLSGGQ 455
Cdd:COG4178 421 ARPAGA-RVLFLPQRPYLPLGTLREALL-YpatAEAFSDAELREALEAVGLGHLA--------ERLDEEadwDQVLSLGE 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488386603 456 MRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIR 513
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAA 548
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
325-493 |
1.24e-24 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 102.83 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN-------------IG 391
Cdd:COG3638 5 LRNLSKRYPGGTP-ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTalrgralrrlrrrIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 392 FLSQRPHIfadsIKN-----NIAM----------------YDDEIcdEQVIQVLDEVGLKEKVLslkygiytsigEGGEM 450
Cdd:COG3638 84 MIFQQFNL----VPRlsvltNVLAgrlgrtstwrsllglfPPEDR--ERALEALERVGLADKAY-----------QRADQ 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488386603 451 LSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVL 493
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLL 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
340-507 |
1.47e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.07 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQaSLNIGFLSQRPHIFAD-SIKNNIAMYDDEICD- 417
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLRIGYLPQEPPLDDDlTVLDTVLDGDAELRAl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 418 -------EQVIQVLDEVGLK--------------------EKVLSlKYGIYTSIGEG--GEmLSGGQMRRIELSRLLLLK 468
Cdd:COG0488 93 eaeleelEAKLAEPDEDLERlaelqeefealggweaearaEEILS-GLGFPEEDLDRpvSE-LSGGWRRRVALARALLSE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488386603 469 PDIVIFDEPAIGLDIETekvIQQvLEHHFST--TTVFIIAH 507
Cdd:COG0488 171 PDLLLLDEPTNHLDLES---IEW-LEEFLKNypGTVLVVSH 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
339-527 |
1.67e-24 |
|
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: 102.13 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-----------QASLNIG--FlsQRPHIFAD-SI 404
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeditglppheIARLGIGrtF--QIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 405 KNNIAM----------------YDDEICDEQVIQVLDEVGLKEKvlslkygIYTSIGEggemLSGGQMRRIELSRLLLLK 468
Cdd:cd03219 93 LENVMVaaqartgsglllararREEREARERAEELLERVGLADL-------ADRPAGE----LSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386603 469 PDIVIFDEPAIGLDI-ETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIY-IESGHLI 527
Cdd:cd03219 162 PKLLLLDEPAAGLNPeETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTvLDQGRVI 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
325-532 |
5.12e-24 |
|
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: 100.82 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANsnHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN-------------IG 391
Cdd:COG1127 8 VRNLTKSFGD--RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglsekelyelrrrIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 392 FLSQRPHIFAD-SIKNNIAMY--------DDEIcDEQVIQVLDEVGLKEkVLSLkygiYTSigEggemLSGGQMRRIELS 462
Cdd:COG1127 86 MLFQGGALFDSlTVFENVAFPlrehtdlsEAEI-RELVLEKLELVGLPG-AADK----MPS--E----LSGGMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386603 463 RLLLLKPDIVIFDEPAIGLDIETEKVIQQ-VLEHHFST-TTVFIIAHRDSTIRSSARRIY-IESGHLIKDDSI 532
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDElIRELRDELgLTSVVVTHDLDSAFAIADRVAvLADGKIIAEGTP 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
325-507 |
5.23e-24 |
|
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: 99.64 E-value: 5.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYaNSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN-------IGFLSQRP 397
Cdd:cd03226 2 IENISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKakerrksIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 398 --HIFADSIKNNIAMYDDEICDEQVIQvldevglkEKVLSlKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFD 475
Cdd:cd03226 81 dyQLFTDSVREELLLGLKELDAGNEQA--------ETVLK-DLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190
....*....|....*....|....*....|...
gi 488386603 476 EPAIGLDIETEKVIQQVLEHHFS-TTTVFIIAH 507
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAqGKAVIVITH 184
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
325-504 |
7.10e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 100.93 E-value: 7.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQY--ANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-----QASLNIGFLSQRP 397
Cdd:COG1116 10 LRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgkpvtGPGPDRGVVFQEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 398 HIFA-DSIKNNIAM------YDDEICDEQVIQVLDEVGLKEKvlsLKYgiYTSigeggeMLSGGQMRRIELSRLLLLKPD 470
Cdd:COG1116 90 ALLPwLTVLDNVALglelrgVPKAERRERARELLELVGLAGF---EDA--YPH------QLSGGMRQRVAIARALANDPE 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 488386603 471 IVIFDEPAIGLDIETEKVIQQVL-----EHHFstTTVFI 504
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELlrlwqETGK--TVLFV 195
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
17-296 |
9.92e-24 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. 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). The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350054 [Multi-domain] Cd Length: 290 Bit Score: 101.08 E-value: 9.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 17 LMLIMSVFLSFTVVAqniSISHFLNHLLYYQQQSLLLLlsVIFISLILRATFNMLIQFLGDHLAFKVKHMLREQvILKKS 96
Cdd:cd18781 7 ISLLANIAFVFSIAN---LLQKLLEGKLTTASLLIVLG--ILAIAIIVRFICTRLASRASYRASADVKKTLREK-IYDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 97 VR---------SIGEEINILTESIDGIGPFFQSYLPQVFKSMLIPIVIIITMCFVHLPTAIIMIVTAPFIPLFYVIFGLK 167
Cdd:cd18781 81 LRlgpsyqekvSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 168 TrdeSKDQMTYLNQFSQ---RFLNTAKGLITFKLLNQTKQSEQQLYKDSTRFRDLTMRILKSAFLSGLMLEFI----SML 240
Cdd:cd18781 161 A---KKLLSKYWGSYTDlgdSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVayggAAL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 241 GIGLvaleaALSLVVFNHINFVTAAIAIILAPEFYNAIKDLGQAFHTGKQSEGASD 296
Cdd:cd18781 238 GIIL-----ALLQFANGSISLAGALFIILLSAEFFLPLRLLGSFFHIAMNGMAASD 288
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
101-531 |
1.08e-23 |
|
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: 106.18 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 101 GEEINILTESIDGIgpffQSYLPQVFKSMLIPIVIIITMCFV-HLPTAIIMIVTAP------FIPLFYVIFG--LKtRDE 171
Cdd:TIGR00957 1062 GNLVNRFSKELDTV----DSMIPPVIKMFMGSLFNVIGALIViLLATPIAAVIIPPlgllyfFVQRFYVASSrqLK-RLE 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 172 SKDQMTYLNQFSQRFLNTAkgLI-------TFKLLNQTKQSEQQ--LYKDSTRFRDLTMRIlksAFLSGLMLEFISMLGI 242
Cdd:TIGR00957 1137 SVSRSPVYSHFNETLLGVS--VIrafeeqeRFIHQSDLKVDENQkaYYPSIVANRWLAVRL---ECVGNCIVLFAALFAV 1211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 243 --------GLVALEAALSLVVFNHINFVtaaiaIILAPEFYNAIkdlgQAFHTGKQ-SEGASDVVFSFLESEDKADSPtl 313
Cdd:TIGR00957 1212 isrhslsaGLVGLSVSYSLQVTFYLNWL-----VRMSSEMETNI----VAVERLKEySETEKEAPWQIQETAPPSGWP-- 1280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 314 kvdeqQFEQVLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTL---SFNQASL-- 388
Cdd:TIGR00957 1281 -----PRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIiidGLNIAKIgl 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 389 -----NIGFLSQRPHIFADSIKNNIAMYDdEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSR 463
Cdd:TIGR00957 1356 hdlrfKITIIPQDPVLFSGSLRMNLDPFS-QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLAR 1434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386603 464 LLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDS 531
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGA 1502
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
325-526 |
1.52e-23 |
|
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: 97.47 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANsnHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNqaslnigflSQRPHIFADSI 404
Cdd:cd03230 3 VRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL---------GKDIKKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 405 KNNIAMyddeicdeqviqVLDEVGLkekvlslkYGIYTsigeGGEML--SGGQMRRIELSRLLLLKPDIVIFDEPAIGLD 482
Cdd:cd03230 72 KRRIGY------------LPEEPSL--------YENLT----VRENLklSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488386603 483 IETEKVIQQVL-EHHFSTTTVFIIAHRDSTIRSSARRIY-IESGHL 526
Cdd:cd03230 128 PESRREFWELLrELKKEGKTILLSSHILEEAERLCDRVAiLNNGRI 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
325-507 |
1.89e-23 |
|
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: 98.79 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANsnHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLL-----SQSVTPTHGTLSFNQASLN---------- 389
Cdd:cd03260 3 LRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYdldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 --IGFLSQRPHIFADSIKNNIA-------MYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYtsigeggemLSGGQMRRIE 460
Cdd:cd03260 81 rrVGMVFQKPNPFPGSIYDNVAyglrlhgIKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRLC 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488386603 461 LSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAH 507
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTH 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
325-519 |
4.17e-23 |
|
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: 102.67 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPT---HGTLSFNQASL----------NIG 391
Cdd:COG1123 7 VRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLlelsealrgrRIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 392 FLSQRP--HIFADSIKNNIA-------MYDDEIcDEQVIQVLDEVGLKEkvlslKYGIYTSigeggeMLSGGQMRRIELS 462
Cdd:COG1123 87 MVFQDPmtQLNPVTVGDQIAealenlgLSRAEA-RARVLELLEAVGLER-----RLDRYPH------QLSGGQRQRVAIA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488386603 463 RLLLLKPDIVIFDEPAIGLDIETEKVIQQVLE--HHFSTTTVFIIAHRDSTIRSSARRI 519
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEIADRV 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
326-526 |
6.37e-23 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 97.09 E-value: 6.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 326 KHVDFQYANsNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN------IGFLsqRPHI 399
Cdd:cd03292 4 INVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgraIPYL--RRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 400 ---FADS-------IKNNIAmYDDEICD-------EQVIQVLDEVGLKEKVLSLKygiytsigeggEMLSGGQMRRIELS 462
Cdd:cd03292 81 gvvFQDFrllpdrnVYENVA-FALEVTGvppreirKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 463 RLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEH-HFSTTTVFIIAHRDSTI-RSSARRIYIESGHL 526
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
325-493 |
6.70e-23 |
|
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: 97.64 E-value: 6.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN-------------IG 391
Cdd:cd03256 3 VENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgkalrqlrrqIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 392 FLSQRPHIFA--DSIKN-------------NIAMYDDEICDEQVIQVLDEVGLKEKvlslkygIYTSIGEggemLSGGQM 456
Cdd:cd03256 82 MIFQQFNLIErlSVLENvlsgrlgrrstwrSLFGLFPKEEKQRALAALERVGLLDK-------AYQRADQ----LSGGQQ 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 488386603 457 RRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVL 493
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLL 187
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
339-530 |
2.05e-22 |
|
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: 96.25 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN---QASLNIGFLSQRPHIF------------ADS 403
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAglvPWKRRKKFLRRIGVVFgqktqlwwdlpvIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 404 IKNNIAMYDdeICDEQVIQVLDEvgLKEkVLSLKYGIYTSIGEggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDI 483
Cdd:cd03267 116 FYLLAAIYD--LPPARFKKRLDE--LSE-LLDLEELLDTPVRQ----LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488386603 484 ETEKVIQQVL-----EHHfstTTVFIIAHRDSTIRSSARR-IYIESGHLIKDD 530
Cdd:cd03267 187 VAQENIRNFLkeynrERG---TTVLLTSHYMKDIEALARRvLVIDKGRLLYDG 236
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
325-529 |
2.79e-22 |
|
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: 94.04 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYanSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNigflSQRPHIFAdsi 404
Cdd:cd03214 2 VENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA----SLSPKELA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 405 kNNIAMyddeicdeqVIQVLDEVGLkekvLSLKYGIYTSigeggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDI- 483
Cdd:cd03214 73 -RKIAY---------VPQALELLGL----AHLADRPFNE-------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIa 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488386603 484 ---ETEKVIQQvLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKD 529
Cdd:cd03214 132 hqiELLELLRR-LARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
325-526 |
3.16e-22 |
|
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: 94.90 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYanSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN------------IGF 392
Cdd:cd03262 3 IKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkninelrqkVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 393 LSQRPHIFAD-SIKNNIAM-------YDDEICDEQVIQVLDEVGLKEKVLSlkygiYTSigeggeMLSGGQMRRIELSRL 464
Cdd:cd03262 81 VFQQFNLFPHlTVLENITLapikvkgMSKAEAEERALELLEKVGLADKADA-----YPA------QLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 465 LLLKPDIVIFDEPAIGLDIET----EKVIQQVLEHHfstTTVFIIAHRDSTIRSSARR-IYIESGHL 526
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELvgevLDVMKDLAEEG---MTMVVVTHEMGFAREVADRvIFMDDGRI 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-507 |
3.38e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 322 QVL-IKHVDFQYANsnHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQaSLNIGFLSQRPHIF 400
Cdd:COG0488 314 KVLeLEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE-TVKIGYFDQHQEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 401 --ADSIKNNIAMYDDEICDEQVIQVL-------DEVglkekvlslkygiYTSIGEggemLSGGQMRRIELSRLLLLKPDI 471
Cdd:COG0488 391 dpDKTVLDELRDGAPGGTEQEVRGYLgrflfsgDDA-------------FKPVGV----LSGGEKARLALAKLLLSPPNV 453
|
170 180 190
....*....|....*....|....*....|....*.
gi 488386603 472 VIFDEPAIGLDIETEKVIQQVLEhHFStTTVFIIAH 507
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEALD-DFP-GTVLLVSH 487
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
325-525 |
9.05e-22 |
|
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: 92.64 E-value: 9.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANsnHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIGFLSQRPHifadsi 404
Cdd:cd03229 3 LKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 405 KNNIAMyddeicdeqVIQ---------VLDEVGLKekvlslkygiytsigeggemLSGGQMRRIELSRLLLLKPDIVIFD 475
Cdd:cd03229 75 RRRIGM---------VFQdfalfphltVLENIALG--------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488386603 476 EPAIGLDIETEKVIQQVLE--HHFSTTTVFIIAHR-DSTIRSSARRIYIESGH 525
Cdd:cd03229 126 EPTSALDPITRREVRALLKslQAQLGITVVLVTHDlDEAARLADRVVVLRDGK 178
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
340-531 |
1.14e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 99.67 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFLSQRPHIFADSIKNNIA 409
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfgltdlrrvLSIIPQSPVLFSGTVRFNID 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 410 MYDdEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVI 489
Cdd:PLN03232 1332 PFS-EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488386603 490 QQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDS 531
Cdd:PLN03232 1411 QRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDS 1452
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
296-532 |
1.51e-21 |
|
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: 99.21 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 296 DVVFSFLESEDKADSPTLKVDEQQFEQVLI---KHVDFQYANSNHM---------------ALKNISFSVNKGEKVAIVG 357
Cdd:TIGR01271 1173 SRVFKFIDLPQEEPRPSGGGGKYQLSTVLVienPHAQKCWPSGGQMdvqgltakyteagraVLQDLSFSVEGGQRVGLLG 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 358 PSGAGKSTLA----KLLSQSVTPTHGTLSFNQASLN-----IGFLSQRPHIFADSIKNNIAMYDdEICDEQVIQVLDEVG 428
Cdd:TIGR01271 1253 RTGSGKSTLLsallRLLSTEGEIQIDGVSWNSVTLQtwrkaFGVIPQKVFIFSGTFRKNLDPYE-QWSDEEIWKVAEEVG 1331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 429 LKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHR 508
Cdd:TIGR01271 1332 LKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHR 1411
|
250 260
....*....|....*....|....
gi 488386603 509 DSTIRSSARRIYIESGHLIKDDSI 532
Cdd:TIGR01271 1412 VEALLECQQFLVIEGSSVKQYDSI 1435
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
325-527 |
2.32e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 94.31 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFLS 394
Cdd:PRK13635 8 VEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeetvwdvrrqVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 395 QRPH------IFADSIK---NNIAMYDDEICdEQVIQVLDEVGLKEKVLslkygiytsigEGGEMLSGGQMRRIELSRLL 465
Cdd:PRK13635 88 QNPDnqfvgaTVQDDVAfglENIGVPREEMV-ERVDQALRQVGMEDFLN-----------REPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 466 LLKPDIVIFDEPAIGLD----IETEKVIQQVLEHhfSTTTVFIIAHRDSTIRSSARRIYIESGHLI 527
Cdd:PRK13635 156 ALQPDIIILDEATSMLDprgrREVLETVRQLKEQ--KGITVLSITHDLDEAAQADRVIVMNKGEIL 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
340-531 |
4.36e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 97.89 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHG--------TLSFNQASL--NIGFLSQRPHIFADSIKNNIA 409
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGrilidgcdISKFGLMDLrkVLGIIPQAPVLFSGTVRFNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 410 MYDdEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVI 489
Cdd:PLN03130 1335 PFN-EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALI 1413
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488386603 490 QQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDS 531
Cdd:PLN03130 1414 QKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDT 1455
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
326-531 |
6.24e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.97 E-value: 6.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 326 KHVDFQYANSNHM---ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN------------- 389
Cdd:PRK13641 6 ENVDYIYSPGTPMekkGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnknlkklrk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 -IGFLSQRP--HIFADSIKNNIAM------YDDEICDEQVIQVLDEVGLKEKVLSlkygiyTSIGEggemLSGGQMRRIE 460
Cdd:PRK13641 86 kVSLVFQFPeaQLFENTVLKDVEFgpknfgFSEDEAKEKALKWLKKVGLSEDLIS------KSPFE----LSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386603 461 LSRLLLLKPDIVIFDEPAIGLDIETEKVIQQV-LEHHFSTTTVFIIAHRDSTIRSSARRIYI-ESGHLIKDDS 531
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVAEYADDVLVlEHGKLIKHAS 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
325-535 |
1.70e-20 |
|
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: 90.33 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVD--FQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-------------QASLN 389
Cdd:cd03258 4 LKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtdltllsgkelrKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 IGFLSQRPHIFAD-SIKNNIAM------YDDEICDEQVIQVLDEVGLKEKVlslkyGIYTSigeggeMLSGGQMRRIELS 462
Cdd:cd03258 84 IGMIFQHFNLLSSrTVFENVALpleiagVPKAEIEERVLELLELVGLEDKA-----DAYPA------QLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 463 RLLLLKPDIVIFDEPAIGLDIETEKVIQQVLE--HHFSTTTVFIIAHRDSTIRSSARRI-YIESGHLIKDDSIISV 535
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRdiNRELGLTIVLITHEMEVVKRICDRVaVMEKGEVVEEGTVEEV 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
305-523 |
1.87e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 95.87 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 305 EDKADSPTLKvdeqQFEQVLIKHVDFQYANSNHMAL-KNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTL-- 381
Cdd:PTZ00265 369 ENNDDGKKLK----DIKKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIii 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 382 --SFNQASLN-------IGFLSQRPHIFADSIKNNI----------------------AMYDDE---------------- 414
Cdd:PTZ00265 445 ndSHNLKDINlkwwrskIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnyynedgnDSQENKnkrnscrakcagdlnd 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 415 -------------------ICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFD 475
Cdd:PTZ00265 525 msnttdsneliemrknyqtIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILD 604
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 488386603 476 EPAIGLDIETEKVIQQV---LEHHFSTTTVfIIAHRDSTIRsSARRIYIES 523
Cdd:PTZ00265 605 EATSSLDNKSEYLVQKTinnLKGNENRITI-IIAHRLSTIR-YANTIFVLS 653
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
325-527 |
1.92e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 90.46 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANsnHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSF--NQASL-------------- 388
Cdd:PRK11124 5 LNGINCFYGA--HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFsktpsdkairelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 389 NIGFLSQR----PHIfadSIKNN-------IAMYDDEICDEQVIQVLDEVGLKEKvlSLKYGIYtsigeggemLSGGQMR 457
Cdd:PRK11124 83 NVGMVFQQynlwPHL---TVQQNlieapcrVLGLSKDQALARAEKLLERLRLKPY--ADRFPLH---------LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386603 458 RIELSRLLLLKPDIVIFDEPAIGLDIE-TEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARR-IYIESGHLI 527
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKTASRvVYMENGHIV 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
339-527 |
1.98e-20 |
|
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: 90.87 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------------------------- 389
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglpphriarlgiartfqnprlfpeltvle 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 ---IGFLSQRPHIFADSIKNNIAMYDDEI-CDEQVIQVLDEVGLKEKvlslkygIYTSIGEggemLSGGQMRRIELSRLL 465
Cdd:COG0411 99 nvlVAAHARLGRGLLAALLRLPRARREEReARERAEELLERVGLADR-------ADEPAGN----LSYGQQRRLEIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488386603 466 LLKPDIVIFDEPAIGLDI-ETEKVIQQVLE-HHFSTTTVFIIAHRDSTIRSSARRIY-IESGHLI 527
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPeETEELAELIRRlRDERGITILLIEHDMDLVMGLADRIVvLDFGRVI 232
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
334-531 |
2.66e-20 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 90.05 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 334 NSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL-------------NIGFLSQRPHIF 400
Cdd:TIGR02315 12 PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrgkklrklrrRIGMIFQHYNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 401 ADSI------------KNNIAMYDDEICDEQ---VIQVLDEVGLKEKVLSLkygiytsigegGEMLSGGQMRRIELSRLL 465
Cdd:TIGR02315 92 ERLTvlenvlhgrlgyKPTWRSLLGRFSEEDkerALSALERVGLADKAYQR-----------ADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386603 466 LLKPDIVIFDEPAIGLDIETEKVIQQVLE---HHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDS 531
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKrinKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGA 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
325-504 |
4.94e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 91.70 E-value: 4.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANsnHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL--------NIGFLSQR 396
Cdd:COG3842 8 LENVSKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekrNVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 397 ----PHIfadSIKNNIA-------MYDDEIcDEQVIQVLDEVGLKEkvLSLKYgiytsIGEggemLSGGQMRRIELSRLL 465
Cdd:COG3842 86 yalfPHL---TVAENVAfglrmrgVPKAEI-RARVAELLELVGLEG--LADRY-----PHQ----LSGGQQQRVALARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488386603 466 LLKPDIVIFDEPAIGLDIET-EKVIQQVLEHH--FSTTTVFI 504
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLrEEMREELRRLQreLGITFIYV 192
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
339-504 |
7.76e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.79 E-value: 7.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-------------------Q-------ASLN--- 389
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQgqdllkadpeaqkllrqkiQivfqnpyGSLNprk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 -IGFlsqrphIFADSIKNNIAMYDDEIcDEQVIQVLDEVGLKEKvlslKYGIYTsigeggEMLSGGQMRRIELSRLLLLK 468
Cdd:PRK11308 110 kVGQ------ILEEPLLINTSLSAAER-REKALAMMAKVGLRPE----HYDRYP------HMFSGGQRQRIAIARALMLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488386603 469 PDIVIFDEPAIGLDIEtekvIQ-QVL------EHHFSTTTVFI 504
Cdd:PRK11308 173 PDVVVADEPVSALDVS----VQaQVLnlmmdlQQELGLSYVFI 211
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
322-539 |
7.82e-20 |
|
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: 89.20 E-value: 7.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 322 QVLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHG----------TLSFNQASLNIG 391
Cdd:cd03288 19 EIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGkividgidisKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 392 FLSQRPHIFADSIKNNIamyDDE--ICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKP 469
Cdd:cd03288 99 IILQDPILFSGSIRFNL---DPEckCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 470 DIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDSIISVTRSE 539
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
339-507 |
9.55e-20 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 87.81 E-value: 9.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL---------NIGFLSQRPHifADSI---KN 406
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvreprevrrRIGIVFQDLS--VDDEltgWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 407 NIAM------YDDEICDEQVIQVLDEVGLKEKV--LSLKYgiytsigeggemlSGGQMRRIELSRLLLLKPDIVIFDEPA 478
Cdd:cd03265 93 NLYIharlygVPGAERRERIDELLDFVGLLEAAdrLVKTY-------------SGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190
....*....|....*....|....*....|...
gi 488386603 479 IGLDIETE----KVIQQVLEHHfsTTTVFIIAH 507
Cdd:cd03265 160 IGLDPQTRahvwEYIEKLKEEF--GMTILLTTH 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
340-521 |
1.07e-19 |
|
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: 88.16 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL--------NIGFLSQR----PHIfadSIKNN 407
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDItnlppekrDISYVPQNyalfPHM---TVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 408 IA------MYDDEICDEQVIQVLDEVGLKEkVLSLKygiytsigegGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGL 481
Cdd:cd03299 92 IAyglkkrKVDKKEIERKVLEIAEMLGIDH-LLNRK----------PETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488386603 482 DIET-EKVIQQVLE-HHFSTTTVFIIAHRDSTIRSSARRIYI 521
Cdd:cd03299 161 DVRTkEKLREELKKiRKEFGVTVLHVTHDFEEAWALADKVAI 202
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
325-488 |
1.12e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 88.56 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYanSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLL--------SQSVTpthGTLSFNQASLN------- 389
Cdd:COG1117 14 VRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipGARVE---GEILLDGEDIYdpdvdvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 -----IGFLSQRPHIFADSIKNNIA-------MYDDEICDEQVIQVL------DEVG--LKEKVLSLkygiytsigegge 449
Cdd:COG1117 89 elrrrVGMVFQKPNPFPKSIYDNVAyglrlhgIKSKSELDEIVEESLrkaalwDEVKdrLKKSALGL------------- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488386603 450 mlSGGQMRRIELSRLLLLKPDIVIFDEPAIGLD-IETEKV 488
Cdd:COG1117 156 --SGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAKI 193
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
340-507 |
1.20e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.20 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLS--QSVTPTHGTLSFNQASLN-----------IgFLS-QRP-------- 397
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILelspderaragI-FLAfQYPveipgvsv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 398 HIFADSIKNNIA--MYDDEICDEQVIQVLDEVGLKEKVLSlkygiyTSIGEGgemLSGGQMRRIELSRLLLLKPDIVIFD 475
Cdd:COG0396 95 SNFLRTALNARRgeELSAREFLKLLKEKMKELGLDEDFLD------RYVNEG---FSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190
....*....|....*....|....*....|...
gi 488386603 476 EPAIGLDIET-EKVIQQVLEHHFSTTTVFIIAH 507
Cdd:COG0396 166 ETDSGLDIDAlRIVAEGVNKLRSPDRGILIITH 198
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
336-494 |
1.56e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 87.74 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 336 NHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL------------NIGFLSQRPHIFAD- 402
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskkdinklrrKVGMVFQQFNLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 403 SIKNNIAM-------YDDEICDEQVIQVLDEVGLKEKVLSlkygiYTSigeggeMLSGGQMRRIELSRLLLLKPDIVIFD 475
Cdd:COG1126 93 TVLENVTLapikvkkMSKAEAEERAMELLERVGLADKADA-----YPA------QLSGGQQQRVAIARALAMEPKVMLFD 161
|
170
....*....|....*....
gi 488386603 476 EPAIGLDIETekvIQQVLE 494
Cdd:COG1126 162 EPTSALDPEL---VGEVLD 177
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
325-528 |
2.62e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.12 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLS----------FNQASLNIGFLS 394
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKidgitiskenLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 395 QRP--HIFADSIKNNIAMYDDEICdeqviqvLDEVGLKEKV--LSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPD 470
Cdd:PRK13632 90 QNPdnQFIGATVEDDIAFGLENKK-------VPPKKMKDIIddLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 471 IVIFDEPAIGLDIETEKVIQQVLE--HHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIK 528
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIA 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
325-491 |
2.81e-19 |
|
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: 87.36 E-value: 2.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYaNSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------NIGFLS 394
Cdd:cd03295 3 FENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIreqdpvelrrKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 395 QR----PHIfadSIKNNIAM------YDDEICDEQVIQVLDEVGLKEKVLSLKYgiytsigegGEMLSGGQMRRIELSRL 464
Cdd:cd03295 82 QQiglfPHM---TVEENIALvpkllkWPKEKIRERADELLALVGLDPAEFADRY---------PHELSGGQQQRVGVARA 149
|
170 180
....*....|....*....|....*..
gi 488386603 465 LLLKPDIVIFDEPAIGLDIETEKVIQQ 491
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQE 176
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
325-532 |
3.02e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 86.73 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYansNHMALkNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIGFLSQRP--HIFAD 402
Cdd:COG3840 4 LDDLTYRY---GDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPvsMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 403 -------SIKNNIAM-------YDDEicD-EQVIQVLDEVGLKEKvLSLKYGIytsigeggemLSGGQMRRIELSRLLLL 467
Cdd:COG3840 80 nnlfphlTVAQNIGLglrpglkLTAE--QrAQVEQALERVGLAGL-LDRLPGQ----------LSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 468 KPDIVIFDEPAIGLDI----ETEKVIQQVLEHHfsTTTVFIIAHR-DSTIRSSARRIYIESGHLIKDDSI 532
Cdd:COG3840 147 KRPILLLDEPFSALDPalrqEMLDLVDELCRER--GLTVLMVTHDpEDAARIADRVLLVADGRIAADGPT 214
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
325-507 |
3.39e-19 |
|
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: 84.04 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYanSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQaSLNIGFLSQrphifadsi 404
Cdd:cd03221 3 LENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-TVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 405 knniamyddeicdeqviqvldevglkekvlslkygiytsigeggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIE 484
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180
....*....|....*....|...
gi 488386603 485 TEKVIQQVLEHHfsTTTVFIIAH 507
Cdd:cd03221 105 SIEALEEALKEY--PGTVILVSH 125
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
339-504 |
3.44e-19 |
|
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: 86.03 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL--------NIGFLSQR----PHIfadSIKN 406
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVtgvpperrNIGMVFQDyalfPHL---TVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 407 NIA-------MYDDEIcDEQVIQVLDEVGLKEKvlsLKYGIYTsigeggemLSGGQMRRIELSRLLLLKPDIVIFDEPAI 479
Cdd:cd03259 92 NIAfglklrgVPKAEI-RARVRELLELVGLEGL---LNRYPHE--------LSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180
....*....|....*....|....*...
gi 488386603 480 GLDIETEKVIQQVLE---HHFSTTTVFI 504
Cdd:cd03259 160 ALDAKLREELREELKelqRELGITTIYV 187
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
325-527 |
3.51e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 86.99 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANsnHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNigfLSQRPHIFA-DS 403
Cdd:COG4161 5 LKNINCFYGS--HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFD---FSQKPSEKAiRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 404 IKNNIAM----YD----------------------DEICDEQVIQVLDEVGLKEKvlSLKYGIYtsigeggemLSGGQMR 457
Cdd:COG4161 80 LRQKVGMvfqqYNlwphltvmenlieapckvlglsKEQAREKAMKLLARLRLTDK--ADRFPLH---------LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386603 458 RIELSRLLLLKPDIVIFDEPAIGLDIE-TEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARR-IYIESGHLI 527
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKVASQvVYMEKGRII 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
326-530 |
5.31e-19 |
|
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: 85.95 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 326 KHVDFQYANSNHM--ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL--------------N 389
Cdd:COG4181 12 RGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldedararlrarH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 IGFLSQR----PHIFAdsiKNNIAM------YDDeiCDEQVIQVLDEVGLKEKVlslkyGIYTSigeggeMLSGGQMRRI 459
Cdd:COG4181 92 VGFVFQSfqllPTLTA---LENVMLplelagRRD--ARARARALLERVGLGHRL-----DHYPA------QLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 460 ELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVL-----EHHfstTTVFIIAHRDSTIRSSARRIYIESGHLIKDD 530
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLfelnrERG---TTLVLVTHDPALAARCDRVLRLRAGRLVEDT 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
325-483 |
5.52e-19 |
|
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: 86.64 E-value: 5.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANsnHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------NIGFLS 394
Cdd:COG1120 4 AENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslsrrelarRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 395 QRPHI-FADSIKNNIAMY--------------DDEICDEqviqVLDEVGLKEkvLSLKYgiYTSigeggemLSGGQMRRI 459
Cdd:COG1120 82 QEPPApFGLTVRELVALGryphlglfgrpsaeDREAVEE----ALERTGLEH--LADRP--VDE-------LSGGERQRV 146
|
170 180
....*....|....*....|....
gi 488386603 460 ELSRLLLLKPDIVIFDEPAIGLDI 483
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDL 170
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
336-495 |
9.87e-19 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 85.29 E-value: 9.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 336 NHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQ-----------ASLNIGFLSQRPHIFAD-S 403
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrARLGIGYLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 404 IKNNI------AMYDDEICDEQVIQVLDEVGLKEkvLSLKYGIYtsigeggemLSGGQMRRIELSRLLLLKPDIVIFDEP 477
Cdd:cd03218 92 VEENIlavleiRGLSKKEREEKLEELLEEFHITH--LRKSKASS---------LSGGERRRVEIARALATNPKFLLLDEP 160
|
170
....*....|....*...
gi 488386603 478 AIGLDIETEKVIQQVLEH 495
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKI 178
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
325-529 |
1.14e-18 |
|
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: 84.55 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSnhMALKNISFSVNKGeKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN---------IGFLSQ 395
Cdd:cd03264 3 LENLTKRYGKK--RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 396 R----PHIFADSIKNNIAMY---DDEICDEQVIQVLDEVGL----KEKVLSLkygiytsigeggemlSGGQMRRIELSRL 464
Cdd:cd03264 80 EfgvyPNFTVREFLDYIAWLkgiPSKEVKARVDEVLELVNLgdraKKKIGSL---------------SGGMRRRVGIAQA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 465 LLLKPDIVIFDEPAIGLDIEtEKViqqVLEHHF---STTTVFIIA-HRDSTIRSSARRIYI-ESGHLIKD 529
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPE-ERI---RFRNLLselGEDRIVILStHIVEDVESLCNQVAVlNKGKLVFE 210
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
326-506 |
1.31e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 85.96 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 326 KHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFLSQ 395
Cdd:PRK13648 11 KNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddnfeklrkhIGIVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 396 RP-HIFADSI---------KNNIAMYDDeiCDEQVIQVLDEVGLKEKVLSLKYGiytsigeggemLSGGQMRRIELSRLL 465
Cdd:PRK13648 91 NPdNQFVGSIvkydvafglENHAVPYDE--MHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAGVL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488386603 466 LLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIA 506
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIIS 198
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
339-532 |
1.39e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.68 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-------QASL--NIGF-LSQRPHIF-----ADS 403
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyvpfkrRKEFarRIGVvFGQRSQLWwdlpaIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 404 IKNNIAMYddEICDEQVIQVLDEvgLKEkVLSLKYGIYTSIGEggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDI 483
Cdd:COG4586 117 FRLLKAIY--RIPDAEYKKRLDE--LVE-LLDLGELLDTPVRQ----LSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488386603 484 ETEKVIQQVL-----EHHfstTTVFIIAHRDSTIRSSARRIY-IESGHLIKDDSI 532
Cdd:COG4586 188 VSKEAIREFLkeynrERG---TTILLTSHDMDDIEALCDRVIvIDHGRIIYDGSL 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
339-507 |
1.69e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 86.71 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN--------------------------QASLN--- 389
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqditglsgrelrplrrrmqmvfqdpYASLNprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 -IGflsqrpHIFADSIKNNiAMYDDEICDEQVIQVLDEVGLKEKVLSlKYGiytsigeggEMLSGGQMRRIELSRLLLLK 468
Cdd:COG4608 113 tVG------DIIAEPLRIH-GLASKAERRERVAELLELVGLRPEHAD-RYP---------HEFSGGQRQRIGIARALALN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488386603 469 PDIVIFDEPAIGLDIEtekvIQ-QV------LEHHFSTTTVFiIAH 507
Cdd:COG4608 176 PKLIVCDEPVSALDVS----IQaQVlnlledLQDELGLTYLF-ISH 216
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
339-532 |
2.05e-18 |
|
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: 85.90 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN---------QASLNIGFLSQRPHIFAD-SIKNNI 408
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAgydvvreprKVRRSIGIVPQYASVDEDlTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 409 AMYDD------EICDEQVIQVLDEVGLKEKVlSLKYGIYtsigeggemlSGGQMRRIELSRLLLLKPDIVIFDEPAIGLD 482
Cdd:TIGR01188 88 EMMGRlyglpkDEAEERAEELLELFELGEAA-DRPVGTY----------SGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488386603 483 IETEKVIQQVLEHHFST-TTVFIIAHRDSTIRSSARRI-YIESGHLIKDDSI 532
Cdd:TIGR01188 157 PRTRRAIWDYIRALKEEgVTILLTTHYMEEADKLCDRIaIIDHGRIIAEGTP 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
339-521 |
2.16e-18 |
|
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: 82.48 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNigFLSQRphifaDSIKNNIAMyddeicde 418
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--FASPR-----DARRAGIAM-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 419 qVIQvldevglkekvlslkygiytsigeggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDI-ETEKVIQQVLEHHF 497
Cdd:cd03216 80 -VYQ----------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPaEVERLFKVIRRLRA 130
|
170 180
....*....|....*....|....
gi 488386603 498 STTTVFIIAHRDSTIRSSARRIYI 521
Cdd:cd03216 131 QGVAVIFISHRLDEVFEIADRVTV 154
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
338-496 |
2.41e-18 |
|
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: 83.31 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 338 MALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL---------NIGFLSQRPHIFAD-SIKNN 407
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdfqrdsiarGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 408 IAMYDDEICDEQVIQVLDEVGLKekvlSLKYGIYTSigeggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEK 487
Cdd:cd03231 94 LRFWHADHSDEQVEEALARVGLN----GFEDRPVAQ-------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
....*....
gi 488386603 488 VIQQVLEHH 496
Cdd:cd03231 163 RFAEAMAGH 171
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
339-521 |
2.57e-18 |
|
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: 83.42 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN--------IGFLSQRPHIFAD-------S 403
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQkniealrrIGALIEAPGFYPNltarenlR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 404 IKNNIAMYDDEICDEqviqVLDEVGLKEkVLSLKYGIYtSIGeggemlsggqMR-RIELSRLLLLKPDIVIFDEPAIGLD 482
Cdd:cd03268 95 LLARLLGIRKKRIDE----VLDVVGLKD-SAKKKVKGF-SLG----------MKqRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488386603 483 IETEKVIQQVLEHHFST-TTVFIIAHRDSTIRSSARRIYI 521
Cdd:cd03268 159 PDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGI 198
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
340-526 |
3.81e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.71 E-value: 3.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN--------------IGFLSQRPHIFAD-SI 404
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaakaelrnqkLGFIYQFHHLLPDfTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 405 KNNIAM-------YDDEIcDEQVIQVLDEVGLKEKVlslkygiYTSIGEggemLSGGQMRRIELSRLLLLKPDIVIFDEP 477
Cdd:PRK11629 105 LENVAMplligkkKPAEI-NSRALEMLAAVGLEHRA-------NHRPSE----LSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488386603 478 AIGLDIETEKVIQQVL-EHHFSTTTVFIIAHRDSTI-RSSARRIYIESGHL 526
Cdd:PRK11629 173 TGNLDARNADSIFQLLgELNRLQGTAFLVVTHDLQLaKRMSRQLEMRDGRL 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
321-507 |
3.98e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.45 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 321 EQVLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQ--SVTPT---HGTLSFNQASLN------ 389
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlnDLIPGfrvEGKVTFHGKNLYapdvdp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 ------IGFLSQRPHIFADSIKNNIAmYDDEI------CDEQVIQVLDEVGLKEKVLSlkygiytSIGEGGEMLSGGQMR 457
Cdd:PRK14243 87 vevrrrIGMVFQKPNPFPKSIYDNIA-YGARIngykgdMDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488386603 458 RIELSRLLLLKPDIVIFDEPAIGLD-IET---EKVIQQVLEHHfsttTVFIIAH 507
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDpISTlriEELMHELKEQY----TIIIVTH 208
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
340-533 |
4.17e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 82.57 E-value: 4.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLS--QSVTPTHGTLSFN-----------QASLNIGFLSQRPhifadsikn 406
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKgeditdlppeeRARLGIFLAFQYP--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 407 niamydDEIcdeqviqvlDEVGLKEKVLSLKYGiytsigeggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETE 486
Cdd:cd03217 87 ------PEI---------PGVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488386603 487 KVIQQVLEH-HFSTTTVFIIAHRdstirssaRRI--YIES--GHLIKDDSII 533
Cdd:cd03217 141 RLVAEVINKlREEGKSVLIITHY--------QRLldYIKPdrVHVLYDGRIV 184
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
327-521 |
4.89e-18 |
|
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: 85.10 E-value: 4.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 327 HVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTP---THGTLSFN------------------- 384
Cdd:COG0444 8 KVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDgedllklsekelrkirgre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 385 --------QASLN----IGflsqrpHIFADSIKNNIAMYDDEIcDEQVIQVLDEVGLK--EKVLSlKYgiytsigegGEM 450
Cdd:COG0444 88 iqmifqdpMTSLNpvmtVG------DQIAEPLRIHGGLSKAEA-RERAIELLERVGLPdpERRLD-RY---------PHE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386603 451 LSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIetekVIQ-QVLE------HHFSTTTVFiIAHrD-STIRSSARRIYI 521
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlqRELGLAILF-ITH-DlGVVAEIADRVAV 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
339-494 |
4.91e-18 |
|
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: 82.87 E-value: 4.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-----------QASLNIGFLSQRPHIFAD-SIKN 406
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglppheRARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 407 NIAMYDDEICDEQVIQVLDEV-----GLKEKVLSLkygiytsigeGGEmLSGGQMRRIELSRLLLLKPDIVIFDEPAIGL 481
Cdd:cd03224 95 NLLLGAYARRRAKRKARLERVyelfpRLKERRKQL----------AGT-LSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170
....*....|...
gi 488386603 482 dieTEKVIQQVLE 494
Cdd:cd03224 164 ---APKIVEEIFE 173
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
339-528 |
6.19e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.97 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHG-------TLSFNQASL-----NIGFLSQRP--HIFADSI 404
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGevlikgePIKYDKKSLlevrkTVGIVFQNPddQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 405 KNNIA-------MYDDEIcDEQVIQVLDEVGLkekvlslkygiytsigEGGE-----MLSGGQMRRIELSRLLLLKPDIV 472
Cdd:PRK13639 97 EEDVAfgplnlgLSKEEV-EKRVKEALKAVGM----------------EGFEnkpphHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488386603 473 IFDEPAIGLDIETEKVIQQVL-EHHFSTTTVFIIAHRDSTIRSSARRIYIES-GHLIK 528
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVPVYADKVYVMSdGKIIK 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
325-504 |
6.42e-18 |
|
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: 83.21 E-value: 6.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYanSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGtlsfNQASL---------------N 389
Cdd:COG1119 6 LRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----NDVRLfgerrggedvwelrkR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 IGFLSQ------RPHI---------FADSI---KNniamYDDEIcDEQVIQVLDEVGLKEKvLSLKYGiytsigeggeML 451
Cdd:COG1119 80 IGLVSPalqlrfPRDEtvldvvlsgFFDSIglyRE----PTDEQ-RERARELLELLGLAHL-ADRPFG----------TL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 452 SGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIE-TEKVIQQV--LEHHFSTTTVFI 504
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGaRELLLALLdkLAAEGAPTLVLV 199
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
328-530 |
9.41e-18 |
|
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: 81.96 E-value: 9.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 328 VDFQYANSNHMAlkNISFSVNkGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN--------------IGFL 393
Cdd:cd03297 4 VDIEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdsrkkinlppqqrkIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 394 SQR----PHIfadSIKNNIAM-------YDDEICDEQVIQVLDEVGLKEKvlslkyGIYTsigeggemLSGGQMRRIELS 462
Cdd:cd03297 81 FQQyalfPHL---NVRENLAFglkrkrnREDRISVDELLDLLGLDHLLNR------YPAQ--------LSGGEKQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386603 463 RLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEH---HFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDD 530
Cdd:cd03297 144 RALAAQPELLLLDEPFSALDRALRLQLLPELKQikkNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
323-526 |
1.01e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.19 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 323 VLIKHVDFQYANSNhmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIGFLSQRpHIFAD 402
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR-LMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 403 -------SIKNNIAMYDDEICDEQVIQVLDEVGLKEKVlslkygiytsiGEGGEMLSGGQMRRIELSRLLLLKPDIVIFD 475
Cdd:PRK11247 90 arllpwkKVIDNVGLGLKGQWRDAALQALAAVGLADRA-----------NEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 476 EPAIGLD----IETEKVIQQV-LEHHFsttTVFIIAHRDSTIRSSARR-IYIESGHL 526
Cdd:PRK11247 159 EPLGALDaltrIEMQDLIESLwQQHGF---TVLLVTHDVSEAVAMADRvLLIEEGKI 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
336-533 |
1.14e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 86.10 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 336 NHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASlNIGFLSQRP-HIFAD--SIKNNIAMYD 412
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA-NIGYYAQDHaYDFENdlTLFDWMSQWR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 413 DEICDEQVIQ-VL-------DEVGLKEKVLSlkyGiytsiGEGGEMLSGgqmrrielsRLLLLKPDIVIFDEPAIGLDIE 484
Cdd:PRK15064 410 QEGDDEQAVRgTLgrllfsqDDIKKSVKVLS---G-----GEKGRMLFG---------KLMMQKPNVLVMDEPTNHMDME 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488386603 485 TEKVIQQVLEhHFSTTTVFiIAHRDSTIRSSARRIyIEsghlIKDDSII 533
Cdd:PRK15064 473 SIESLNMALE-KYEGTLIF-VSHDREFVSSLATRI-IE----ITPDGVV 514
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
340-489 |
1.54e-17 |
|
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: 82.98 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLsfnQASLNIGFLSQRPHIFADSIKNNI--AMYDDEICD 417
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---KHSGRISFSSQFSWIMPGTIKENIifGVSYDEYRY 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386603 418 EQVIQVLDevgLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVI 489
Cdd:cd03291 130 KSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
322-503 |
2.73e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 83.20 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 322 QVLIKHVDFQYanSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN--------IGFL 393
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTdlppkdrnIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 394 SQR----PHIfadSIKNNIA-------MYDDEIcDEQVIQVLDEVGLkEKVLSLKygiytsIGEggemLSGGQMRRIELS 462
Cdd:COG3839 81 FQSyalyPHM---TVYENIAfplklrkVPKAEI-DRRVREAAELLGL-EDLLDRK------PKQ----LSGGQRQRVALG 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488386603 463 RLLLLKPDIVIFDEPAIGLD----IETEKVIQQvLEHHFSTTTVF 503
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDaklrVEMRAEIKR-LHRRLGTTTIY 189
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
340-529 |
3.62e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.91 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIGFLSQR----------------PHIFAds 403
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlirqeagmvfqqfylfPHLTA-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 404 iKNNIAM-------YDDEICDEQVIQVLDEVGLKEKVlslkyGIYTSigeggeMLSGGQMRRIELSRLLLLKPDIVIFDE 476
Cdd:PRK09493 95 -LENVMFgplrvrgASKEEAEKQARELLAKVGLAERA-----HHYPS------ELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488386603 477 PAIGLDIETE----KVIQQVLEHHFsttTVFIIAHRDSTIRSSARR-IYIESGHLIKD 529
Cdd:PRK09493 163 PTSALDPELRhevlKVMQDLAEEGM---TMVIVTHEIGFAEKVASRlIFIDKGRIAED 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
340-496 |
4.07e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.92 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIGFLSQRPHIFA--DSIKNNI--------- 408
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGhrNAMKPALtvaenlefw 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 409 -AMYDDEicDEQVIQVLDEVGLKEkVLSLKYGiytsigeggeMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEK 487
Cdd:PRK13539 98 aAFLGGE--ELDIAAALEAVGLAP-LAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
....*....
gi 488386603 488 VIQQVLEHH 496
Cdd:PRK13539 165 LFAELIRAH 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
323-482 |
4.52e-17 |
|
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: 80.24 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 323 VLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL---------NIGFL 393
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrtdrkaarqSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 394 SQRPHIFAD-SIKNNIAMY------DDEICDEQVIQVLDEVGLKEKVLSLkygiytsIGEggemLSGGQMRRIELSRLLL 466
Cdd:cd03263 81 PQFDALFDElTVREHLRFYarlkglPKSEIKEEVELLLRVLGLTDKANKR-------ART----LSGGMKRKLSLAIALI 149
|
170
....*....|....*.
gi 488386603 467 LKPDIVIFDEPAIGLD 482
Cdd:cd03263 150 GGPSVLLLDEPTSGLD 165
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
340-489 |
5.75e-17 |
|
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: 84.96 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLsfnQASLNIGFLSQRPHIFADSIKNNIAM---YDDEic 416
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---KHSGRISFSPQTSWIMPGTIKDNIIFglsYDEY-- 516
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386603 417 deQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVI 489
Cdd:TIGR01271 517 --RYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
337-519 |
6.36e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.20 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 337 HMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSfNQASLNIGFLSQRPHI---FADSIKNNIAM--- 410
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR-RAGGARVAYVPQRSEVpdsLPLTVRDLVAMgrw 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 411 ----------YDDEicdEQVIQVLDEVGLKEkvLSLKygiytSIGEggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIG 480
Cdd:NF040873 84 arrglwrrltRDDR---AAVDDALERVGLAD--LAGR-----QLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488386603 481 LDIETEKVIQQVL-EHHFSTTTVFIIAHRDSTIRSSARRI 519
Cdd:NF040873 150 LDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
339-509 |
8.65e-17 |
|
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: 78.62 E-value: 8.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN------------IGFLSQRP--HIFADSI 404
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysrkgllerrqrVGLVFQDPddQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 405 KNNIA-------MYDDEICD--EQVIQVLDEVGLKEKVLSlkygiytsigeggeMLSGGQMRRIELSRLLLLKPDIVIFD 475
Cdd:TIGR01166 87 DQDVAfgplnlgLSEAEVERrvREALTAVGASGLRERPTH--------------CLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|....
gi 488386603 476 EPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRD 509
Cdd:TIGR01166 153 EPTAGLDPAGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
325-507 |
9.19e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.83 E-value: 9.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQY-ANS--NHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSF---------NQASL---- 388
Cdd:PRK13634 5 FQKVEHRYqYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkKNKKLkplr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 389 -NIGFLSQRP--HIFADSIKNNIAM------YDDEICDEQVIQVLDEVGLKEKVLSlkygiyTSIGEggemLSGGQMRRI 459
Cdd:PRK13634 85 kKVGIVFQFPehQLFEETVEKDICFgpmnfgVSEEDAKQKAREMIELVGLPEELLA------RSPFE----LSGGQMRRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488386603 460 ELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLE--HHFSTTTVFIIAH 507
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYklHKEKGLTTVLVTH 204
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
337-529 |
1.26e-16 |
|
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: 78.69 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 337 HMALkNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIGFLSQRP--------HIFAD-SIKNN 407
Cdd:cd03298 12 EQPM-HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPvsmlfqenNLFAHlTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 408 IA------MYDDEICDEQVIQVLDEVGLKEKVLSLKygiytsigeggEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGL 481
Cdd:cd03298 91 VGlglspgLKLTAEDRQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488386603 482 D-IETEKVIQQVLEHHFST-TTVFIIAHRDSTIRSSARR-IYIESGHLIKD 529
Cdd:cd03298 160 DpALRAEMLDLVLDLHAETkMTVLMVTHQPEDAKRLAQRvVFLDNGRIAAQ 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
327-504 |
1.86e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.35 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 327 HVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLniGFLSQRPH-------- 398
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL--AKLNRAQRkafrrdiq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 399 -IFADSIKN-NIAMYDDEICDE---------------QVIQVLDEVGLKEKVLSLKYGiytsigeggeMLSGGQMRRIEL 461
Cdd:PRK10419 93 mVFQDSISAvNPRKTVREIIREplrhllsldkaerlaRASEMLRAVDLDDSVLDKRPP----------QLSGGQLQRVCL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488386603 462 SRLLLLKPDIVIFDEPAIGLDIETE-KVIQQV--LEHHFSTTTVFI 504
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQaGVIRLLkkLQQQFGTACLFI 208
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
340-510 |
1.97e-16 |
|
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: 76.81 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASlNIGFLSQRPHIFADSIKnniamyddeicdEQ 419
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-DLLFLPQRPYLPLGTLR------------EQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 420 VIQVLDEVglkekvlslkygiytsigeggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFst 499
Cdd:cd03223 84 LIYPWDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG-- 138
|
170
....*....|.
gi 488386603 500 TTVFIIAHRDS 510
Cdd:cd03223 139 ITVISVGHRPS 149
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
340-483 |
2.13e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.05 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFLSQRPHI-FADSIKNNI 408
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwspaelarrRAVLPQHSSLsFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 409 AM-----YDDEICDEQVIQ-VLDEVGLkekvLSLKYGIYTSigeggemLSGGQMRRIELSRLL--LLKPD----IVIFDE 476
Cdd:PRK13548 98 AMgraphGLSRAEDDALVAaALAQVDL----AHLAGRDYPQ-------LSGGEQQRVQLARVLaqLWEPDgpprWLLLDE 166
|
....*..
gi 488386603 477 PAIGLDI 483
Cdd:PRK13548 167 PTSALDL 173
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
339-482 |
2.51e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 79.32 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-------QASLN-----IGFLSQRP--HIFADSI 404
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvditdkKVKLSdirkkVGLVFQYPeyQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 405 KNNIA-------MYDDEIcDEQVIQVLDEVGLKEKVLSLKygiytSIGEggemLSGGQMRRIELSRLLLLKPDIVIFDEP 477
Cdd:PRK13637 102 EKDIAfgpinlgLSEEEI-ENRVKRAMNIVGLDYEDYKDK-----SPFE----LSGGQKRRVAIAGVVAMEPKILILDEP 171
|
....*
gi 488386603 478 AIGLD 482
Cdd:PRK13637 172 TAGLD 176
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
339-532 |
2.63e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.58 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQ--ASL---NIGF---LSQRphifaDSIKNNIAM 410
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvSALlelGAGFhpeLTGR-----ENIYLNGRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 411 YDdeICDEQVIQVLDEV----GLkEKVLSLKYGIYTSiGeggemlsggqMRrielSRL-----LLLKPDIVIFDEpAIGL 481
Cdd:COG1134 116 LG--LSRKEIDEKFDEIvefaEL-GDFIDQPVKTYSS-G----------MR----ARLafavaTAVDPDILLVDE-VLAV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 482 -DIE----TEKVIQQVLEhhfSTTTVFIIAHRDSTIRSSARR-IYIESGHLIKDDSI 532
Cdd:COG1134 177 gDAAfqkkCLARIRELRE---SGRTVIFVSHSMGAVRRLCDRaIWLEKGRLVMDGDP 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
339-529 |
5.22e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.97 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN------------QASLNIGFLSQRP--------- 397
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktkeKEKVLEKLVIQKTrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 398 ---------------HIFADSIKNNIAM------YDDEICDEQVIQVLDEVGLKEKVLSlkygiyTSIGEggemLSGGQM 456
Cdd:PRK13651 102 eirrrvgvvfqfaeyQLFEQTIEKDIIFgpvsmgVSKEEAKKRAAKYIELVGLDESYLQ------RSPFE----LSGGQK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488386603 457 RRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEH-HFSTTTVFIIAHR-DSTIRSSARRIYIESGHLIKD 529
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDlDNVLEWTKRTIFFKDGKIIKD 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
339-494 |
5.26e-16 |
|
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: 80.88 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQsVTPTHGTLSFN-----------------------Q---ASLN--- 389
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDgqdldglsrralrplrrrmqvvfQdpfGSLSprm 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 ----I---GFLSQRPHIfadsiknniamyDDEICDEQVIQVLDEVGLKEKVLSlKYgiytsIGEggemLSGGQMRRIELS 462
Cdd:COG4172 380 tvgqIiaeGLRVHGPGL------------SAAERRARVAEALEEVGLDPAARH-RY-----PHE----FSGGQRQRIAIA 437
|
170 180 190
....*....|....*....|....*....|...
gi 488386603 463 RLLLLKPDIVIFDEPAIGLDieteKVIQ-QVLE 494
Cdd:COG4172 438 RALILEPKLLVLDEPTSALD----VSVQaQILD 466
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
324-512 |
6.33e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.06 E-value: 6.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 324 LIKHVDFQyANSNHMaLKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------NIGFL 393
Cdd:PRK10247 9 QLQNVGYL-AGDAKI-LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIstlkpeiyrqQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 394 SQRPHIFADSIKNNIAM---YDDEICDEQVIQV-LDEVGLKEKVLSlkygiyTSIGEggemLSGGQMRRIELSRLLLLKP 469
Cdd:PRK10247 87 AQTPTLFGDTVYDNLIFpwqIRNQQPDPAIFLDdLERFALPDTILT------KNIAE----LSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488386603 470 DIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFI---------IAHRDSTI 512
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwvthdkdeINHADKVI 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
330-495 |
6.76e-16 |
|
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: 76.64 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 330 FQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN---------QASLNIGFLSqrphif 400
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdvvkepaEARRRLGFVS------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 401 adsikNNIAMYDDEICDEQVIQVLDEVGLKE-------KVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVI 473
Cdd:cd03266 85 -----DSTGLYDRLTARENLEYFAGLYGLKGdeltarlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180
....*....|....*....|..
gi 488386603 474 FDEPAIGLDIETEKVIQQVLEH 495
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQ 181
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
321-529 |
9.07e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.82 E-value: 9.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 321 EQVLIKHVDFQYANS----NHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTL-------SFNQASLN 389
Cdd:PRK13633 3 EMIKCKNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtSDEENLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 I----GFLSQRP--HIFADSIKNNIA-------MYDDEIcDEQVIQVLDEVGLKEkvlslkYGIYTSigeggEMLSGGQM 456
Cdd:PRK13633 83 IrnkaGMVFQNPdnQIVATIVEEDVAfgpenlgIPPEEI-RERVDESLKKVGMYE------YRRHAP-----HLLSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 457 RRIELSRLLLLKPDIVIFDEPAIGLD----IETEKVIQQVLEHHfsTTTVFIIAHRDSTIRSSARRIYIESGHLIKD 529
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKY--GITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
325-535 |
9.44e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.58 E-value: 9.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVD--FQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-------------QASLN 389
Cdd:COG1135 4 LENLSktFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvdltalserelrAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 IGF-------LSQRphifadSIKNNIAM------YD-DEIcDEQVIQVLDEVGLKEKVLSlkygiYTSigeggeMLSGGQ 455
Cdd:COG1135 84 IGMifqhfnlLSSR------TVAENVALpleiagVPkAEI-RKRVAELLELVGLSDKADA-----YPS------QLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 456 MRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVL-----EHHfstTTVFIIAHRDSTIRSSARRI-YIESGHLIKD 529
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLkdinrELG---LTIVLITHEMDVVRRICDRVaVLENGRIVEQ 222
|
....*.
gi 488386603 530 DSIISV 535
Cdd:COG1135 223 GPVLDV 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
325-504 |
1.06e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 78.65 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANsnHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN----QASL-----NIGFLSQ 395
Cdd:COG1118 5 VRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgrdlFTNLpprerRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 396 R----PHIfadSIKNNIA-------MYDDEIcDEQVIQVLDEVGLkekvlslkygiytsigegGEM-------LSGGQMR 457
Cdd:COG1118 83 HyalfPHM---TVAENIAfglrvrpPSKAEI-RARVEELLELVQL------------------EGLadrypsqLSGGQRQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488386603 458 RIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVL-EHH--FSTTTVFI 504
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLrRLHdeLGGTTVFV 190
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
340-495 |
1.96e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.84 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQ-----------ASLNIGFLSQRPHIFAD-SIKNN 407
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithlpmhkrARLGIGYLPQEASIFRKlTVEDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 408 IAM------YDDEICDEQVIQVLDEVGLkEKVLSLKygiytsigegGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGL 481
Cdd:COG1137 99 ILAvlelrkLSKKEREERLEELLEEFGI-THLRKSK----------AYSLSGGERRRVEIARALATNPKFILLDEPFAGV 167
|
170
....*....|....*...
gi 488386603 482 D----IEtekvIQQVLEH 495
Cdd:COG1137 168 DpiavAD----IQKIIRH 181
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
339-494 |
2.17e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.37 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIG---FLSQRPH-IFADS----------- 403
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGdysYRSQRIRmIFQDPstslnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 404 ------IKNNIAMyDDEICDEQVIQVLDEVGLkekvLSLKYGIYTsigeggEMLSGGQMRRIELSRLLLLKPDIVIFDEP 477
Cdd:PRK15112 108 qildfpLRLNTDL-EPEQREKQIIETLRQVGL----LPDHASYYP------HMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170
....*....|....*...
gi 488386603 478 AIGLDIETE-KVIQQVLE 494
Cdd:PRK15112 177 LASLDMSMRsQLINLMLE 194
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
339-528 |
2.18e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.97 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQ------SVTPThGTLSFNQASL------------NIGFLSQRPHIF 400
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndlnpEVTIT-GSIVYNGHNIysprtdtvdlrkEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 401 ADSIKNNI-------AMYDDEICDEQVIQVLDEVGLKEKVlslKYGIYTS-IGeggemLSGGQMRRIELSRLLLLKPDIV 472
Cdd:PRK14239 99 PMSIYENVvyglrlkGIKDKQVLDEAVEKSLKGASIWDEV---KDRLHDSaLG-----LSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 473 IFDEPAIGLD-IETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIK 528
Cdd:PRK14239 171 LLDEPTSALDpISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIE 227
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
344-519 |
2.60e-15 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 74.90 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 344 SFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIGFLSQRP--------HIFAD-SIKNNIAM---- 410
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPvsmlfqenNLFAHlTVRQNIGLglhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 411 --YDDEICDEQVIQVLDEVGLKEKVLSLKygiytsigeggEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLD----IE 484
Cdd:TIGR01277 98 glKLNAEQQEKVVDAAQQVGIADYLDRLP-----------EQLSGGQRQRVALARCLVRPNPILLLDEPFSALDpllrEE 166
|
170 180 190
....*....|....*....|....*....|....*
gi 488386603 485 TEKVIQQVLEHHfsTTTVFIIAHRDSTIRSSARRI 519
Cdd:TIGR01277 167 MLALVKQLCSER--QRTLLMVTHHLSDARAIASQI 199
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
324-527 |
2.62e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 76.34 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 324 LIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-------------QASLNI 390
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDgenipamsrsrlyTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 391 GFLSQRPHIFAD-SIKNNIAM-------YDDEICDEQVIQVLDEVGLKekvlslkygiytsiGEGGEM---LSGGQMRRI 459
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVAYplrehtqLPAPLLHSTVMMKLEAVGLR--------------GAAKLMpseLSGGMARRA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386603 460 ELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQV---LEHHFSTTTVfIIAHRDSTIRSSARRIYIESGHLI 527
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLiseLNSALGVTCV-VVSHDVPEVLSIADHAYIVADKKI 222
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
342-496 |
2.99e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.46 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 342 NISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNigflSQRPHIFAD--------SIKN------N 407
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDEYHQDllylghqpGIKTeltaleN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 408 IAMY---DDEICDEQVIQVLDEVGLKekvlslkygiytsigeGGEM-----LSGGQMRRIELSRLLLLKPDIVIFDEPAI 479
Cdd:PRK13538 95 LRFYqrlHGPGDDEALWEALAQVGLA----------------GFEDvpvrqLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170
....*....|....*..
gi 488386603 480 GLDIETEKVIQQVLEHH 496
Cdd:PRK13538 159 AIDKQGVARLEALLAQH 175
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
325-507 |
3.37e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.93 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFLS 394
Cdd:PRK13647 7 VEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaenekwvrskVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 395 QRP--HIFADSIKNNIA-------MYDDEIcDEQVIQVLDEVGLKEKVLSLKYgiytsigeggeMLSGGQMRRIELSRLL 465
Cdd:PRK13647 86 QDPddQVFSSTVWDDVAfgpvnmgLDKDEV-ERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488386603 466 LLKPDIVIFDEPAIGLDIETEKVIQQVL-EHHFSTTTVFIIAH 507
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATH 196
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
339-504 |
3.98e-15 |
|
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: 75.07 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN--QAS------LNIGFLSQRPHIFAD-SIKNNIA 409
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgeDATdvpvqeRNVGFVFQHYALFRHmTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 410 M-----------YDDEIcDEQVIQVLDEVGLKEkvLSLKYgiytsigegGEMLSGGQMRRIELSRLLLLKPDIVIFDEPA 478
Cdd:cd03296 97 FglrvkprserpPEAEI-RAKVHELLKLVQLDW--LADRY---------PAQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180
....*....|....*....|....*....
gi 488386603 479 IGLDIETEKVIQQVLE--HH-FSTTTVFI 504
Cdd:cd03296 165 GALDAKVRKELRRWLRrlHDeLHVTTVFV 193
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
344-529 |
4.63e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.62 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 344 SFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIGFLSQRP--------HIFAD-SIKNNIA----- 409
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPvsmlfqenNLFSHlTVAQNIGlglnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 410 -MYDDEICDEQVIQVLDEVGLKEKVLSLKygiytsiGEggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLD----IE 484
Cdd:PRK10771 99 gLKLNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488386603 485 TEKVIQQVLEHHfsTTTVFIIAHR-DSTIRSSARRIYIESGHLIKD 529
Cdd:PRK10771 168 MLTLVSQVCQER--QLTLLMVSHSlEDAARIAPRSLVVADGRIAWD 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
328-512 |
4.74e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 78.67 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 328 VDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN--------------QASLnigfL 393
Cdd:PTZ00243 1314 VQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNgreigayglrelrrQFSM----I 1389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 394 SQRPHIFADSIKNNIAMYDdEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLK-PDIV 472
Cdd:PTZ00243 1390 PQDPVLFDGTVRQNVDPFL-EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFI 1468
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488386603 473 IFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTI 512
Cdd:PTZ00243 1469 LMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTV 1508
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
323-489 |
4.99e-15 |
|
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: 78.45 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 323 VLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQAslnIGFLSQRPHIFAD 402
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS---VAYVPQQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 403 SIKNNIaMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLD 482
Cdd:TIGR00957 714 SLRENI-LFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
....*..
gi 488386603 483 IETEKVI 489
Cdd:TIGR00957 793 AHVGKHI 799
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
339-527 |
5.83e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.54 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN--------------IGFLSQRP--HIFAD 402
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkeikpvrkkVGVVFQFPesQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 403 SIKNNIAM------YDDEICDEQVIQVLDEVGLKEKVLSlkygiytsigEGGEMLSGGQMRRIELSRLLLLKPDIVIFDE 476
Cdd:PRK13643 101 TVLKDVAFgpqnfgIPKEKAEKIAAEKLEMVGLADEFWE----------KSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488386603 477 PAIGLDIETEKVIQQVLEH-HFSTTTVFIIAHRDSTIRSSARRIY-IESGHLI 527
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYlLEKGHII 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
340-527 |
6.17e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.54 E-value: 6.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQ-----------ASLNIGFLSQRPHIFadsikNNI 408
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplharARRGIGYLPQEASIF-----RRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 409 AMYDDEICDEQVIQVLDEVGLKEKVLSL--KYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETE 486
Cdd:PRK10895 94 SVYDNLMAVLQIRDDLSAEQREDRANELmeEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488386603 487 KVIQQVLEH-HFSTTTVFIIAHRDSTIRSSARRIYIES-GHLI 527
Cdd:PRK10895 174 IDIKRIIEHlRDSGLGVLITDHNVRETLAVCERAYIVSqGHLI 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
323-490 |
6.44e-15 |
|
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: 74.20 E-value: 6.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 323 VLIKHVDFQYANSnhMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSF----------NQASLNIGF 392
Cdd:cd03300 1 IELENVSKFYGGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLdgkditnlppHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 393 LSQR--PHIfadSIKNNIA-------MYDDEIcDEQVIQVLDEVGLKEkvLSLKYgiytsIGEggemLSGGQMRRIELSR 463
Cdd:cd03300 79 QNYAlfPHL---TVFENIAfglrlkkLPKAEI-KERVAEALDLVQLEG--YANRK-----PSQ----LSGGQQQRVAIAR 143
|
170 180
....*....|....*....|....*..
gi 488386603 464 LLLLKPDIVIFDEPAIGLDIETEKVIQ 490
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQ 170
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
325-529 |
6.85e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.13 E-value: 6.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHM-ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFL 393
Cdd:PRK13642 7 VENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaenvwnlrrkIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 394 SQRP--HIFADSIKNNIA--MYDDEICDEQVIQVLDEVGLKEKVLSLKygiytsiGEGGEMLSGGQMRRIELSRLLLLKP 469
Cdd:PRK13642 87 FQNPdnQFVGATVEDDVAfgMENQGIPREEMIKRVDEALLAVNMLDFK-------TREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386603 470 DIVIFDEPAIGLD----IETEKVIQQVLEHHFstTTVFIIAHRDSTIRSSARRIYIESGHLIKD 529
Cdd:PRK13642 160 EIIILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
329-495 |
7.28e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 73.67 E-value: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 329 DFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTP---THGTLSFNQASLN--------IGFLSQRP 397
Cdd:COG4136 6 NLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTalpaeqrrIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 398 HIFAD-SIKNNIAM-----YDDEICDEQVIQVLDEVGLKekvlslkyGIYTS-IGEggemLSGGQMRRIELSRLLLLKPD 470
Cdd:COG4136 86 LLFPHlSVGENLAFalpptIGRAQRRARVEQALEEAGLA--------GFADRdPAT----LSGGQRARVALLRALLAEPR 153
|
170 180
....*....|....*....|....*.
gi 488386603 471 IVIFDEPAIGLDIE-TEKVIQQVLEH 495
Cdd:COG4136 154 ALLLDEPFSKLDAAlRAQFREFVFEQ 179
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
340-483 |
8.19e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 74.38 E-value: 8.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFLSQRPHI-FADSIKNNI 408
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawspwelarrRAVLPQHSSLaFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 409 AM------YDDEICDEQVIQVLDEVGLkekvLSLKYGIYTSigeggemLSGGQMRRIELSRLL--LLKPD-----IVIFD 475
Cdd:COG4559 97 ALgraphgSSAAQDRQIVREALALVGL----AHLAGRSYQT-------LSGGEQQRVQLARVLaqLWEPVdggprWLFLD 165
|
....*...
gi 488386603 476 EPAIGLDI 483
Cdd:COG4559 166 EPTSALDL 173
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
339-481 |
1.38e-14 |
|
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: 73.48 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN-----------IGFLSQRPHIFAD-SIKN 406
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITglpphriarlgIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 407 NIAM----YDDeicDEQVIQVLDEVG-----LKEKvlslkygiytsIGEGGEMLSGG--QMrrIELSRLLLLKPDIVIFD 475
Cdd:COG0410 98 NLLLgayaRRD---RAEVRADLERVYelfprLKER-----------RRQRAGTLSGGeqQM--LAIGRALMSRPKLLLLD 161
|
....*.
gi 488386603 476 EPAIGL 481
Cdd:COG0410 162 EPSLGL 167
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
57-245 |
1.63e-14 |
|
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: 74.12 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 57 VIFISLILRATFNMLIQFLGDHLAFKVKHMLREQV---ILKKSVR-----SIGEEINILTESIDGIGPFFQSYLPQVFKS 128
Cdd:cd07346 44 LLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLfrhLQRLSLSffdrnRTGDLMSRLTSDVDAVQNLVSSGLLQLLSD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 129 MLIPIVIIITMCFVHLPTAIIMIVTAPFIPLFYVIFGLKTRDESKDQMTYLNQFSQRFLNTAKGLITFKLLNQTKQSEQQ 208
Cdd:cd07346 124 VLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIER 203
|
170 180 190
....*....|....*....|....*....|....*..
gi 488386603 209 LYKDSTRFRDLTMRILKSAFLSGLMLEFISMLGIGLV 245
Cdd:cd07346 204 FREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
337-528 |
2.08e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 73.25 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 337 HMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN------------------IGFLSQRPH 398
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarslsqqkglirqlrqhVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 399 IFAD-SIKNNIAmyddeicdEQVIQVLDEVglKEKVLSLKYGIYTSIGEGGE------MLSGGQMRRIELSRLLLLKPDI 471
Cdd:PRK11264 96 LFPHrTVLENII--------EGPVIVKGEP--KEEATARARELLAKVGLAGKetsyprRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386603 472 VIFDEPAIGLDI----ETEKVIQQVLEHHfstTTVFIIAHRDSTIRSSARR-IYIESGHLIK 528
Cdd:PRK11264 166 ILFDEPTSALDPelvgEVLNTIRQLAQEK---RTMVIVTHEMSFARDVADRaIFMDQGRIVE 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
339-539 |
3.00e-14 |
|
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: 73.06 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQ---ASLN-----------IGFLSQR----PHIf 400
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiAAMSrkelrelrrkkISMVFQSfallPHR- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 401 adSIKNNIAM------YDDEICDEQVIQVLDEVGLKekvlslKYGiYTSIGEggemLSGGQMRRIELSRLLLLKPDIVIF 474
Cdd:cd03294 118 --TVLENVAFglevqgVPRAEREERAAEALELVGLE------GWE-HKYPDE----LSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386603 475 DEPAIGLD--IETEkvIQQVL-----EHHfsTTTVFIIAHRDSTIRsSARRIYIesghlIKDDSIISVTRSE 539
Cdd:cd03294 185 DEAFSALDplIRRE--MQDELlrlqaELQ--KTIVFITHDLDEALR-LGDRIAI-----MKDGRLVQVGTPE 246
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
340-541 |
3.23e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.53 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSF---NQASLN-----------IGFLSQRPHIFAD-SI 404
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVagqDVATLDadalaqlrrehFGFIFQRYHLLSHlTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 405 KNNI---AMY---DDEICDEQVIQVLDEVGLKEKVlslkygiytsiGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPA 478
Cdd:PRK10535 104 AQNVevpAVYaglERKQRLLRAQELLQRLGLEDRV-----------EYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386603 479 IGLD----IETEKVIQQVLEH-HfsttTVFIIAHrDSTIRSSARRIyIEsghlIKDDSIISVTRSEVK 541
Cdd:PRK10535 173 GALDshsgEEVMAILHQLRDRgH----TVIIVTH-DPQVAAQAERV-IE----IRDGEIVRNPPAQEK 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
337-530 |
3.57e-14 |
|
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: 71.79 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 337 HMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQA-----SLNIGF---LSQRphifaDSIKNNI 408
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssllGLGGGFnpeLTGR-----ENIYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 409 AMYDdeICDEQVIQVLDEV----GLkEKVLSLKYGIYTSigeggemlsgGQMRRIELSRLLLLKPDIVIFDEP-AIGlDI 483
Cdd:cd03220 110 RLLG--LSRKEIDEKIDEIiefsEL-GDFIDLPVKTYSS----------GMKARLAFAIATALEPDILLIDEVlAVG-DA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488386603 484 ETEKVIQQVLEHHFSTTTVFIIA-HRDSTIRSSARR-IYIESGHLIKDD 530
Cdd:cd03220 176 AFQEKCQRRLRELLKQGKTVILVsHDPSSIKRLCDRaLVLEKGKIRFDG 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
335-493 |
4.81e-14 |
|
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: 70.54 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 335 SNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIGflsqRPHifaDSIKNNIAMydde 414
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR----SPR---DAIRAGIAY---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 415 icdeqviqVLDE---VGLkekVLSLkygiytSIGE---GGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKV 488
Cdd:cd03215 80 --------VPEDrkrEGL---VLDL------SVAEniaLSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
....*
gi 488386603 489 IQQVL 493
Cdd:cd03215 143 IYRLI 147
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
337-494 |
4.83e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.50 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 337 HMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN--------------IGFLSQRP--HIF 400
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkyirpvrkrIGMVFQFPesQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 401 ADSIK-------NNIAMYDDEIcDEQVIQVLDEVGLKEKVLSLKygiytsigegGEMLSGGQMRRIELSRLLLLKPDIVI 473
Cdd:PRK13646 100 EDTVEreiifgpKNFKMNLDEV-KNYAHRLLMDLGFSRDVMSQS----------PFQMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180
....*....|....*....|.
gi 488386603 474 FDEPAIGLDIETEkviQQVLE 494
Cdd:PRK13646 169 LDEPTAGLDPQSK---RQVMR 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
322-515 |
5.41e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.45 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 322 QVLIKHVDFQYANSNHMAL-KNISFSVNKGEKVAIVGPSGAGKSTLAKLL------------------------------ 370
Cdd:PTZ00265 1165 KIEIMDVNFRYISRPNVPIyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 371 --------------SQSVTPTHGTLS--FNQAS------LNI------------GFLSQRPHIFADSIKNNIAMYDDEIC 416
Cdd:PTZ00265 1245 deeqnvgmknvnefSLTKEGGSGEDStvFKNSGkilldgVDIcdynlkdlrnlfSIVSQEPMLFNMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 417 DEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLE-- 494
Cdd:PTZ00265 1325 REDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdi 1404
|
250 260
....*....|....*....|.
gi 488386603 495 HHFSTTTVFIIAHRDSTIRSS 515
Cdd:PTZ00265 1405 KDKADKTIITIAHRIASIKRS 1425
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
340-507 |
6.47e-14 |
|
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: 74.20 E-value: 6.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTlSFNQASLNIGFLSQRPHIFAD-SIKNNIAMYDDEICDe 418
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE-ARPQPGIKVGYLPQEPQLDPTkTVRENVEEGVAEIKD- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 419 qVIQVLDEVglkekvlSLKYGIYTS-----IGEGGEM----------------------------------LSGGQMRRI 459
Cdd:TIGR03719 99 -ALDRFNEI-------SAKYAEPDAdfdklAAEQAELqeiidaadawdldsqleiamdalrcppwdadvtkLSGGERRRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488386603 460 ELSRLLLLKPDIVIFDEPAIGLDIETekviqqV--LEHHFS--TTTVFIIAH 507
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDAES------VawLERHLQeyPGTVVAVTH 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
337-508 |
7.67e-14 |
|
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: 70.77 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 337 HMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLnigflsqrphifADSIKNNIA------- 409
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL------------DIAARNRIGylpeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 410 MYDDEICDEQVIQVLDEVGLKEK-----VLSL--KYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLD 482
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEearrrIDEWleRLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180
....*....|....*....|....*..
gi 488386603 483 -IETEKVIQQVLEHHFSTTTVFIIAHR 508
Cdd:cd03269 161 pVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
336-482 |
8.25e-14 |
|
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: 70.75 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 336 NHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQ--------ASLNIGFLSQR----PHIfadS 403
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppKDRDIAMVFQNyalyPHM---T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 404 IKNNIA-------MYDDEIcDEQVIQVLDEVGLkEKVLSLKygiytsigegGEMLSGGQMRRIELSRLLLLKPDIVIFDE 476
Cdd:cd03301 89 VYDNIAfglklrkVPKDEI-DERVREVAELLQI-EHLLDRK----------PKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
....*.
gi 488386603 477 PAIGLD 482
Cdd:cd03301 157 PLSNLD 162
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
335-519 |
1.00e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.83 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 335 SNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQaSLNIGFLSQRP------HIF-------- 400
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLIVARLQQDPprnvegTVYdfvaegie 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 401 --ADSIKNNIAMYDDEICD---------EQVIQVLDEVGL-------KEKVLSLKYGIYTSIGEggemLSGGQMRRIELS 462
Cdd:PRK11147 93 eqAEYLKRYHDISHLVETDpseknlnelAKLQEQLDHHNLwqlenriNEVLAQLGLDPDAALSS----LSGGWLRKAALG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 463 RLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEhHFSTTTVFiIAHRDSTIRSSARRI 519
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLK-TFQGSIIF-ISHDRSFIRNMATRI 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
340-504 |
1.40e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.04 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL--------NIGFLSQRPHIFAD-SIKNNIAM 410
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsrlhardrKVGFVFQHYALFRHmTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 411 ----------YDDEICDEQVIQVLDEVGLKEkvLSLKYgiytsigegGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIG 480
Cdd:PRK10851 98 gltvlprrerPNAAAIKAKVTQLLEMVQLAH--LADRY---------PAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180
....*....|....*....|....*..
gi 488386603 481 LDIETEKVIQ---QVLEHHFSTTTVFI 504
Cdd:PRK10851 167 LDAQVRKELRrwlRQLHEELKFTSVFV 193
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
325-533 |
1.43e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.42 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL------------NIGF 392
Cdd:PRK13636 8 VEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrkglmklreSVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 393 LSQRP--HIFADSIKN-------NIAMYDDEIcDEQVIQVLDEVG---LKEKVLslkygiytsigeggEMLSGGQMRRIE 460
Cdd:PRK13636 87 VFQDPdnQLFSASVYQdvsfgavNLKLPEDEV-RKRVDNALKRTGiehLKDKPT--------------HCLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386603 461 LSRLLLLKPDIVIFDEPAIGLD-IETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSsarrIYIESGHLIKDDSII 533
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKELGLTIIIATHDIDIVP----LYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
339-528 |
1.49e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.81 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLS--------------------------FNQASLNIGF 392
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiyigdkknnhelitnpyskkiknFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 393 LSQRP--HIFADSIKNNIaMY-------DDEICDEQVIQVLDEVGLKEKVLSLK-YGiytsigeggemLSGGQMRRIELS 462
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDI-MFgpvalgvKKSEAKKLAKFYLNKMGLDDSYLERSpFG-----------LSGGQKRRVAIA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386603 463 RLLLLKPDIVIFDEPAIGLDIETEK-VIQQVLEHHFSTTTVFIIAHR-DSTIRSSARRIYIESGHLIK 528
Cdd:PRK13631 189 GILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTmEHVLEVADEVIVMDKGKILK 256
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
340-508 |
1.68e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 73.66 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLsfnQASLNIGFLSQRPHIFADSIKNNIAMYDDEicDEQ 419
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---WAERSIAYVPQQAWIMNATVRGNILFFDEE--DAA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 420 VIQVLDEVG-LKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIET-EKVIQQVLEHHF 497
Cdd:PTZ00243 751 RLADAVRVSqLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVEECFLGAL 830
|
170
....*....|.
gi 488386603 498 STTTVFIIAHR 508
Cdd:PTZ00243 831 AGKTRVLATHQ 841
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
340-489 |
2.27e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.60 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIGflSQRPHIFADSIKNNIAmyddeicdeQ 419
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFG--REASLIDAIGRKGDFK---------D 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 420 VIQVLDEVGLKEKVLSLKygiytSIGEggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVI 489
Cdd:COG2401 115 AVELLNAVGLSDAVLWLR-----RFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
325-507 |
2.78e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.07 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLS-----QSVTPTHGTLSF------------NQAS 387
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmnelESEVRVEGRVEFfnqniyerrvnlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 388 LNIGFLSQRPHIFADSIKNNIAmYDDEICDEQVIQVLD---EVGLKEKVL--SLKYGIYTSIGEggemLSGGQMRRIELS 462
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVA-YGVKIVGWRPKLEIDdivESALKDADLwdEIKHKIHKSALD----LSGGQQQRLCIA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488386603 463 RLLLLKPDIVIFDEPAIGLD----IETEKVIQQVLEHhfSTTTVFIIAH 507
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSH 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
340-507 |
3.45e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.07 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTlSFNQASLNIGFLSQRPHI-------------FADsIKN 406
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-ARPAPGIKVGYLPQEPQLdpektvrenveegVAE-VKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 407 NIAMYD-------------DEICDEQ-----VIQVLDEVGLKEKVlslkygiytsigeggEM----------------LS 452
Cdd:PRK11819 101 ALDRFNeiyaayaepdadfDALAAEQgelqeIIDAADAWDLDSQL---------------EIamdalrcppwdakvtkLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488386603 453 GGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETekviqqV--LEHHFST--TTVFIIAH 507
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAES------VawLEQFLHDypGTVVAVTH 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
330-521 |
3.80e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 69.83 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 330 FQYANSNHmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTL----------SFNQASLNIGFLSQRP-- 397
Cdd:PRK13652 11 YSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitkeNIREVRKFVGLVFQNPdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 398 HIFADSIKNNIAM------YDDEICDEQVIQVLDEVGLKEKVLSLKYgiytsigeggeMLSGGQMRRIELSRLLLLKPDI 471
Cdd:PRK13652 90 QIFSPTVEQDIAFgpinlgLDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488386603 472 VIFDEPAIGLDIETEKVIQQVLEHHFST--TTVFIIAHRDSTIRSSARRIYI 521
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYV 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
339-477 |
3.89e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.60 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIGflsqRPhifADSIKNNIAMyddeicde 418
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIR----SP---RDAIALGIGM-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 419 qVIQ------------------------VLDEVGLKEKV--LSLKYGI----YTSIGEggemLSGGQMRRIELSRLLLLK 468
Cdd:COG3845 85 -VHQhfmlvpnltvaenivlgleptkggRLDRKAARARIreLSERYGLdvdpDAKVED----LSVGEQQRVEILKALYRG 159
|
....*....
gi 488386603 469 PDIVIFDEP 477
Cdd:COG3845 160 ARILILDEP 168
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
307-482 |
4.00e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.02 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 307 KADSPTLKVDEqqfeqvLIKHVDFQyansnhMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-- 384
Cdd:PRK11607 14 KALTPLLEIRN------LTKSFDGQ------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 385 --------QASLNIGFLSQR--PHIfadSIKNNIA-------MYDDEICDeQVIQVLDEVGLKEKVlslkygiytsiGEG 447
Cdd:PRK11607 82 dlshvppyQRPINMMFQSYAlfPHM---TVEQNIAfglkqdkLPKAEIAS-RVNEMLGLVHMQEFA-----------KRK 146
|
170 180 190
....*....|....*....|....*....|....*
gi 488386603 448 GEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLD 482
Cdd:PRK11607 147 PHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
339-509 |
4.41e-13 |
|
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: 71.76 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSF-----------------NQASLNIGFLSQR----P 397
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgrGRAKRYIGILHQEydlyP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 398 H-IFADSIKNNIAM-YDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSigeggeMLSGGQMRRIELSRLLLLKPDIVIFD 475
Cdd:TIGR03269 379 HrTVLDNLTEAIGLeLPDELARMKAVITLKMVGFDEEKAEEILDKYPD------ELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190
....*....|....*....|....*....|....*
gi 488386603 476 EPAIGLD-IETEKVIQQVLEHHFSTTTVFIIAHRD 509
Cdd:TIGR03269 453 EPTGTMDpITKVDVTHSILKAREEMEQTFIIVSHD 487
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
325-543 |
4.83e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.83 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANsnHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSF---------NQASLNIGFLSQ 395
Cdd:PRK13537 10 FRNVEKRYGD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepvpsraRHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 396 RPHIFAD-SIKNNIAMY------DDEICDEQVIQVLDEVGLKEKVLSlkygiytSIGEggemLSGGQMRRIELSRLLLLK 468
Cdd:PRK13537 88 FDNLDPDfTVRENLLVFgryfglSAAAARALVPPLLEFAKLENKADA-------KVGE----LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 469 PDIVIFDEPAIGLDIETEKVIQQVLEHHFST-TTVFIIAH-RDSTIRSSARRIYIESGHLIKDDSIISVTRSEVKID 543
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHfMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCD 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
325-527 |
5.18e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.63 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTL------SFNQASLN-----IGFL 393
Cdd:PRK13644 4 LENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidTGDFSKLQgirklVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 394 SQRP--HIFADSIKNNIAMYDDEIC------DEQVIQVLDEVGLKekvlslKYGIYTSigeggEMLSGGQMRRIELSRLL 465
Cdd:PRK13644 83 FQNPetQFVGRTVEEDLAFGPENLClppieiRKRVDRALAEIGLE------KYRHRSP-----KTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386603 466 LLKPDIVIFDEPAIGLDIET-EKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLI 527
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
339-526 |
5.42e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.36 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN-------------IGFLSQRPHIFAD-SI 404
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrevpflrrqIGMIFQDHHLLMDrTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 405 KNNIAM------YDDEICDEQVIQVLDEVGLKEKVLSlkYGIytsigeggeMLSGGQMRRIELSRLLLLKPDIVIFDEPA 478
Cdd:PRK10908 97 YDNVAIpliiagASGDDIRRRVSAALDKVGLLDKAKN--FPI---------QLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488386603 479 IGLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTI--RSSARRIYIESGHL 526
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLisRRSYRMLTLSDGHL 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-528 |
6.05e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.92 E-value: 6.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------------NIGFLSQRPHIFAD- 402
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifqidaiklrkEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 403 SIKNNIA--MYDDEICDEQVIQVLDEVGLKEkvLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIG 480
Cdd:PRK14246 106 SIYDNIAypLKSHGIKEKREIKKIVEECLRK--VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488386603 481 LDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRI-YIESGHLIK 528
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVaFLYNGELVE 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
339-477 |
6.99e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.82 E-value: 6.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN---------QASLN--IGFLSQRPHIFAD-SIKN 406
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgepvrfrspRDAQAagIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 407 NIAM---------YDDEICDEQVIQVLDEVGLKEKVlslkygiYTSIGEggemLSGGQMRRIELSRLLLLKPDIVIFDEP 477
Cdd:COG1129 99 NIFLgreprrgglIDWRAMRRRARELLARLGLDIDP-------DTPVGD----LSVAQQQLVEIARALSRDARVLILDEP 167
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
325-507 |
9.34e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 68.35 E-value: 9.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSN--HMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNiGFLSQRPHIFAD 402
Cdd:COG4525 6 VRHVSVRYPGGGqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT-GPGADRGVVFQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 403 -------SIKNNIAM------YDDEICDEQVIQVLDEVGLKEkvlslkYG---IYTsigeggemLSGGQMRRIELSRLLL 466
Cdd:COG4525 85 dallpwlNVLDNVAFglrlrgVPKAERRARAEELLALVGLAD------FArrrIWQ--------LSGGMRQRVGIARALA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488386603 467 LKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTT--TVFIIAH 507
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITH 193
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
340-507 |
1.01e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.13 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLS--QSVTPTHGTLSFNQASLNIGFLSQRPH--IF--------------A 401
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEPEERAHlgIFlafqypieipgvsnA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 402 DSIK-----NNIAMYDDEICDEQVIQVLDE----VGLKEKVLSlkygiyTSIGEGgemLSGGQMRRIELSRLLLLKPDIV 472
Cdd:CHL00131 103 DFLRlaynsKRKFQGLPELDPLEFLEIINEklklVGMDPSFLS------RNVNEG---FSGGEKKRNEILQMALLDSELA 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 488386603 473 IFDEPAIGLDIETEKVIQQVLeHHFSTTT--VFIIAH 507
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGI-NKLMTSEnsIILITH 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
325-507 |
1.12e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.19 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNhmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNiGFLSQRPHIFAD-- 402
Cdd:PRK11248 4 ISHLYADYGGKP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-GPGAERGVVFQNeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 403 -----SIKNNIAM------YDDEICDEQVIQVLDEVGLkekvlslkygiytsigEGGE-----MLSGGQMRRIELSRLLL 466
Cdd:PRK11248 81 llpwrNVQDNVAFglqlagVEKMQRLEIAHQMLKKVGL----------------EGAEkryiwQLSGGQRQRVGIARALA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488386603 467 LKPDIVIFDEPAIGLDIETEKVIQQVLEH--HFSTTTVFIIAH 507
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
309-493 |
1.52e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 309 DSPTLKVDEQQ--FEqvlIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKST--LAKLlsqSVTPTHGTLSFN 384
Cdd:PRK15134 272 ASPLLDVEQLQvaFP---IRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtgLALL---RLINSQGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 385 QASLN-------------IGFLSQRPH-----------IFADSIKNNIAMYDDEICDEQVIQVLDEVGLkEKVLSLKYGi 440
Cdd:PRK15134 346 GQPLHnlnrrqllpvrhrIQVVFQDPNsslnprlnvlqIIEEGLRVHQPTLSAAQREQQVIAVMEEVGL-DPETRHRYP- 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488386603 441 ytsiGEggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVL 493
Cdd:PRK15134 424 ----AE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALL 468
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
327-520 |
1.82e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.51 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 327 HVDFQYanSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFnqaslnigflsqrphiFADSIKN 406
Cdd:PRK13540 6 ELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILF----------------ERQSIKK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 407 NIAMYDDEICdeqviqvldEVGLKEKV---LSLK----YGIYTSIGEGG------------------EMLSGGQMRRIEL 461
Cdd:PRK13540 68 DLCTYQKQLC---------FVGHRSGInpyLTLRenclYDIHFSPGAVGitelcrlfslehlidypcGLLSSGQKRQVAL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 462 SRLLLLKPDIVIFDEPAIGLD-IETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIY 520
Cdd:PRK13540 139 LRLWMSKAKLWLLDEPLVALDeLSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKADYEEY 198
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
322-531 |
2.51e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.35 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 322 QVLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQAslnIGFLSQRPHIFA 401
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIEL---LGRTVQREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 402 DSIKNNIAMYDdeiCDEQVIQVLDEVGLKEKVLSLKYG----------------------IYTSIG------EGGEMLSG 453
Cdd:PRK09984 79 RDIRKSRANTG---YIFQQFNLVNRLSVLENVLIGALGstpfwrtcfswftreqkqralqALTRVGmvhfahQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 454 GQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLE--HHFSTTTVFIIAHR-DSTIRSSARRIYIESGHLIKDD 530
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQvDYALRYCERIVALRQGHVFYDG 235
|
.
gi 488386603 531 S 531
Cdd:PRK09984 236 S 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
338-521 |
2.69e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.94 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 338 MALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------------------------- 388
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvrtfqhvrlfremtvi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 389 -NIgFLSQRPH----IFADSIKNNIAMYDDEICDEQVIQVLDEVGLKEkvlslkygiyTSIGEGGEmLSGGQMRRIELSR 463
Cdd:PRK11300 99 eNL-LVAQHQQlktgLFSGLLKTPAFRRAESEALDRAATWLERVGLLE----------HANRQAGN-LAYGQQRRLEIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386603 464 LLLLKPDIVIFDEPAIGLD----IETEKVIQQVLEHHfsTTTVFIIAHRDSTIRSSARRIYI 521
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNpketKELDELIAELRNEH--NVTVLLIEHDMKLVMGISDRIYV 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
340-507 |
4.27e-12 |
|
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: 65.95 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNqaslniGFLSQRPH-----IFAD-------SIKNN 407
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILE------GKQITEPGpdrmvVFQNysllpwlTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 408 IAMYDDEIC-------DEQVI-QVLDEVGLKEKVlslkygiYTSIGEggemLSGGQMRRIELSRLLLLKPDIVIFDEPAI 479
Cdd:TIGR01184 75 IALAVDRVLpdlskseRRAIVeEHIALVGLTEAA-------DKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190
....*....|....*....|....*....|...
gi 488386603 480 GLDIET-----EKVIQQVLEHHfstTTVFIIAH 507
Cdd:TIGR01184 144 ALDALTrgnlqEELMQIWEEHR---VTVLMVTH 173
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
339-528 |
4.73e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 66.69 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN--------------IGFLSQRP--HIFAD 402
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkdikqirkkVGLVFQFPesQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 403 SIKNNIAMYDDEIcdeQVIQVLDEVGLKEKVLSLkyGIYTSIGEGGEM-LSGGQMRRIELSRLLLLKPDIVIFDEPAIGL 481
Cdd:PRK13649 102 TVLKDVAFGPQNF---GVSQEEAEALAREKLALV--GISESLFEKNPFeLSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488386603 482 DIETEKVIQQVLEH-HFSTTTVFIIAHRDSTIRSSARRIYI-ESGHLIK 528
Cdd:PRK13649 177 DPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVlEKGKLVL 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
313-507 |
5.55e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.44 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 313 LKVDEQQ------FEqvlIKHVDFQYANSNhmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGtlsfnqa 386
Cdd:PRK11147 307 MQVEEASrsgkivFE---MENVNYQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG------- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 387 SLNIGflsqrphifadsIKNNIAMYDD--EICDEQViQVLDEV----------GLKEKVLSlkygiY------------T 442
Cdd:PRK11147 375 RIHCG------------TKLEVAYFDQhrAELDPEK-TVMDNLaegkqevmvnGRPRHVLG-----YlqdflfhpkramT 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 443 SIgeggEMLSGGQMRRIELSRlLLLKP-DIVIFDEPAIGLDIETEKVIQQVLEHHfsTTTVFIIAH 507
Cdd:PRK11147 437 PV----KALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETLELLEELLDSY--QGTVLLVSH 495
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
355-531 |
6.04e-12 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 66.75 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 355 IVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN--------IGFLSQR----PHIfadSIKNNIAM------YDDEIC 416
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTnvpphlrhINMVFQSyalfPHM---TVEENVAFglkmrkVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 417 DEQVIQVLDEVGLKEkvlslkYGIYTSIgeggeMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQ---VL 493
Cdd:TIGR01187 78 KPRVLEALRLVQLEE------FADRKPH-----QLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLelkTI 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 488386603 494 EHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDS 531
Cdd:TIGR01187 147 QEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
323-544 |
6.67e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 66.36 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 323 VLIKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTP--------THGTLSFNQASL-----N 389
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskiTVDGITLTAKTVwdireK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 390 IGFLSQRP--HIFADSIKNNIA--MYDDEICDEQVI----QVLDEVGLkekvlsLKYgiytsIGEGGEMLSGGQMRRIEL 461
Cdd:PRK13640 86 VGIVFQNPdnQFVGATVGDDVAfgLENRAVPRPEMIkivrDVLADVGM------LDY-----IDSEPANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 462 SRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEH--HFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDSIISVTRSE 539
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
....*
gi 488386603 540 VKIDQ 544
Cdd:PRK13640 235 EMLKE 239
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
335-491 |
7.42e-12 |
|
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: 65.04 E-value: 7.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 335 SNHMALKNISFSVNKGEKVAIVGPSGAGKSTL------------AKLLSQSVTPTHGTLSFNQAS--LNIGFLSQRPHIF 400
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLllailgemqtleGKVHWSNKNESEPSFEATRSRnrYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 401 ADSIKNNIaMYDDEICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIG 480
Cdd:cd03290 92 NATVEENI-TFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170
....*....|.
gi 488386603 481 LDIETEKVIQQ 491
Cdd:cd03290 171 LDIHLSDHLMQ 181
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
337-524 |
8.69e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 8.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 337 HMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNI-----GFLSQRPHIFADSIKNNIAMY 411
Cdd:PRK10619 18 HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdGQLKVADKNQLRLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 412 DD-----------EICDEQVIQVLDEVGLKEKVLSLKYGIYTSIGEGGEM-----LSGGQMRRIELSRLLLLKPDIVIFD 475
Cdd:PRK10619 98 FQhfnlwshmtvlENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkypvhLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488386603 476 EPAIGLDI----ETEKVIQQVLEHhfsTTTVFIIAHRDSTIRS-SARRIYIESG 524
Cdd:PRK10619 178 EPTSALDPelvgEVLRIMQQLAEE---GKTMVVVTHEMGFARHvSSHVIFLHQG 228
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
341-523 |
9.25e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 67.58 E-value: 9.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 341 KNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLsFNQASLNIGFLSQRpHIFADSIKNNIAMYDDEI---CD 417
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKVRMAVFSQH-HVDGLDLSSNPLLYMMRCfpgVP 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 418 EQVIQV-LDEVGLKEKvLSLKyGIYTsigeggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIE-TEKVIQQVLeh 495
Cdd:PLN03073 604 EQKLRAhLGSFGVTGN-LALQ-PMYT--------LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDaVEALIQGLV-- 671
|
170 180
....*....|....*....|....*...
gi 488386603 496 hFSTTTVFIIAHRDSTIRSSARRIYIES 523
Cdd:PLN03073 672 -LFQGGVLMVSHDEHLISGSVDELWVVS 698
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
343-513 |
9.89e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 67.47 E-value: 9.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 343 ISFSVNKGEKVAIVGPSGAGKSTLAKLLSQsVTPTHGTLSFNQASLNIGFLSQRPH----------IFADSIKNniaMYD 412
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYGGRLTKPAKGKLFYVPQRPYmtlgtlrdqiIYPDSSED---MKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 413 DEICDEQVIQVLDEVGLkEKVLSLKYGiYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDE--PAIGLDIEtEKVIQ 490
Cdd:TIGR00954 547 RGLSDKDLEQILDNVQL-THILEREGG-WSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDEctSAVSVDVE-GYMYR 623
|
170 180
....*....|....*....|...
gi 488386603 491 QVLEHHFsttTVFIIAHRDSTIR 513
Cdd:TIGR00954 624 LCREFGI---TLFSVSHRKSLWK 643
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
339-541 |
1.10e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-----------QASLNIGFLSQRPHIFAD-SIKN 406
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINninynkldhklAAQLGIGIIYQELSVIDElTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 407 NiaMYDDEICDEQV--IQVLD--EVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGL- 481
Cdd:PRK09700 100 N--LYIGRHLTKKVcgVNIIDwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLt 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 482 DIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRIYIesghlIKDDSiiSVTRSEVK 541
Cdd:PRK09700 178 NKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTV-----MKDGS--SVCSGMVS 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
339-535 |
1.17e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.13 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLS--QSVTPTHGTLSFNQA--------------------------SLNI 390
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmDQYEPTSGRIIYHVAlcekcgyverpskvgepcpvcggtlePEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 391 GFLSQRPHIFADSIKNN-------IAMYDDEICDEQVIQVLDEVGLK-EKVLSLKYGIYTSIGEGGEM------LSGGQM 456
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIaimlqrtFALYGDDTVLDNVLEALEEIGYEgKEAVGRAVDLIEMVQLSHRIthiardLSGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 457 RRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHF--STTTVFIIAHRDSTIRS-SARRIYIESGHLIKD---D 530
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIWLENGEIKEEgtpD 254
|
....*
gi 488386603 531 SIISV 535
Cdd:TIGR03269 255 EVVAV 259
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
325-499 |
1.29e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 65.52 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANsnHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN------IGFLsqrP- 397
Cdd:COG4152 4 LKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDpedrrrIGYL---Pe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 398 ------------HI--FAdSIKNniaMYDDEIcDEQVIQVLDEVGLKEKvlslkygIYTSIGEggemLSGGQMRRIELSR 463
Cdd:COG4152 79 erglypkmkvgeQLvyLA-RLKG---LSKAEA-KRRADEWLERLGLGDR-------ANKKVEE----LSKGNQQKVQLIA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488386603 464 LLLLKPDIVIFDEPAIGLD-IETEKVIQQVLEHH-------FST 499
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDpVNVELLKDVIRELAakgttviFSS 186
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
323-493 |
1.38e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 323 VLIKHVDFQYANSnHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN-------IGFLSQ 395
Cdd:PRK15056 7 IVVNDVTVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqalqknlVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 396 RPHI---FADSIKNNIAM--------------YDDEICDEQVIQVlDEVGLKekvlslkygiYTSIGEggemLSGGQMRR 458
Cdd:PRK15056 86 SEEVdwsFPVLVEDVVMMgryghmgwlrrakkRDRQIVTAALARV-DMVEFR----------HRQIGE----LSGGQKKR 150
|
170 180 190
....*....|....*....|....*....|....*
gi 488386603 459 IELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVL 493
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL 185
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
340-482 |
2.79e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASlnIGFLSQRPHIFADSIKNNIaMYDDEICDEQ 419
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGS--VAYVPQVSWIFNATVRENI-LFGSDFESER 709
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488386603 420 VIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLD 482
Cdd:PLN03232 710 YWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
338-519 |
3.23e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 338 MALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGT----------LSFNQA-SLNIGFLSQRPHIFAD-SIK 405
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTleiggnpcarLTPAKAhQLGIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 406 NNIA--MYDDEICDEQVIQVLDEVGLKekvLSLkygiytsigeggEMLSGG------QMrrIELSRLLLLKPDIVIFDEP 477
Cdd:PRK15439 105 ENILfgLPKRQASMQKMKQLLAALGCQ---LDL------------DSSAGSlevadrQI--VEILRGLMRDSRILILDEP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488386603 478 AIGLD-IETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRI 519
Cdd:PRK15439 168 TASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRI 210
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
340-483 |
3.40e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSfNQASLNIGFLSQRPHIFAD---SIKnNIAMYDDEIC 416
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-RNGKLRIGYVPQKLYLDTTlplTVN-RFLRLRPGTK 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 417 DEQVIQVLDEVGLKEkvlslkygiytSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDI 483
Cdd:PRK09544 98 KEDILPALKRVQAGH-----------LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
340-494 |
3.84e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.30 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASlnIGFLSQRPHIFADSIKNNIaMYDDEICDEQ 419
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGT--VAYVPQVSWIFNATVRDNI-LFGSPFDPER 709
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488386603 420 VIQVLDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIEtekVIQQVLE 494
Cdd:PLN03130 710 YERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH---VGRQVFD 781
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
339-507 |
4.07e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 64.34 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIGFLSQRPH-------IFADSIKN-NIAM 410
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsdiqmIFQDPLASlNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 411 YDDEICDEQVIQVL-----DEVGLKEKVLSLKYGIYTS-IGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIE 484
Cdd:PRK15079 116 TIGEIIAEPLRTYHpklsrQEVKDRVKAMMLKVGLLPNlINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180
....*....|....*....|....*.
gi 488386603 485 TE-KVIQ--QVLEHHFSTTTVFiIAH 507
Cdd:PRK15079 196 IQaQVVNllQQLQREMGLSLIF-IAH 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
343-527 |
4.97e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.08 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 343 ISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSF------NQASL---NIGFLSQRPHIFAD-SIKNNI---- 408
Cdd:PRK13536 60 LSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvpARARLaraRIGVVPQFDNLDLEfTVRENLlvfg 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 409 ---AMYDDEIcdEQVIQVLDEVGLKEKVLSLKYGiytsigeggeMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIET 485
Cdd:PRK13536 140 ryfGMSTREI--EAVIPSLLEFARLESKADARVS----------DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488386603 486 EKVIQQVLEHHFST-TTVFIIAH-RDSTIRSSARRIYIESGHLI 527
Cdd:PRK13536 208 RHLIWERLRSLLARgKTILLTTHfMEEAERLCDRLCVLEAGRKI 251
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
346-507 |
5.53e-11 |
|
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: 62.81 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 346 SVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHG-------TLSFNQASLNIGFLSQRPHIFADSIKN--NIAMYDDEIC 416
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdieieldTVSYKPQYIKADYEGTVRDLLSSITKDfyTHPYFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 417 DE-QVIQVLDevglkEKVLSlkygiytsigeggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIE----TEKVIQQ 491
Cdd:cd03237 101 KPlQIEQILD-----REVPE---------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRR 160
|
170
....*....|....*.
gi 488386603 492 VLEHHfsTTTVFIIAH 507
Cdd:cd03237 161 FAENN--EKTAFVVEH 174
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
338-507 |
5.63e-11 |
|
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: 64.96 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 338 MALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQaSLNIGFLSQrphiFADSIKNNIAMYddeicd 417
Cdd:TIGR03719 336 LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-TVKLAYVDQ----SRDALDPNKTVW------ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 418 EQVIQVLDEVGL-KEKVLSLKYgiytsIG----EGGE------MLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETE 486
Cdd:TIGR03719 405 EEISGGLDIIKLgKREIPSRAY-----VGrfnfKGSDqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETL 479
|
170 180
....*....|....*....|.
gi 488386603 487 KVIQQVLEhHFSTTTVfIIAH 507
Cdd:TIGR03719 480 RALEEALL-NFAGCAV-VISH 498
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
343-538 |
7.56e-11 |
|
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: 63.59 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 343 ISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN--------------IGFLSQRPHIFAD-SIKNN 407
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdsrkgiflppekrrIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 408 I------AMYDD-EICDEQVIQVLdevglkekvlslkyGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIG 480
Cdd:TIGR02142 96 LrygmkrARPSErRISFERVIELL--------------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488386603 481 LDIETEKVIQQVLEH---HFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDSIISVTRS 538
Cdd:TIGR02142 162 LDDPRKYEILPYLERlhaEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
335-505 |
7.98e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.27 E-value: 7.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 335 SNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTL--SFNQASLnigfLS--QRPHIFADSIK-NNIA 409
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsQFSHITR----LSfeQLQKLVSDEWQrNNTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 410 MYDDEICD-----EQVIQvlDEVGLKEKVLSL--KYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLD 482
Cdd:PRK10938 90 MLSPGEDDtgrttAEIIQ--DEVKDPARCEQLaqQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180
....*....|....*....|....*
gi 488386603 483 IETEKVIQQVLE--HHFSTTTVFII 505
Cdd:PRK10938 168 VASRQQLAELLAslHQSGITLVLVL 192
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
339-531 |
8.26e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN-----------IGFLSQRPHIFAD-SIKN 406
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwqtakimreaVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 407 NIAMYDDEICDEQVIQVLDEVglkekvlslkYGIYTSIGE-----GGEMlSGGQMRRIELSRLLLLKPDIVIFDEPAIGL 481
Cdd:PRK11614 100 NLAMGGFFAERDQFQERIKWV----------YELFPRLHErriqrAGTM-SGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488386603 482 D----IETEKVIQQVLEHHFsttTVFIIAHRDSTIRSSARRIYI-ESGHLIKDDS 531
Cdd:PRK11614 169 ApiiiQQIFDTIEQLREQGM---TIFLVEQNANQALKLADRGYVlENGHVVLEDT 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
336-482 |
8.31e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.59 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 336 NHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTL----------SFNQASLNIGFLSQR--PHIfadS 403
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvthrSIQQRDICMVFQSYAlfPHM---S 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 404 IKNNIA-------MYDDEIcDEQVIQVLDEVGLkekvlslkygiytsigEGGE-----MLSGGQMRRIELSRLLLLKPDI 471
Cdd:PRK11432 95 LGENVGyglkmlgVPKEER-KQRVKEALELVDL----------------AGFEdryvdQISGGQQQRVALARALILKPKV 157
|
170
....*....|.
gi 488386603 472 VIFDEPAIGLD 482
Cdd:PRK11432 158 LLFDEPLSNLD 168
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
339-494 |
1.13e-10 |
|
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: 61.68 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN---------QAS----LN-----IGFLSQ----R 396
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaQASpreiLAlrrrtIGYVSQflrvI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 397 PHIFADSIknniamyddeicdeqVIQVLDEVGLKEKvlslkygiyTSIGEGGEML-----------------SGGQMRRI 459
Cdd:COG4778 106 PRVSALDV---------------VAEPLLERGVDRE---------EARARARELLarlnlperlwdlppatfSGGEQQRV 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 488386603 460 ELSRLLLLKPDIVIFDEPAIGLDIET-EKVIQQVLE 494
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANrAVVVELIEE 197
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
340-482 |
1.41e-10 |
|
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: 60.64 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTH--GTLSFNqaslniGFlSQRPHIFADSIknNIAMYDDeicd 417
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLIN------GR-PLDKRSFRKII--GYVPQDD---- 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488386603 418 eqviQVLDEVGLKEKVLslkygiYTSIGEGgemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLD 482
Cdd:cd03213 92 ----ILHPTLTVRETLM------FAAKLRG---LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
340-482 |
1.80e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.53 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTP---THGTLSFN-----------------QASLNIGFLSQRPH- 398
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNgmpidakemraisayvqQDDLFIPTLTVREHl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 399 IFADSIKNNIAMYDDEIcDEQVIQVLDEVGLKEKVlslkygiYTSIGEGGEM--LSGGQMRRIELSRLLLLKPDIVIFDE 476
Cdd:TIGR00955 121 MFQAHLRMPRRVTKKEK-RERVDEVLQALGLRKCA-------NTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
....*.
gi 488386603 477 PAIGLD 482
Cdd:TIGR00955 193 PTSGLD 198
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
330-535 |
2.22e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 62.13 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 330 FQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN-------------QASLNIG----- 391
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDgqdltalsekelrKARRQIGmifqh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 392 --FLSQRphifadSIKNNIA-------MYDDEIcDEQVIQVLDEVGLKEKVLSlkygiYTSigeggeMLSGGQMRRIELS 462
Cdd:PRK11153 91 fnLLSSR------TVFDNVAlplelagTPKAEI-KARVTELLELVGLSDKADR-----YPA------QLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386603 463 RLLLLKPDIVIFDEPAIGLDIETEKVIQQVL-----EHHFsttTVFIIAHRDSTIRSSARRI-YIESGHLIKDDSIISV 535
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLkdinrELGL---TIVLITHEMDVVKRICDRVaVIDAGRLVEQGTVSEV 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
325-483 |
2.82e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.80 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNhmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFLS 394
Cdd:PRK11231 5 TENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmlssrqlarrLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 395 QRpHIFADSIK-NNIAMY--------------DDEICDEQVIQVLDEVGLKEKVLSlkygiytsigeggeMLSGGQMRRI 459
Cdd:PRK11231 83 QH-HLTPEGITvRELVAYgrspwlslwgrlsaEDNARVNQAMEQTRINHLADRRLT--------------DLSGGQRQRA 147
|
170 180
....*....|....*....|....
gi 488386603 460 ELSRLLLLKPDIVIFDEPAIGLDI 483
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
347-507 |
4.14e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 347 VNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFnqaSLNIGFLSQRphIFADS-------IKNNIAMYDDEICDEQ 419
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELKISYKPQY--IKPDYdgtvedlLRSITDDLGSSYYKSE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 420 VIQVLDEVGLKEKvlslkygiytSIGEggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIE----TEKVIQQVLEH 495
Cdd:PRK13409 437 IIKPLQLERLLDK----------NVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAEE 502
|
170
....*....|..
gi 488386603 496 HfsTTTVFIIAH 507
Cdd:PRK13409 503 R--EATALVVDH 512
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
327-494 |
5.33e-10 |
|
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: 62.01 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 327 HVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLA----KLLSQSVTPTHGTLSFNQASL-------------- 388
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTAlsilRLLPDPAAHPSGSILFDGQDLlglserelrrirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 389 NIGFLSQRP-------HifadSIKNNIA-------MYDDEICDEQVIQVLDEVGLKEKVLSLK-YgiytsigegGEMLSG 453
Cdd:COG4172 93 RIAMIFQEPmtslnplH----TIGKQIAevlrlhrGLSGAAARARALELLERVGIPDPERRLDaY---------PHQLSG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488386603 454 GQMRRIELSRLLLLKPDIVIFDEPAIGLDIetekVIQ-QVLE 494
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaQILD 197
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
339-508 |
6.21e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL-------------NIGFLSQRP-------H 398
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspgklqalrrDIQFIFQDPyasldprQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 399 IFADSIKNNIAMY---DDEICDEQVIQVLDEVGLKEKvLSLKYgiytsigegGEMLSGGQMRRIELSRLLLLKPDIVIFD 475
Cdd:PRK10261 419 TVGDSIMEPLRVHgllPGKAAAARVAWLLERVGLLPE-HAWRY---------PHEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488386603 476 EPAIGLDIETEKVIQQV---LEHHFSTTTVFI---------IAHR 508
Cdd:PRK10261 489 EAVSALDVSIRGQIINLlldLQRDFGIAYLFIshdmavverISHR 533
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
338-495 |
6.45e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 338 MALKNI---------SFSVNKGEKVAIVGPSGAGKSTL----AKLLSQSvtpthGTLSFNQASLNI----------GFLS 394
Cdd:PRK03695 1 MQLNDVavstrlgplSAEVRAGEILHLVGPNGAGKSTLlarmAGLLPGS-----GSIQFAGQPLEAwsaaelarhrAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 395 Q--RPhIFADSIKNNIAMYDDEICDEQVIQ-VLDEV----GLKEKvlslkygIYTSIGEggemLSGGQMRRIEL------ 461
Cdd:PRK03695 76 QqqTP-PFAMPVFQYLTLHQPDKTRTEAVAsALNEVaealGLDDK-------LGRSVNQ----LSGGEWQRVRLaavvlq 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488386603 462 --------SRLLLLkpdivifDEPAIGLDIETEKVIQQVLEH 495
Cdd:PRK03695 144 vwpdinpaGQLLLL-------DEPMNSLDVAQQAALDRLLSE 178
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
336-521 |
1.17e-09 |
|
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: 57.72 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 336 NHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKllsqsvtpthGTLSFNQASLNIGFLSQRPH---IFADSIKNniamyd 412
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN----------EGLYASGKARLISFLPKFSRnklIFIDQLQF------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 413 deicdeqviqvLDEVGLKekvlslkygiYTSIGEGGEMLSGGQMRRIELSRLLL--LKPDIVIFDEPAIGLD-IETEKVI 489
Cdd:cd03238 71 -----------LIDVGLG----------YLTLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHqQDINQLL 129
|
170 180 190
....*....|....*....|....*....|..
gi 488386603 490 QQVLEHHFSTTTVFIIAHRDSTIRSSARRIYI 521
Cdd:cd03238 130 EVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
325-524 |
1.18e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.36 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQY-ANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFL 393
Cdd:PRK13650 7 VKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeenvwdirhkIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 394 SQRP--HIFADSIKNNIAM------YDDEICDEQVIQVLDEVGL---KEKVLSlkygiytsigeggeMLSGGQMRRIELS 462
Cdd:PRK13650 87 FQNPdnQFVGATVEDDVAFglenkgIPHEEMKERVNEALELVGMqdfKEREPA--------------RLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 463 RLLLLKPDIVIFDEPAIGLD----IETEKVIQQVLEHHfsTTTVFIIAHRDSTIRSSARRIYIESG 524
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDY--QMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
339-483 |
1.28e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.42 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN-----------IGFLSQ-RPH--IFAD-S 403
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdairagIAYVPEdRKGegLVLDlS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 404 IKNNIamyddeicdeqVIQVLDEV---GL----KEKVLSLKY---------GIYTSIGEggemLSGGQMRRIELSRLLLL 467
Cdd:COG1129 347 IRENI-----------TLASLDRLsrgGLldrrRERALAEEYikrlriktpSPEQPVGN----LSGGNQQKVVLAKWLAT 411
|
170
....*....|....*.
gi 488386603 468 KPDIVIFDEPAIGLDI 483
Cdd:COG1129 412 DPKVLILDEPTRGIDV 427
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
338-528 |
1.72e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.66 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 338 MALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNqaSLNIGFLSQRPhiFADSIKNNIAMYDDEICD 417
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID--GVDIAKISDAE--LREVRRKKIAMVFQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 418 EQVIQVLDEVGL------------KEKVLSL--KYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLD- 482
Cdd:PRK10070 118 MPHMTVLDNTAFgmelaginaeerREKALDAlrQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDp 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488386603 483 -IETEKVIQQV-LEHHFSTTTVFIIAHRDSTIRSSARRIYIESGHLIK 528
Cdd:PRK10070 198 lIRTEMQDELVkLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
346-507 |
2.11e-09 |
|
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: 60.18 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 346 SVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNqasLNIGFLSQRphifadsIKNNIamyddeicDEQVIQVLD 425
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED---LKISYKPQY-------ISPDY--------DGTVEEFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 426 EVgLKEKVLSLKYgiYTSIGEGGEM----------LSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIE----TEKVIQQ 491
Cdd:COG1245 424 SA-NTDDFGSSYY--KTEIIKPLGLeklldknvkdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRR 500
|
170
....*....|....*.
gi 488386603 492 VLEHHfsTTTVFIIAH 507
Cdd:COG1245 501 FAENR--GKTAMVVDH 514
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
329-482 |
2.56e-09 |
|
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: 57.67 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 329 DFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVtPTHGTLS----FNQASLN-------IGFLSQRp 397
Cdd:cd03234 12 KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV-EGGGTTSgqilFNGQPRKpdqfqkcVAYVRQD- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 398 HIFADSIK--------NNIAMydDEICDEQVIQVLDEvglkekVLSLKYGIYTSIG----EGgemLSGGQMRRIELSRLL 465
Cdd:cd03234 90 DILLPGLTvretltytAILRL--PRKSSDAIRKKRVE------DVLLRDLALTRIGgnlvKG---ISGGERRRVSIAVQL 158
|
170
....*....|....*..
gi 488386603 466 LLKPDIVIFDEPAIGLD 482
Cdd:cd03234 159 LWDPKVLILDEPTSGLD 175
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
340-493 |
2.64e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 57.93 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSqSVTPTHGTLSFNQASLNI----------GFLSQR-PHIFADSIKNNI 408
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMA-GLLPGQGEILLNGRPLSDwsaaelarhrAYLSQQqSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 409 AMY-DDEICDEQVIQVLDEvgLKEKV-LSLKYGiyTSIGEggemLSGGQMRRIEL--------------SRLLLLkpdiv 472
Cdd:COG4138 91 ALHqPAGASSEAVEQLLAQ--LAEALgLEDKLS--RPLTQ----LSGGEWQRVRLaavllqvwptinpeGQLLLL----- 157
|
170 180
....*....|....*....|.
gi 488386603 473 ifDEPAIGLDIetekvIQQVL 493
Cdd:COG4138 158 --DEPMNSLDV-----AQQAA 171
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
339-491 |
3.58e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN---------QASLNIG------------------ 391
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqemrfastTAALAAGvaiiyqelhlvpemtvae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 392 --FLSQRPHIFadsiknniAMYDDEICDEQVIQVLDEVGLK-EKVLSLKYgiytsigeggemLSGGQMRRIELSRLLLLK 468
Cdd:PRK11288 99 nlYLGQLPHKG--------GIVNRRLLNYEAREQLEHLGVDiDPDTPLKY------------LSIGQRQMVEIAKALARN 158
|
170 180
....*....|....*....|....*..
gi 488386603 469 PDIVIFDEPAIGLDI-ETE---KVIQQ 491
Cdd:PRK11288 159 ARVIAFDEPTSSLSArEIEqlfRVIRE 185
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
341-482 |
7.15e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 57.73 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 341 KNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN--------IGFLSQR----PHI-FAD--SIK 405
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNdvppaergVGMVFQSyalyPHLsVAEnmSFG 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 406 NNIAMYDDEICDEQVIQVLDEVGLkEKVLSLKygiytsigegGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLD 482
Cdd:PRK11000 100 LKLAGAKKEEINQRVNQVAEVLQL-AHLLDRK----------PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
325-507 |
8.92e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.39 E-value: 8.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAK------------------------LLSQSVTPThgt 380
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrllelneearvegevrlfgrnIYSPDVDPI--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 381 lsfnQASLNIGFLSQRPHIFAD-SIKNNIAM---------YDDEIcDEQVIQVLDEVGLKEKVLSlKYGIYTSigeggeM 450
Cdd:PRK14267 82 ----EVRREVGMVFQYPNPFPHlTIYDNVAIgvklnglvkSKKEL-DERVEWALKKAALWDEVKD-RLNDYPS------N 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488386603 451 LSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAH 507
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
336-531 |
9.84e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 57.26 E-value: 9.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 336 NHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN----------QASLNIGFLSQR--PHIfadS 403
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqdithvpaeNRHVNTVFQSYAlfPHM---T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 404 IKNNIA----MY---DDEIcDEQVIQVLDEVGLKE----KVLSlkygiytsigeggemLSGGQMRRIELSRLLLLKPDIV 472
Cdd:PRK09452 103 VFENVAfglrMQktpAAEI-TPRVMEALRMVQLEEfaqrKPHQ---------------LSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386603 473 IFDEPAIGLDIETEKVIQQVLEH---HFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDS 531
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKAlqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
337-526 |
2.00e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.82 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 337 HMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNI----GFLSQRPHIFADSIKNNIAMYD 412
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIaissGLNGQLTGIENIELKGLMMGLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 413 DEICDEQVIQVLD--EVGlkeKVLSLKYGIYTSigeggemlsgGQMRRIELSRLLLLKPDIVIFDEP-AIGLDIETEKVI 489
Cdd:PRK13545 117 KEKIKEIIPEIIEfaDIG---KFIYQPVKTYSS----------GMKSRLGFAISVHINPDILVIDEAlSVGDQTFTKKCL 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 488386603 490 QQVLEHHFSTTTVFIIAHRDSTIRS-SARRIYIESGHL 526
Cdd:PRK13545 184 DKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQV 221
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
340-494 |
2.38e-08 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 55.19 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASlnIGFLSQRPHIF--ADS-----IKNNIAMY- 411
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEE--IRLKPDRDGELvpADRrqlqrIRTRLGMVf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 412 -------------------------DDEICDEQVIQVLDEVGLKEKvlslkYGIYTSigeggeMLSGGQMRRIELSRLLL 466
Cdd:COG4598 102 qsfnlwshmtvlenvieapvhvlgrPKAEAIERAEALLAKVGLADK-----RDAYPA------HLSGGQQQRAAIARALA 170
|
170 180 190
....*....|....*....|....*....|..
gi 488386603 467 LKPDIVIFDEPAIGLDIETE----KVIQQVLE 494
Cdd:COG4598 171 MEPEVMLFDEPTSALDPELVgevlKVMRDLAE 202
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
18-476 |
2.69e-08 |
|
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: 56.34 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 18 MLIMSVFLSFTVVAQNISISHFLNHLLYYQQQSLLLLLSVIFISLILRATFNMLIQFLGDHLAFKVKHMLREQV---ILK 94
Cdd:COG4615 14 LLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLsrrILA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 95 KSVRSIgEEI------NILTESIDGIGPFFQSyLPQVFKSMLIPIVIIITMCFVHLPTAIIMIVTAPFIPLFYVIFGLKT 168
Cdd:COG4615 94 APLERL-ERIgaarllAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLLVRRA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 169 R---DESKDQMTYLNQFSQRFLNTAKGLitfkLLNQTKQS---EQQLYKDSTRFRDLTMRILkSAFLSGLMLEFISMLG- 241
Cdd:COG4615 172 RrhlRRAREAEDRLFKHFRALLEGFKEL----KLNRRRRRaffDEDLQPTAERYRDLRIRAD-TIFALANNWGNLLFFAl 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 242 IGLV------------ALEAALSLVVFnhinFVTAAIAIILA--PEF------YNAIKDLGQAFHTGKQSEGASDvvfsf 301
Cdd:COG4615 247 IGLIlfllpalgwadpAVLSGFVLVLL----FLRGPLSQLVGalPTLsranvaLRKIEELELALAAAEPAAADAA----- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 302 lESEDKADSPTLKVDEqqfeqvlikhVDFQYAN---SNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTH 378
Cdd:COG4615 318 -APPAPADFQTLELRG----------VTYRYPGedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPES 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 379 GTLSFNQASLNIGFLSQ-RPH---IFAD-SIKNNIAMYDDEICDEQVIQVLDEVGLKEKVlSLKYGIYTSIGeggemLSG 453
Cdd:COG4615 387 GEILLDGQPVTADNREAyRQLfsaVFSDfHLFDRLLGLDGEADPARARELLERLELDHKV-SVEDGRFSTTD-----LSQ 460
|
490 500
....*....|....*....|...
gi 488386603 454 GQMRRIELSRLLLLKPDIVIFDE 476
Cdd:COG4615 461 GQRKRLALLVALLEDRPILVFDE 483
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
339-383 |
2.79e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.93 E-value: 2.79e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSF 383
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHY 65
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
340-483 |
2.79e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 56.00 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGT----------LSFNQASLNIGFLSQRPHI-FADSIKNNI 408
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTvlvagddveaLSARAASRRVASVPQDTSLsFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 409 AM--------YD--DEICDEQVIQVLDEVGlkekVLSLKYGIYTSigeggemLSGGQMRRIELSRLLLLKPDIVIFDEPA 478
Cdd:PRK09536 99 EMgrtphrsrFDtwTETDRAAVERAMERTG----VAQFADRPVTS-------LSGGERQRVLLARALAQATPVLLLDEPT 167
|
....*
gi 488386603 479 IGLDI 483
Cdd:PRK09536 168 ASLDI 172
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-529 |
3.61e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 54.72 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQ-------------------SVTPTHGTLSFNQaslNIGFLSQRPHIF 400
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmndkvsgyrysgdvllggrSIFNYRDVLEFRR---RVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 401 ADSIKNNI--AMYDDEICDEQVIQVLDEVGLKEkvLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPA 478
Cdd:PRK14271 114 PMSIMDNVlaGVRAHKLVPRKEFRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488386603 479 IGLDIETEKVIQQVLEHHFSTTTVFIIAHR-DSTIRSSARRIYIESGHLIKD 529
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNlAQAARISDRAALFFDGRLVEE 243
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
328-493 |
3.94e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 328 VDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLA----KLL-SQSVTPTHGTLSFNQASL-------------- 388
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTAlsilRLLpSPPVVYPSGDIRFHGESLlhaseqtlrgvrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 389 NIGFLSQRPHIFADSIKN-NIAMYD---------DEICDEQVIQVLDEVGLKEKVLSLKygiytsigEGGEMLSGGQMRR 458
Cdd:PRK15134 93 KIAMIFQEPMVSLNPLHTlEKQLYEvlslhrgmrREAARGEILNCLDRVGIRQAAKRLT--------DYPHQLSGGERQR 164
|
170 180 190
....*....|....*....|....*....|....*
gi 488386603 459 IELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVL 493
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLL 199
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
341-483 |
5.03e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.22 E-value: 5.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 341 KNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN----------IGFLSQRPHIFAD-SIKNNIA 409
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyaskevarrIGLLAQNATTPGDiTVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 410 -------------MYDDEicdEQVIQVLDEVGLKEKVlslkygiytsiGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDE 476
Cdd:PRK10253 104 rgryphqplftrwRKEDE---EAVTKAMQATGITHLA-----------DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
....*..
gi 488386603 477 PAIGLDI 483
Cdd:PRK10253 170 PTTWLDI 176
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
316-504 |
5.84e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 316 DEQQFEQVLIKH---VDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLS---------- 382
Cdd:PRK10261 5 DELDARDVLAVEnlnIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 383 --------FNQASL------NIGFLSQRPH-----IFA--DSIKNNIAMYDDEICDEQVIQ---VLDEVGLKEKvlslky 438
Cdd:PRK10261 85 rqvielseQSAAQMrhvrgaDMAMIFQEPMtslnpVFTvgEQIAESIRLHQGASREEAMVEakrMLDQVRIPEA------ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488386603 439 giYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQ---VLEHHFSTTTVFI 504
Cdd:PRK10261 159 --QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQlikVLQKEMSMGVIFI 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
298-493 |
5.88e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 298 VFSFLESEDKADSPTLKVDEQQFEQVLIKH-----VDFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQ 372
Cdd:TIGR00956 732 VLGSTDLTDESDDVNDEKDMEKESGEDIFHwrnltYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 373 SVTP---THGTLSFN----QASL--NIGFLSQRP-HIFADSIK------------NNIAMYDDEICDEQVIQVLDEVGLK 430
Cdd:TIGR00956 812 RVTTgviTGGDRLVNgrplDSSFqrSIGYVQQQDlHLPTSTVReslrfsaylrqpKSVSKSEKMEYVEEVIKLLEMESYA 891
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488386603 431 EKVlslkygiytsIGEGGEMLSGGQMRRIELSRLLLLKPDIVIF-DEPAIGLDIETEKVIQQVL 493
Cdd:TIGR00956 892 DAV----------VGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLM 945
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
342-507 |
7.18e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 342 NISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNqASLNIGFLSQRPHIFAD-SIKNNIAMYDDEICdeQV 420
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD-PNERLGKLRQDQFAFEEfTVLDTVIMGHTELW--EV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 421 IQVLD----------EVGLKEKVLSLKYGI---YTSIGEGGEMLSG---------GQMR--------RIELSRLLLLKPD 470
Cdd:PRK15064 96 KQERDriyalpemseEDGMKVADLEVKFAEmdgYTAEARAGELLLGvgipeeqhyGLMSevapgwklRVLLAQALFSNPD 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 488386603 471 IVIFDEPAIGLDIETEKVIQQVLEHHFSttTVFIIAH 507
Cdd:PRK15064 176 ILLLDEPTNNLDINTIRWLEDVLNERNS--TMIIISH 210
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
341-485 |
8.71e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 341 KNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQaSLNIGFLSQrphiFADSIKNNIAMYdDEICDEQ- 419
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE-TVKLAYVDQ----SRDALDPNKTVW-EEISGGLd 414
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 420 VIQvldeVGLKEkVLSLKYgiytsIG----EGGE------MLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIET 485
Cdd:PRK11819 415 IIK----VGNRE-IPSRAY-----VGrfnfKGGDqqkkvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
57-245 |
9.14e-08 |
|
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: 53.93 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 57 VIFISLILRATFNMLIQFLGdhlaFKVKHMLREQV---ILKKSVR-----SIGEEINILTESIDGIGPFFQSYLPQVFKS 128
Cdd:cd18544 50 LLLLSFLLQYLQTYLLQKLG----QRIIYDLRRDLfshIQRLPLSffdrtPVGRLVTRVTNDTEALNELFTSGLVTLIGD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 129 MLIPIVIIITMCFVHLPTAIIMIVTAPFIPLFYVIFGLKTRD---ESKDQMTYLNQFSQRFLNtakGLITFKLLNQTKQS 205
Cdd:cd18544 126 LLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKayrEVREKLSRLNAFLQESIS---GMSVIQLFNREKRE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488386603 206 EQQLYKDSTRFRDLTMRILKSAFLSGLMLEFISMLGIGLV 245
Cdd:cd18544 203 FEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALV 242
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
286-494 |
1.14e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 286 HTGKQSEGASDVVFSFL------------ESEDKADSPTLKVDEQQFEqvlIKHVDFQYanSNHMALKNISFSVNKGEKV 353
Cdd:PRK10938 215 ETGEREEILQQALVAQLahseqlegvqlpEPDEPSARHALPANEPRIV---LNNGVVSY--NDRPILHNLSWQVNPGEHW 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 354 AIVGPSGAGKSTLAKLlsqsVTPTHGTLSFNQASL----------------NIGFLSQRPHI---------------FAD 402
Cdd:PRK10938 290 QIVGPNGAGKSTLLSL----ITGDHPQGYSNDLTLfgrrrgsgetiwdikkHIGYVSSSLHLdyrvstsvrnvilsgFFD 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 403 SiknnIAMYdDEICDEQ---VIQVLDEVGLKEKVLSLKYgiytsigeggEMLSGGQMRRIELSRLLLLKPDIVIFDEPAI 479
Cdd:PRK10938 366 S----IGIY-QAVSDRQqklAQQWLDILGIDKRTADAPF----------HSLSWGQQRLALIVRALVKHPTLLILDEPLQ 430
|
250
....*....|....*
gi 488386603 480 GLDIETEKVIQQVLE 494
Cdd:PRK10938 431 GLDPLNRQLVRRFVD 445
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
340-526 |
1.32e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.47 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTL--------------AKLLSQsvtPTHGTLSFNQASL---NIGFLSQR----PH 398
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLlailaglddgssgeVSLVGQ---PLHQMDEEARAKLrakHVGFVFQSfmliPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 399 IFAdsiKNNIAM------YDDEICDEQVIQVLDEVGLKEKVLSLKygiytsigeggEMLSGGQMRRIELSRLLLLKPDIV 472
Cdd:PRK10584 103 LNA---LENVELpallrgESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488386603 473 IFDEPAIGLDIETEKVIQQVLehhFS-----TTTVFIIAHRDSTIRSSARRIYIESGHL 526
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLL---FSlnrehGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
349-519 |
1.50e-07 |
|
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: 50.83 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 349 KGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLsfnqaslnigflsqrphIFADsiknniamyddeiCDEQVIQVLDEVg 428
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-----------------IYID-------------GEDILEEVLDQL- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 429 lkekvlslkygIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLE-------HHFSTTT 501
Cdd:smart00382 50 -----------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllllKSEKNLT 118
|
170
....*....|....*...
gi 488386603 502 VFIIAHRDSTIRSSARRI 519
Cdd:smart00382 119 VILTTNDEKDLGPALLRR 136
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
323-531 |
1.60e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.09 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 323 VLIKHVDFQYANSNHM---ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL----------- 388
Cdd:PRK13645 7 IILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkikevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 389 ----NIGFLSQRP--HIFADSIKNNIAM------YDDEICDEQVIQVLDEVGLKEKVLSlkygiyTSIGEggemLSGGQM 456
Cdd:PRK13645 87 rlrkEIGLVFQFPeyQLFQETIEKDIAFgpvnlgENKQEAYKKVPELLKLVQLPEDYVK------RSPFE----LSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488386603 457 RRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVLEH---HFSTTTVFIIAHRDSTIRSSARRIYIESGHLIKDDS 531
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
326-526 |
2.28e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.44 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 326 KHVDFQYANSNhMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIGFLSQRPHIFAdSIK 405
Cdd:PRK10522 326 RNVTFAYQDNG-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS-AVF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 406 NNIAMYD-------DEICDEQVIQVLDEVGLKEKvLSLKYGIYTSIgeggeMLSGGQMRRIELSRLLLLKPDIVIFDEPA 478
Cdd:PRK10522 404 TDFHLFDqllgpegKPANPALVEKWLERLKMAHK-LELEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488386603 479 IGLDIETEKVIQQVLEHHFSTT--TVFIIAHRDSTIRSSARRIYIESGHL 526
Cdd:PRK10522 478 ADQDPHFRREFYQVLLPLLQEMgkTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
340-521 |
4.86e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQAsLNIGFLSQRPHIFADSiknniamyddeicDEQ 419
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKG-IKLGYFAQHQLEFLRA-------------DES 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 420 VIQVLDEVGLKEKVLSLK-----YGIY-TSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVL 493
Cdd:PRK10636 394 PLQHLARLAPQELEQKLRdylggFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
170 180
....*....|....*....|....*...
gi 488386603 494 EhHFSTTTVfIIAHRDSTIRSSARRIYI 521
Cdd:PRK10636 474 I-DFEGALV-VVSHDRHLLRSTTDDLYL 499
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
339-384 |
7.35e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 50.85 E-value: 7.35e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN 384
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID 66
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
354-483 |
7.52e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.41 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 354 AIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL--------------NIGFLSQ--R--PHIfadSIKNN----IAMY 411
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekgiclppekrRIGYVFQdaRlfPHY---KVRGNlrygMAKS 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488386603 412 DDEICDeQVIQVLdevGLkEKVLSlKYGIytsigeggeMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDI 483
Cdd:PRK11144 105 MVAQFD-KIVALL---GI-EPLLD-RYPG---------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
339-380 |
1.53e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 1.53e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSqSVTPtHGT 380
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLS-GVYP-HGT 59
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
347-524 |
1.63e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.34 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 347 VNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLnigflSQRPhifadsiknniamyddeicdeqviQVLDe 426
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-----VYKP------------------------QYID- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 427 vglkekvlslkygiytsigeggemLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIE----TEKVIQQVLEHhfSTTTV 502
Cdd:cd03222 72 ------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEE--GKKTA 125
|
170 180
....*....|....*....|..
gi 488386603 503 FIIAHRDSTIRSSARRIYIESG 524
Cdd:cd03222 126 LVVEHDLAVLDYLSDRIHVFEG 147
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
339-380 |
1.65e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.56 E-value: 1.65e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSqSVTPtHGT 380
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLS-GVYP-HGS 55
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
342-492 |
2.05e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.21 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 342 NISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTH-GTLSFNQASLNIgflsQRPhifADSIKNNIAMYDDEICDEQV 420
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFeGNVFINGKPVDI----RNP---AQAIRAGIAMVPEDRKRHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 421 IQVLDeVGLKEKVLSL-KYGIYTSIGEGGEM-----------------------LSGGQMRRIELSRLLLLKPDIVIFDE 476
Cdd:TIGR02633 351 VPILG-VGKNITLSVLkSFCFKMRIDAAAELqiigsaiqrlkvktaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180
....*....|....*....|
gi 488386603 477 PAIGLDI----ETEKVIQQV 492
Cdd:TIGR02633 430 PTRGVDVgakyEIYKLINQL 449
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
340-491 |
2.76e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.02 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLS--QSVTPTHGTLSF-----------NQASLNIGFLSQRP--------H 398
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFkgkdllelspeDRAGEGIFMAFQYPveipgvsnQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 399 IFADSIKNNIAMY-DDEICDEQVIQvlDEVGLKEKVLSLKYGIYT-SIGEGgemLSGGQMRRIELSRLLLLKPDIVIFDE 476
Cdd:PRK09580 97 FFLQTALNAVRSYrGQEPLDRFDFQ--DLMEEKIALLKMPEDLLTrSVNVG---FSGGEKKRNDILQMAVLEPELCILDE 171
|
170
....*....|....*
gi 488386603 477 PAIGLDIETEKVIQQ 491
Cdd:PRK09580 172 SDSGLDIDALKIVAD 186
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
325-384 |
3.02e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 48.54 E-value: 3.02e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 325 IKHVDFQYanSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFN 384
Cdd:COG4604 4 IKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD 61
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
334-494 |
4.10e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 334 NSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQAslNIGFLSQRP-------HIFAD---- 402
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE--DITGLSPRErrrlgvaYIPEDrlgr 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 403 ------SIKNNIAM--YDDEICDEQVIqvLDEVGLKEKVLSL--KYGI-YTSIGEGGEMLSGGQMRRIELSRLLLLKPDI 471
Cdd:COG3845 346 glvpdmSVAENLILgrYRRPPFSRGGF--LDRKAIRAFAEELieEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKL 423
|
170 180
....*....|....*....|....
gi 488386603 472 VIFDEPAIGLDIE-TEKVIQQVLE 494
Cdd:COG3845 424 LIAAQPTRGLDVGaIEFIHQRLLE 447
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
332-526 |
4.28e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.27 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 332 YANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLS----FNQASLNIGFLSQRPHIfadsikNN 407
Cdd:PRK13546 32 HKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDrngeVSVIAISAGLSGQLTGI------EN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 408 IAMydDEICdeqviqvldeVGLKEKVLSLKYGIYTSIGEGGEML-------SGGQMRRIELSRLLLLKPDIVIFDEP-AI 479
Cdd:PRK13546 106 IEF--KMLC----------MGFKRKEIKAMTPKIIEFSELGEFIyqpvkkySSGMRAKLGFSINITVNPDILVIDEAlSV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488386603 480 GLDIETEKVIQQVLEHHFSTTTVFIIAHRDSTIRSSARRI-YIESGHL 526
Cdd:PRK13546 174 GDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIaWIEGGKL 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
342-482 |
4.88e-06 |
|
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: 48.94 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 342 NISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASL--------------NIGFLSQRPHIFAD-SIKN 406
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargiflpphrrRIGYVFQEARLFPHlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 407 NI-------AMYDDEICDEQVIQVLdEVG--LKEKVLSlkygiytsigeggemLSGGQMRRIELSRLLLLKPDIVIFDEP 477
Cdd:COG4148 97 NLlygrkraPRAERRISFDEVVELL-GIGhlLDRRPAT---------------LSGGERQRVAIGRALLSSPRLLLMDEP 160
|
....*
gi 488386603 478 AIGLD 482
Cdd:COG4148 161 LAALD 165
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
322-482 |
5.34e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 48.69 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 322 QVLIKHVDFQYANsNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSF-----NQ---ASLNIGFL 393
Cdd:PRK11650 3 GLKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIggrvvNElepADRDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 394 SQR----PHIfadSIKNNIA-------MYDDEIcDEQVIQVldevglkEKVLSLkygiytsigegGEM-------LSGGQ 455
Cdd:PRK11650 82 FQNyalyPHM---SVRENMAyglkirgMPKAEI-EERVAEA-------ARILEL-----------EPLldrkpreLSGGQ 139
|
170 180
....*....|....*....|....*..
gi 488386603 456 MRRIELSRLLLLKPDIVIFDEPAIGLD 482
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
340-491 |
5.78e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN-----------IGFLSQ-RPH---IFADSI 404
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspqdglangIVYISEdRKRdglVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 405 KNNIAmyddeIC--------------DEQVIQVLDEVGLkekvlslkYGIYT-----SIGeggeMLSGGQMRRIELSRLL 465
Cdd:PRK10762 348 KENMS-----LTalryfsraggslkhADEQQAVSDFIRL--------FNIKTpsmeqAIG----LLSGGNQQKVAIARGL 410
|
170 180
....*....|....*....|....*.
gi 488386603 466 LLKPDIVIFDEPAIGLDIETEKVIQQ 491
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKKEIYQ 436
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
329-507 |
7.62e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.60 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 329 DFQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSV-----TPTHGTLSFNQASL----------NIGFL 393
Cdd:PRK14247 8 DLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfkmdvielrrRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 394 SQRPHIFAD-SIKNNIAM--------YDDEICDEQVIQVLDEVGLKEKVLSlkygiytSIGEGGEMLSGGQMRRIELSRL 464
Cdd:PRK14247 88 FQIPNPIPNlSIFENVALglklnrlvKSKKELQERVRWALEKAQLWDEVKD-------RLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488386603 465 LLLKPDIVIFDEPAIGLDIETEKVIQQVLEHHFSTTTVFIIAH 507
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
342-507 |
8.25e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 48.86 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 342 NISFSVNkgEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTL---------SFNQASLNIGFLSQRPHIFAD-SIKNNIAMY 411
Cdd:TIGR01257 950 NITFYEN--QITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggkdietNLDAVRQSLGMCPQHNILFHHlTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 412 DDEICDEQviqvlDEVGLKEKVLSLKYGIYTSIGEGGEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQ 491
Cdd:TIGR01257 1028 AQLKGRSW-----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170
....*....|....*.
gi 488386603 492 VLEHHFSTTTVFIIAH 507
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTH 1118
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
341-493 |
1.28e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 341 KNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN-----------IGFL--SQRPHIFAD--SIK 405
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavkkgMAYIteSRRDNGFFPnfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 406 NNIAMYDD----------EICDEQVIQVLDEVglKEKVLSLK-YGIYTSIGEggemLSGGQMRRIELSRLLLLKPDIVIF 474
Cdd:PRK09700 360 QNMAISRSlkdggykgamGLFHEVDEQRTAEN--QRELLALKcHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIF 433
|
170
....*....|....*....
gi 488386603 475 DEPAIGLDIETEKVIQQVL 493
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVM 452
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
63-245 |
2.21e-05 |
|
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: 46.27 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 63 ILRATFNMLIQFLGDHLAFKVKHMLREQV---ILKKSVR-----SIGEEINILTESIDGIGPFFQSYLPQVFKSMLIPIV 134
Cdd:cd18542 50 LLRGVFRYLQGYLAEKASQKVAYDLRNDLydhLQRLSFSfhdkaRTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 135 IIITMCFVHLPTAIIMIVTAPFIPLFYVIFGLKTR---DESKDQMTYLNQFSQRFLNtakGLITFKLLNQTKQSEQQLYK 211
Cdd:cd18542 130 ALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRpafEEIREQEGELNTVLQENLT---GVRVVKAFAREDYEIEKFDK 206
|
170 180 190
....*....|....*....|....*....|....*.
gi 488386603 212 DSTRFRDLTMRILK--SAFLSglMLEFISMLGIGLV 245
Cdd:cd18542 207 ENEEYRDLNIKLAKllAKYWP--LMDFLSGLQIVLV 240
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
339-508 |
2.36e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLN-----------IGFLSQRPHIFAD-SIKN 406
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqeagIGIIHQELNLIPQlTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 407 NI----------------AMYddeicdeqviqvlDEVGLKEKVLSLKYGIYTSIGEggemLSGGQMRRIELSRLLLLKPD 470
Cdd:PRK10762 99 NIflgrefvnrfgridwkKMY-------------AEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488386603 471 IVIFDEPAIGL-DIETE---KVIQQVLEHHFStttVFIIAHR 508
Cdd:PRK10762 162 VIIMDEPTDALtDTETEslfRVIRELKSQGRG---IVYISHR 200
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
340-482 |
3.79e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.41 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTH--GTLSFN------QASLNIGFLSQR----PH-------IF 400
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANnrkptkQILKRTGFVTQDdilyPHltvretlVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 401 ADSIK--NNIAMYDDEICDEQVIQvldEVGLKEKVLSLkygIYTSIGEGgemLSGGQMRRIELSRLLLLKPDIVIFDEPA 478
Cdd:PLN03211 164 CSLLRlpKSLTKQEKILVAESVIS---ELGLTKCENTI---IGNSFIRG---ISGGERKRVSIAHEMLINPSLLILDEPT 234
|
....
gi 488386603 479 IGLD 482
Cdd:PLN03211 235 SGLD 238
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
330-482 |
4.27e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 45.38 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 330 FQYANSNhmALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNI---GFLSQRPH-------- 398
Cdd:PRK13638 9 FRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYskrGLLALRQQvatvfqdp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 399 ---IFADSIKNNIA-------MYDDEICD--EQVIQVLDEVGLKEKVLslkygiytsigeggEMLSGGQMRRIELSRLLL 466
Cdd:PRK13638 87 eqqIFYTDIDSDIAfslrnlgVPEAEITRrvDEALTLVDAQHFRHQPI--------------QCLSHGQKKRVAIAGALV 152
|
170
....*....|....*.
gi 488386603 467 LKPDIVIFDEPAIGLD 482
Cdd:PRK13638 153 LQARYLLLDEPTAGLD 168
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
57-285 |
6.02e-05 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 45.09 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 57 VIFISLILRATFNMLIQFLGDHLAFKVKHMLREQV---ILKKSVR-----SIGEEINILTESIDGIGPFFQSYLPQVFKS 128
Cdd:cd18547 50 LLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLfekLQRLPLSyfdthSHGDIMSRVTNDVDNISQALSQSLTQLISS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 129 MLIPIVIIITMCFVHLPTAIIMIVTAPFIPLFYVIFGLKTRDESKDQMTY---LNQFSQRFLNtakGLITFKLLNQTKQS 205
Cdd:cd18547 130 ILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKAlgeLNGYIEEMIS---GQKVVKAFNREEEA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 206 EQQLYKDSTRFRDLTMrilKSAFLSGLM---LEFISMLGIGLVALEAALsLVVFNHINFVTAAIAIILAPEFYNAIKDLG 282
Cdd:cd18547 207 IEEFDEINEELYKASF---KAQFYSGLLmpiMNFINNLGYVLVAVVGGL-LVINGALTVGVIQAFLQYSRQFSQPINQIS 282
|
...
gi 488386603 283 QAF 285
Cdd:cd18547 283 QQI 285
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
330-505 |
8.48e-05 |
|
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: 43.79 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 330 FQYANSNHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPT---HGTLSFNqaslnigflSQRPHIFADSIKN 406
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYN---------GIPYKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 407 NIAMyddeiCDEQVIQVldevglkeKVLSLKYGIYTSIG-EGGEML---SGGQMRRIELSRLLLLKPDIVIFDEPAIGLD 482
Cdd:cd03233 84 EIIY-----VSEEDVHF--------PTLTVRETLDFALRcKGNEFVrgiSGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180
....*....|....*....|....*..
gi 488386603 483 ----IETEKVIQQvLEHHFSTTTVFII 505
Cdd:cd03233 151 sstaLEILKCIRT-MADVLKTTTFVSL 176
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
57-285 |
9.80e-05 |
|
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: 44.34 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 57 VIFISLILRATFNMLIQFLGDHLAFKVKHMLREQV---ILKKSV-----RSIGEEINILTESIDGIGPFFQSYLPQVFKS 128
Cdd:cd18552 44 AIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLfdkLLRLPLsffdrNSSGDLISRITNDVNQVQNALTSALTVLVRD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 129 MLIPIVIIITMCFVHLPTAIIMIVTAPFIPLFYVIFGLKTRDESKDQMTYLNQFSQRFLNTAKGLITFKLLNQTKQSEQQ 208
Cdd:cd18552 124 PLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 209 LYKDSTRFRDLTMRILKSAFLSGLMLEFISMLGIGLVALeAALSLVVFNHI---NFVTAAIAIILApefYNAIKDLGQAF 285
Cdd:cd18552 204 FRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLW-YGGYQVISGELtpgEFISFITALLLL---YQPIKRLSNVN 279
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
342-491 |
1.11e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.92 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 342 NISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTH-GTLSFNQASLNIgflsQRPhifADSIKNNIAMYDDEICDEQV 420
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKI----RNP---QQAIAQGIAMVPEDRKRDGI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 421 IQVLDeVGLKEKVLSL-KYGIYTSIGEGGEM-----------------------LSGGQMRRIELSRLLLLKPDIVIFDE 476
Cdd:PRK13549 353 VPVMG-VGKNITLAALdRFTGGSRIDDAAELktilesiqrlkvktaspelaiarLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170
....*....|....*....
gi 488386603 477 PAIGLDI----ETEKVIQQ 491
Cdd:PRK13549 432 PTRGIDVgakyEIYKLINQ 450
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
343-493 |
1.13e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 343 ISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQASLNIgflsQRPHifaDSIKNNIAMyddeiCDE---- 418
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI----RSPR---DAIRAGIML-----CPEdrka 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 419 ----QVIQVLDEVGLKEKVLSLKYG--------------------IYTSIGEGGEM-LSGGQMRRIELSRLLLLKPDIVI 473
Cdd:PRK11288 340 egiiPVHSVADNINISARRHHLRAGclinnrweaenadrfirslnIKTPSREQLIMnLSGGNQQKAILGRWLSEDMKVIL 419
|
170 180
....*....|....*....|
gi 488386603 474 FDEPAIGLDIETEKVIQQVL 493
Cdd:PRK11288 420 LDEPTRGIDVGAKHEIYNVI 439
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
339-494 |
1.36e-04 |
|
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: 44.43 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSqSVTPtHGTLS----FNQASL-----------NIGFLSQRPHIFAD- 402
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILS-GVYP-HGTWDgeiyWSGSPLkasnirdteraGIVIIHQELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 403 SIKNNIAMyDDEICDEQVIQVLDEVGLKEKVL--SLKYGIYTSIGEGGEmLSGGQMRRIELSRLLLLKPDIVIFDEPAIG 480
Cdd:TIGR02633 94 SVAENIFL-GNEITLPGGRMAYNAMYLRAKNLlrELQLDADNVTRPVGD-YGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170
....*....|....
gi 488386603 481 LdieTEKVIQQVLE 494
Cdd:TIGR02633 172 L---TEKETEILLD 182
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
340-513 |
1.70e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.02 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLA---------------------KLLSQSVTP----THG---TLSFNQASLnig 391
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPdvdsIEGlspAIAIDQKTT--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 392 flSQRPHIFADSIKnniamyddEICD-----------EQVIQVLDEVGLKekvlslkygiYTSIGEGGEMLSGGQMRRIE 460
Cdd:cd03270 88 --SRNPRSTVGTVT--------EIYDylrllfarvgiRERLGFLVDVGLG----------YLTLSRSAPTLSGGEAQRIR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 461 LSRLLLLKPD--IVIFDEPAIGL-DIETEKVIQQVLEHHFSTTTVFIIAHRDSTIR 513
Cdd:cd03270 148 LATQIGSGLTgvLYVLDEPSIGLhPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIR 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
336-493 |
3.44e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 336 NHMALKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSFNQ-----------------------------A 386
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkinnhnaneainhgfalvteerrstgiyA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 387 SLNIGFLSQRPHIfaDSIKNNIAMYDDEICDEQVIQVLDEVGLKEKvlslkyGIYTSIGEggemLSGGQMRRIELSRLLL 466
Cdd:PRK10982 340 YLDIGFNSLISNI--RNYKNKVGLLDNSRMKSDTQWVIDSMRVKTP------GHRTQIGS----LSGGNQQKVIIGRWLL 407
|
170 180
....*....|....*....|....*..
gi 488386603 467 LKPDIVIFDEPAIGLDIETEKVIQQVL 493
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKFEIYQLI 434
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
339-519 |
5.52e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.42 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 339 ALKNISFSVNKGEKVAIVGPSGAGK--STLA--KLLSQSVTPTHGTLSFNQASLNIGFLSQRPHIfadsIKNNIAM-YDD 413
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKsvSSLAimGLIDYPGRVMAEKLEFNGQDLQRISEKERRNL----VGAEVAMiFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 414 EICD---------------------------EQVIQVLDEVGLKEKVLSLKygIYTsigeggEMLSGGQMRRIELSRLLL 466
Cdd:PRK11022 98 PMTSlnpcytvgfqimeaikvhqggnkktrrQRAIDLLNQVGIPDPASRLD--VYP------HQLSGGMSQRVMIAMAIA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488386603 467 LKPDIVIFDEPAIGLDIETE-KVIQQVLE-HHFSTTTVFIIAHRDSTIRSSARRI 519
Cdd:PRK11022 170 CRPKLLIADEPTTALDVTIQaQIIELLLElQQKENMALVLITHDLALVAEAAHKI 224
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
340-383 |
6.94e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 6.94e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHGTLSF 383
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF 60
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
340-493 |
8.89e-04 |
|
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: 40.69 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTH--GTLSFNQASLNIGFlsQRPHIFAdsiknniamyddeicd 417
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVitGEILINGRPLDKNF--QRSTGYV---------------- 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488386603 418 EQVIQVLDEVGLKEkvlSLKYGIYTsigeggEMLSGGQMRRIELSRLLLLKPDIVIFDEPAIGLDIETEKVIQQVL 493
Cdd:cd03232 85 EQQDVHSPNLTVRE---ALRFSALL------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
|
| Cmk |
COG0283 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
353-372 |
9.58e-04 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440052 [Multi-domain] Cd Length: 220 Bit Score: 40.78 E-value: 9.58e-04
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
343-508 |
1.23e-03 |
|
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: 39.65 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 343 ISFSvnKGEKVAIVGPSGAGKSTLakllsqsvtpthgtlsFNQASLNIGFLSQRPHifadsiknniaMYDDEICDEQVIQ 422
Cdd:cd03227 16 VTFG--EGSLTIITGPNGSGKSTI----------------LDAIGLALGGAQSATR-----------RRSGVKAGCIVAA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 423 VldEVGLkekvlslkygIYTSIGeggemLSGGQMRRIELS---RLLLLKPD-IVIFDEPAIGLDI-ETEKVIQQVLEHHF 497
Cdd:cd03227 67 V--SAEL----------IFTRLQ-----LSGGEKELSALAlilALASLKPRpLYILDEIDRGLDPrDGQALAEAILEHLV 129
|
170
....*....|.
gi 488386603 498 STTTVFIIAHR 508
Cdd:cd03227 130 KGAQVIVITHL 140
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
352-372 |
1.36e-03 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 39.70 E-value: 1.36e-03
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
352-372 |
1.54e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 39.01 E-value: 1.54e-03
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
347-379 |
2.18e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 40.30 E-value: 2.18e-03
10 20 30
....*....|....*....|....*....|....
gi 488386603 347 VNKGEKVAIVGPSGAGKSTLA-KLLSQSVTPTHG 379
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVnALLGEEVQKTGA 225
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
340-367 |
2.81e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 2.81e-03
10 20
....*....|....*....|....*...
gi 488386603 340 LKNISFSVNKGEKVAIVGPSGAGKSTLA 367
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSLA 43
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
421-507 |
4.48e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488386603 421 IQVLDEVGLKekvlslkygiYTSIGEGGEMLSGGQMRRIELSRLLLLK---PDIVIFDEPAIGLDIETEK----VIQQVL 493
Cdd:TIGR00630 810 LQTLCDVGLG----------YIRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLV 879
|
90
....*....|....
gi 488386603 494 EhhfSTTTVFIIAH 507
Cdd:TIGR00630 880 D---KGNTVVVIEH 890
|
|
| Dck |
COG1428 |
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism]; |
353-372 |
4.75e-03 |
|
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
Pssm-ID: 441037 [Multi-domain] Cd Length: 205 Bit Score: 38.61 E-value: 4.75e-03
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
344-387 |
5.51e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 5.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 488386603 344 SFSVNKGEKVAIVGPSGAGKSTLAKLLSQSVTPTHgTLSFNQAS 387
Cdd:pfam13555 16 TIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK-RARFNKAA 58
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
353-372 |
9.42e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 37.51 E-value: 9.42e-03
|
| |
