|
Name |
Accession |
Description |
Interval |
E-value |
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
493-1017 |
0e+00 |
|
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: 579.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 493 RQKGKSLLTLIVLGLISGFGNAFLIFVINETFVRSNNLENGLLFYFVLGIVMYVFSQRIIRTSIVSYTNELVYEKRMELT 572
Cdd:COG4615 9 RESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 573 DKLLQTPYYKLELIEKGRIEATLNNDTEVISRSLNLLVTAGTSLLTLLFCFLYLGVMNMYAFLLSLCIIFITAGVYSLIG 652
Cdd:COG4615 89 RRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 653 RQADKVWNETRDIQNVYFRLIGDLRHGFKELRLHTGKRNDFRE-VMNESCNNYRVKRTIGDIKFANVFVLGELLFIFVIG 731
Cdd:COG4615 169 RRARRHLRRAREAEDRLFKHFRALLEGFKELKLNRRRRRAFFDeDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 732 IVVFVFPeIFVNMPKETISNYVIVFLYMTGPVNEILGGIPQLVNVRISWQRIQQMVKSVDHIKANEQIATTKEYLDVPIC 811
Cdd:COG4615 249 LILFLLP-ALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADFQT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDfTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQY-- 889
Cdd:COG4615 328 LELRGVTYRYPGEDGD-EGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYrq 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 890 -YSAILSDFHVFDRLYGINTEGMKAEIDHYLELLQLSDKVGIEDGRFTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAA 968
Cdd:COG4615 407 lFSAVFSDFHLFDRLLGLDGEADPARARELLERLELDHKVSVEDGRFSTTDLSQGQRKRLALLVALLEDRPILVFDEWAA 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1005564688 969 DQDPGYRRFFYEELLPQMRAKGKCIIAITHDDQYFHLADKLIVMEMGTV 1017
Cdd:COG4615 487 DQDPEFRRVFYTELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKL 535
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
503-1017 |
4.72e-108 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 347.33 E-value: 4.72e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 503 IVLGLISGFGNAFLIFVINETFVRSNNLENGLLFYFVlGIVMYVFSQRIIRTSIVSYTNELVYEK-RMELTDKLLQTPYY 581
Cdd:TIGR01194 24 IALGLAGGLAIIALLASINNAIHEENFLGQGSLFSFG-GLCLLALLFRIGADIFPAYAGMHIIANlRIALCEKILGAPIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 582 KLELIEKGRIEATLNNDTEVISRSLNLLVTAGTSLLTLLFCFLYLGVMNMYAFLLSLCIIFITAGVYSLIGRQADKVWNE 661
Cdd:TIGR01194 103 EIDRRGAHNLIPLLTHDIDQINAFLFIFPPIAIALAIFFFCIAYLAYLSVPMFAITISAIIIGTAAQLLAFMGGFKFFHA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 662 TRDIQNVYFRLIGDLRHGFKELRLHTGKRNDF-REVMNESCNNYRVKRTIGDIKFANVFVLGELLFIFVIGIVVFVFPEI 740
Cdd:TIGR01194 183 ARDEEDAFNEHTHAIAFGAKELKIHGIRRLSFaHGAIQESANNIADLHIIEILIFIAAENFGQLLFFLLIGCALFAAAMF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 741 FVNMPKeTISNYVIVFLYMTGPVNEILGGIPQLVNVRISWQRIQQMVKSVD----HIKANEQIATTKEYLDVPI-CLQLQ 815
Cdd:TIGR01194 263 ASIDAA-AISAFVLALLYIKGPLEMLVSALPILAQAQIACQRLADFGERFNepepELELSDADNVLLLAHDKSVdSIELK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 816 NVSYKYKNKDGDfTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQY---YSA 892
Cdd:TIGR01194 342 DVHMNPKAPEGS-EGFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDYrdlFSA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 893 ILSDFHVFDRLYGINtEGMKAEIDH---YLELLQLSDKVGIEDGRF-TTTQLSTGQKKRLALLVTYLEDRPILLFDEWAA 968
Cdd:TIGR01194 421 IFADFHLFDDLIGPD-EGEHASLDNaqqYLQRLEIADKVKIEDGGFsTTTALSTGQQKRLALICAWLEDRPILLFDEWAA 499
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1005564688 969 DQDPGYRRFFYEELLPQMRAKGKCIIAITHDDQYFHLADKLIVMEMGTV 1017
Cdd:TIGR01194 500 DQDPAFKRFFYEELLPDLKRQGKTIIIISHDDQYFELADQIIKLAAGCI 548
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
485-1016 |
5.25e-90 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 298.81 E-value: 5.25e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 485 TFLNLCFpRQKGKSLLTLIVLGLIS-GFGNAFLIFvINETFVRSNNLENGLLFYFVLGIVMYVFSQRIIRTSIVSYTNEL 563
Cdd:PRK10522 2 ELLRLVW-RQYRWPFISVMALSLASaALGIGLIAF-INQRLIETADTSLLVLPEFLGLLLLLMAVTLGSQLALTTLGHHF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 564 VYEKRMELTDKLLQTPYYKLELIEKGRIEATLNNDTEVISRSLNLLVTAGTSLLTLLFCFLYLGVMNMYAFLLSLCIIFI 643
Cdd:PRK10522 80 VYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITIAFVRLPELVQGIILTLGSAAYLAWLSPKMLLVTAIWMAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 644 TA-GVYSLIGR--QADKVWNETRD-IQNVYFRLIgdlrHGFKELRLHTGK-RNDFREVMNESCNNYRVKRTIGDI----- 713
Cdd:PRK10522 160 TIwGGFVLVARvyKHMATLRETEDkLYNDYQTVL----EGRKELTLNRERaEYVFENEYEPDAQEYRHHIIRADTfhlsa 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 714 -KFANVFVLGellfifVIGIVVFVFPEI-FVNMpkETISNYVIVFLYMTGPVNEILGGIPQLVNVRISWQRIQQMvksvd 791
Cdd:PRK10522 236 vNWSNIMMLG------AIGLVFYMANSLgWADT--NVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNKL----- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 792 hikaneQIATTKEYLDVPIC------LQLQNVSYKYKNkdgdfTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITG 865
Cdd:PRK10522 303 ------ALAPYKAEFPRPQAfpdwqtLELRNVTFAYQD-----NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 866 LYEPNEGNVLLNGKEIAPEELNQY---YSAILSDFHVFDRLYGI-NTEGMKAEIDHYLELLQLSDKVGIEDGRFTTTQLS 941
Cdd:PRK10522 372 LYQPQSGEILLDGKPVTAEQPEDYrklFSAVFTDFHLFDQLLGPeGKPANPALVEKWLERLKMAHKLELEDGRISNLKLS 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005564688 942 TGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHDDQYFHLADKLIVMEMGT 1016
Cdd:PRK10522 452 KGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| AmpC |
COG1680 |
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms]; |
34-349 |
1.17e-80 |
|
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];
Pssm-ID: 441286 [Multi-domain] Cd Length: 355 Bit Score: 266.55 E-value: 1.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 34 KKIQKHIEEQISQAGIPGLSVVIVKGNETIYKKNYGYANTDKKRQVTNETLFELGSTSKAFTALAVLQLEKEGKIKLSDS 113
Cdd:COG1680 17 AALDAALDAALAEGGIPGAAVAVVRDGKVVYEKAYGVADLETGRPVTPDTLFRIASVTKSFTATAVLQLVEEGKLDLDDP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 114 LTKYVSWFEMEYKGKPyEITLYDLLHHTSGIPEKAIGYIPITNGKD--SIEKTIRNVMPIGLNREPGSSFEYSTVNYDLL 191
Cdd:COG1680 97 VSKYLPEFKLPDDAKR-DITVRHLLTHTSGLPDYEPDPYDAADVARpyTPDDLLARLAALPLLFEPGTRFSYSNLGYDLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 192 GLVIEKATNQSFERYVQDHVLSKLDLLSTYAGREMAPLDNMAQGYKRNflqSLPYDAPNYRGNT-PAGYFISNINDMERW 270
Cdd:COG1680 176 GEIIERVTGQPLEDYLRERIFEPLGMTDTGFGLPDAEAARLAPGYEAD---GEVHDAPAWLGAVaGAGGLFSTARDLARF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 271 LKLQLG---VEKPRMFPEELINDSHKANRKVAPDSNGasYAAGWEVYQSGGGE-ISHGGSNPNYSSYIGFRDEEQIGVVV 346
Cdd:COG1680 253 GQALLNggeWDGKRLLSPETLAEMTTPQVPSGDAGGG--YGLGWWLNDDGGSGsFGHGGATPGFSTFLWVDPERGLGVVV 330
|
...
gi 1005564688 347 LAN 349
Cdd:COG1680 331 LTN 333
|
|
| Beta-lactamase |
pfam00144 |
Beta-lactamase; This family appears to be distantly related to pfam00905 and PF00768 ... |
36-351 |
1.32e-64 |
|
Beta-lactamase; This family appears to be distantly related to pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.
Pssm-ID: 395092 [Multi-domain] Cd Length: 327 Bit Score: 221.61 E-value: 1.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 36 IQKHIEEQISQAGIPGLSVVIVKGNETIYKKNYGYANTDKKRQVTNETLFELGSTSKAFTALAVLQLEKEGKIKLSDSLT 115
Cdd:pfam00144 1 LDRLIRELMAQGGIPGVAVAVTRDGKVVVDRGGGVADLEGGRPVTADTLFRIASVTKTFTAAAVLQLVERGKLDLDDPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 116 KYVSWFEMEYKGKpyeITLYDLLHHTSGIPEKAIGYIPITNGKDSiEKTIRNVMPIGLNREPGSSFEYSTVNYDLLGLVI 195
Cdd:pfam00144 81 KYLPEFAGPGKGG---ITLRDLLTHTSGLPPLFAPDDLEEAAADA-AELVRALAALPPVWPPGTRWGYSNTAYGLLGELL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 196 EKATNQSFERYVQDHVLSKLDLLSTYAGREMAPLDNMAQGYKRNFlqSLPYDAPNYRGNTPAGYFISNINDMERWLKLQL 275
Cdd:pfam00144 157 ERVTGQSYEELLGDRILRPLGMTDTELGVPEPGDPRDAAGYTGEG--PPVRVPPGPLPAGAYGGLKSTARDLARFLLALL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 276 GVEKP-RMFPEELIndSHKANRKVAPDSNGASYAAGWEVYQ---SGGGEISHGGsnpNYSSYIGFRDEEQIGVVVLANLN 351
Cdd:pfam00144 235 GGLLLsAAALAQLT--DWLRGGTTGVGGIRAGLGLGWVLADktgAGPGLFGHTG---GYGTYLAVDPDIGLVVVVLSNRL 309
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
497-1017 |
4.65e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 144.92 E-value: 4.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 497 KSLLTLIVLGLISGFGNAFLIF----VINETFVRSN--NLENGLLFYFVLGIVMYVFSqRIIRTSIVSYTNELVYEKRME 570
Cdd:COG1132 21 GLLILALLLLLLSALLELLLPLllgrIIDALLAGGDlsALLLLLLLLLGLALLRALLS-YLQRYLLARLAQRVVADLRRD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 571 LTDKLLQTPYYKLELIEKGRIEATLNNDTEVISRSL-NLLVTAGTSLLTLLFCFLYLGVMNMYAFLLSLCIIFITAGVYS 649
Cdd:COG1132 100 LFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 650 LIGRQADKVWNETRDIQNVYFRLIGDLRHGFKELRLHtGKRNDFREVMNESCNNYRVKRTIGDIKFANVFVLGELLFIFV 729
Cdd:COG1132 180 LFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAF-GREERELERFREANEELRRANLRAARLSALFFPLMELLGNLG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 730 IGIVVFVFPeIFVNMPKETISNYVIVFLY---MTGPVNEILGGIPQLVNVRISWQRIQQMvksvdhIKANEQIATTKEYL 806
Cdd:COG1132 259 LALVLLVGG-LLVLSGSLTVGDLVAFILYllrLFGPLRQLANVLNQLQRALASAERIFEL------LDEPPEIPDPPGAV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 807 DVPIC---LQLQNVSYKYKNKDGDFTGfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNG---KE 880
Cdd:COG1132 332 PLPPVrgeIEFENVSFSYPGDRPVLKD-----ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 881 IAPEELNQYYSAILSDFHVFDR------LYGiNTEGMKAEIDHYLELLQLSD-----------KVGiEDGrfttTQLSTG 943
Cdd:COG1132 407 LTLESLRRQIGVVPQDTFLFSGtireniRYG-RPDATDEEVEEAAKAAQAHEfiealpdgydtVVG-ERG----VNLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 944 QKKRLALLVTYLEDRPILLFDEWAADQDPG-----YRRFfyEELLpqmraKGKCIIAITHddqyfHL-----ADKLIVME 1013
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTEtealiQEAL--ERLM-----KGRTTIVIAH-----RLstirnADRILVLD 548
|
....
gi 1005564688 1014 MGTV 1017
Cdd:COG1132 549 DGRI 552
|
|
| ampC |
PRK11289 |
beta-lactamase/D-alanine carboxypeptidase; Provisional |
1-351 |
2.94e-35 |
|
beta-lactamase/D-alanine carboxypeptidase; Provisional
Pssm-ID: 236894 Cd Length: 384 Bit Score: 138.87 E-value: 2.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 1 MKLNIWLKFIILMTLIVLPYRQVEAQETVQVnEKKIQKHIEEQISQAGIPGLSV-VIVKGNETIYkkNYGYANTDKKRQV 79
Cdd:PRK11289 1 KMKMMLLLLLAALLLTASASAFAAAATPQQL-KDIVDRTITPLMEEQDIPGMAVaVIYNGKPYYF--NYGVADKATGQPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 80 TNETLFELGSTSKAFTA-LAVLQLEKeGKIKLSDSLTKYVSwfemEYKGKPY-EITLYDLLHHTSG-----IPEKaigyi 152
Cdd:PRK11289 78 TQDTLFELGSVSKTFTAtLAGYAQAR-GELSLSDPASKYLP----ELKGSPFdGITLLHLATYTAGglplqVPDE----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 153 pITNgKDSIEKTIRNVMPIglnREPGSSFEYSTVNYDLLGLVIEKATNQSFERYVQDHVLSKLDLLSTYAGREMAPLDNM 232
Cdd:PRK11289 148 -VKD-DAQLLRYFQAWQPA---YAPGTQRLYSNPSIGLFGYLAAKAMGQPFEQLMEQRLFPPLGLTHTYINVPEAEMADY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 233 AQGYKRNflqslpyDAPnYRGNtPA-----GYFI-SNINDMERWLKLQLGVEKprmFPEEL---INDSHKANRKVAPDSN 303
Cdd:PRK11289 223 AQGYNKE-------GKP-VRVN-PGvldaeAYGVkSTAADMLRFVQANLGPQD---LDPTLqqaIQLTQTGYFRVGDMTQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 304 GasyaAGWEVY---------QSGGGE-----------------------ISHGGSNPNYSSYIGFRDEEQIGVVVLANLN 351
Cdd:PRK11289 291 G----LGWEMYpypvsldtlLAGNSNkmalepqpvtaitppqppvravwINKTGSTNGFGAYVAFVPAKRLGIVMLANKN 366
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
497-1026 |
2.30e-34 |
|
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: 141.51 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 497 KSLLTLIVLGLISG-FGNAFLIF---VINeTFVRSNNLEngLLFYFVLGIVMYVFSQ---RIIRTSIVSYTnelvyEKRM 569
Cdd:COG2274 156 RLLLQVLLASLLINlLALATPLFtqvVID-RVLPNQDLS--TLWVLAIGLLLALLFEgllRLLRSYLLLRL-----GQRI 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 570 ------ELTDKLLQTPyykLELIEKGRIEATLN--NDTEVISRSL-NLLVTAgtsLLTLLFCFLYLGVMNMY-------A 633
Cdd:COG2274 228 dlrlssRFFRHLLRLP---LSFFESRSVGDLASrfRDVESIREFLtGSLLTA---LLDLLFVLIFLIVLFFYspplalvV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 634 FLLSLCIIFITAGVYSLIGRQADKVWNETRDIQNVyfrLIGDLRhGFKELRLhTGKRNDFREVMNESCNNYrVKRTIGDI 713
Cdd:COG2274 302 LLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSL---LVETLR-GIETIKA-LGAESRFRRRWENLLAKY-LNARFKLR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 714 KFANVFVLGELLFIFVIGIVVFVFPEIFVnmpketISN---------YVIVFLYMTGPVNEILGGIPQLVNVRISWQRIQ 784
Cdd:COG2274 376 RLSNLLSTLSGLLQQLATVALLWLGAYLV------IDGqltlgqliaFNILSGRFLAPVAQLIGLLQRFQDAKIALERLD 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 785 QMVKSVDhikanEQiATTKEYLDVPIC---LQLQNVSYKYKNKDGD-FTGfgigpIDMEFNSGEIVFIAGGNGSGKSTLS 860
Cdd:COG2274 450 DILDLPP-----ER-EEGRSKLSLPRLkgdIELENVSFRYPGDSPPvLDN-----ISLTIKPGERVAIVGRSGSGKSTLL 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 861 KLITGLYEPNEGNVLLNG---KEIAPEELNQYYSAILSDFHVFDR---------LYGINTEgmkaEIDHYLELLQLSD-- 926
Cdd:COG2274 519 KLLLGLYEPTSGRILIDGidlRQIDPASLRRQIGVVLQDVFLFSGtirenitlgDPDATDE----EIIEAARLAGLHDfi 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 927 ---------KVGiEDGRftttQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELlpQMRAKGKCIIAIT 997
Cdd:COG2274 595 ealpmgydtVVG-EGGS----NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL--RRLLKGRTVIIIA 667
|
570 580
....*....|....*....|....*....
gi 1005564688 998 HDDQYFHLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:COG2274 668 HRLSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
813-1016 |
1.43e-33 |
|
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: 128.74 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 813 QLQNVSYKYknkdGDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQYYSA 892
Cdd:cd03225 1 ELKNLSFSY----PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 893 ILSDF----------HVFD------RLYGINTEGMKAEIDHYLELLQLSDKvgieDGRFTTTqLSTGQKKRLALLVTYLE 956
Cdd:cd03225 77 VGLVFqnpddqffgpTVEEevafglENLGLPEEEIEERVEEALELVGLEGL----RDRSPFT-LSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005564688 957 DRPILLFDEWAADQDP-GYRRFFyeELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGT 1016
Cdd:cd03225 152 DPDILLLDEPTAGLDPaGRRELL--ELLKKLKAEGKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
812-1027 |
3.14e-33 |
|
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: 128.82 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKdgdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA--PEELNQY 889
Cdd:COG4555 2 IEVENLSKKYGKV------PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkePREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 890 YSAILSDFHVFDRL------------YGINTEGMKAEIDHYLELLQLSDkvgIEDGRftTTQLSTGQKKRLALLVTYLED 957
Cdd:COG4555 76 IGVLPDERGLYDRLtvreniryfaelYGLFDEELKKRIEELIELLGLEE---FLDRR--VGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005564688 958 RPILLFDEWAADQDPGYRRFFYEELLpQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTVKMNKTKEALS 1027
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILR-ALKKEGKTVLFSSHImQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
606-1026 |
2.92e-32 |
|
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: 133.35 E-value: 2.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 606 LNLLVTAGTSLLTLLFCFLYLGVMNMyAFLLSLCIIFITAGV-----YSLIGRQADKVWNETRdiQNVYFRLIgDLRHGF 680
Cdd:COG4987 130 LRVLLPLLVALLVILAAVAFLAFFSP-ALALVLALGLLLAGLllpllAARLGRRAGRRLAAAR--AALRARLT-DLLQGA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 681 KELRLHtGKRNDFREVMNESCNNY-----RVKRTIGDIKFANVFVLGellfIFVIGIVVFVFPEIFVNmpkeTIS-NYVI 754
Cdd:COG4987 206 AELAAY-GALDRALARLDAAEARLaaaqrRLARLSALAQALLQLAAG----LAVVAVLWLAAPLVAAG----ALSgPLLA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 755 VFLYMTGPVNEILGGIP----QLVNVRISWQRIQQMVKSVDHIKANEQIATtkeyLDVPICLQLQNVSYKYKNKDGDftg 830
Cdd:COG4987 277 LLVLAALALFEALAPLPaaaqHLGRVRAAARRLNELLDAPPAVTEPAEPAP----APGGPSLELEDVSFRYPGAGRP--- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 831 fGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELNQYYSAILSDFHVFD------ 901
Cdd:COG4987 350 -VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdldEDDLRRRIAVVPQRPHLFDttlren 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 902 -RLYGIN-TEgmkAEIDHYLELLQLSD-----------KVGiEDGRftttQLSTGQKKRLALLVTYLEDRPILLFDEWAA 968
Cdd:COG4987 429 lRLARPDaTD---EELWAALERVGLGDwlaalpdgldtWLG-EGGR----RLSGGERRRLALARALLRDAPILLLDEPTE 500
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005564688 969 DQDPGYRRFFYEELLPQMraKGKCIIAITHDDQYFHLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:COG4987 501 GLDAATEQALLADLLEAL--AGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
812-1027 |
1.52e-31 |
|
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: 123.60 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDgdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEL----- 886
Cdd:COG1122 1 IELENLSFSYPGGT-----PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLrelrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 ----------NQYYSAIlsdfhVFD------RLYGINTEGMKAEIDHYLELlqlsdkVGIED-GRFTTTQLSTGQKKRLA 949
Cdd:COG1122 76 kvglvfqnpdDQLFAPT-----VEEdvafgpENLGLPREEIRERVEEALEL------VGLEHlADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 950 L---LVTyledRP-ILLFDEWAADQDPGYRRFFYeELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTVKMN-KTK 1023
Cdd:COG1122 145 IagvLAM----EPeVLVLDEPTAGLDPRGRRELL-ELLKRLNKEGKTVIIVTHDlDLVAELADRVIVLDDGRIVADgTPR 219
|
....
gi 1005564688 1024 EALS 1027
Cdd:COG1122 220 EVFS 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
812-1015 |
2.32e-31 |
|
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: 120.95 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNG---KEIAPEELNQ 888
Cdd:cd03228 1 IEFKNVSFSYPGRPK----PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlRDLDLESLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 YYSAILSDFHVFDRlyginTegmkaeidhylellqLSDKVgiedgrftttqLSTGQKKRLALLVTYLEDRPILLFDEWAA 968
Cdd:cd03228 77 NIAYVPQDPFLFSG-----T---------------IRENI-----------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1005564688 969 DQDPGYRRFFYEELLPQMraKGKCIIAITHDDQYFHLADKLIVMEMG 1015
Cdd:cd03228 126 ALDPETEALILEALRALA--KGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
813-1026 |
1.04e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 116.63 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 813 QLQNVSYKYKNKDGdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEL------ 886
Cdd:PRK13632 9 KVENVSFSYPNSEN----NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLkeirkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 ---------NQYYSAILSDfhvfDRLYG-----INTEGMKAEIDHYlellqlSDKVGIEDG-RFTTTQLSTGQKKRLALL 951
Cdd:PRK13632 85 igiifqnpdNQFIGATVED----DIAFGlenkkVPPKKMKDIIDDL------AKKVGMEDYlDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005564688 952 VTYLEDRPILLFDEWAADQDPGYRRFFYeELLPQMRAKG-KCIIAITHDDQYFHLADKLIVMEMGT-VKMNKTKEAL 1026
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIK-KIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKlIAQGKPKEIL 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
813-1016 |
2.03e-28 |
|
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: 111.95 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 813 QLQNVSYKYKNKdgdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPeelnqyysa 892
Cdd:cd00267 1 EIENLSFRYGGR------TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 893 ilsdfhvfdrlygintegmkaeidhyLELLQLSDKVGIedgrftTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDP 972
Cdd:cd00267 66 --------------------------LPLEELRRRIGY------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1005564688 973 gYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGT 1016
Cdd:cd00267 114 -ASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVLKDGK 157
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
812-1017 |
2.53e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.37 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGdftgfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGK---EIAPEEL-- 886
Cdd:COG4619 1 LELEGLSFRVGGKPI------LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsAMPPPEWrr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 --------NQYYSAILSDFhvFDRLYGINTEGMKAE-IDHYLELLQLS----DKvgiedgrfTTTQLSTGQKKRLALLVT 953
Cdd:COG4619 75 qvayvpqePALWGGTVRDN--LPFPFQLRERKFDRErALELLERLGLPpdilDK--------PVERLSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005564688 954 YLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDpEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
812-1000 |
5.00e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 112.57 E-value: 5.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYknkdGDFTGFGigPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI--APEELNQY 889
Cdd:COG4133 3 LEAENLSCRR----GERLLFS--GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrdAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 890 ------YSAILSDFHVFD------RLYGINTEGmkAEIDHYLELLQLSdkvGIEDGRFttTQLSTGQKKRLALLVTYLED 957
Cdd:COG4133 77 laylghADGLKPELTVREnlrfwaALYGLRADR--EAIDEALEAVGLA---GLADLPV--RQLSAGQKRRVALARLLLSP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1005564688 958 RPILLFDE-WAA-DQDpGYRRFfyEELLPQMRAKGKCIIAITHDD 1000
Cdd:COG4133 150 APLWLLDEpFTAlDAA-GVALL--AELIAAHLARGGAVLLTTHQP 191
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
812-1019 |
2.41e-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 upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 112.52 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKN------KDgdftgfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEE 885
Cdd:TIGR04520 1 IEVENVSFSYPEsekpalKN----------VSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 886 L----------------NQYYSAILSD---FHVFDRlyGINTEGMKAEIDHYLELlqlsdkVGIEDGR-FTTTQLSTGQK 945
Cdd:TIGR04520 71 NlweirkkvgmvfqnpdNQFVGATVEDdvaFGLENL--GVPREEMRKRVDEALKL------VGMEDFRdREPHLLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 946 KR------LALlvtyledRP-ILLFDEWAADQDPGYRRffyeELLPQMRA----KGKCIIAITHDDQYFHLADKLIVMEM 1014
Cdd:TIGR04520 143 QRvaiagvLAM-------RPdIIILDEATSMLDPKGRK----EVLETIRKlnkeEGITVISITHDMEEAVLADRVIVMNK 211
|
....*
gi 1005564688 1015 GTVKM 1019
Cdd:TIGR04520 212 GKIVA 216
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
812-1026 |
7.57e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.15 E-value: 7.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYknkdGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA--PEELNQY 889
Cdd:COG1131 1 IEVRGLTKRY----GDKTA--LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVArdPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 890 YSAILSDFHVFD------------RLYGINTEGMKAEIDHYLELLQLSD----KVGiedgrftttQLSTGQKKRLALLVT 953
Cdd:COG1131 75 IGYVPQEPALYPdltvrenlrffaRLYGLPRKEARERIDELLELFGLTDaadrKVG---------TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 954 YLEDRPILLFDEWAADQDPGYRRFFYEELLpQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLR-ELAAEGKTVLLSTHYlEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| PRK03642 |
PRK03642 |
putative periplasmic esterase; Provisional |
27-313 |
1.34e-26 |
|
putative periplasmic esterase; Provisional
Pssm-ID: 179620 [Multi-domain] Cd Length: 432 Bit Score: 114.12 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 27 ETVQVNEKKIQK---HIEEQISqAGIPGLSVVIVKGNETIYKKNYGYA-----NTDKKR--QVTNETLFELGSTSKAF-T 95
Cdd:PRK03642 31 EKAGFNSEKLNQmdrWISQQID-AGYPGVNLLIIKDNQIVYRKAWGYAkkydgSTLLAHpvKATTNTMYDLASNTKMYaT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 96 ALAVLQLEKEGKIKLSDSLTKYVSWFEME----YKGKPyEITLYDLLHHTSGIPEKAIGYIPITNGK---DSIEKTIRNV 168
Cdd:PRK03642 110 NFALQKLVSEGKLDVNDLISKYIPGFKDSpgdkIKGKN-TLRIIDLLHHSAGFPADPQYPNKAVAGAlysQDKSTTLEMI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 169 MPIGLNREPGSSFEYSTVNYDLLGLVIEKATNQSFERYVQDHVLSKLDLLSTYagreMAPLDnmaQGYKRNFLQSLP--- 245
Cdd:PRK03642 189 KKTPLEYQPGSKHIYSDVDYMLLGFIVESITGQPLDRYVEESIYRPLGLTHTV----FNPLQ---KGFKPQQIAATElng 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 246 ------YDAPNYRGNT-------------------PAGYFiSNINDMERWLKLQL---GVEKPRMFpeelinDSHKANRK 297
Cdd:PRK03642 262 ntrdgvIHFPNIRTNTlwgqvhdekafysmggvsgHAGLF-SNTGDMAVLMQVMLnggGYGNVQLF------DAETVKMF 334
|
330
....*....|....*.
gi 1005564688 298 VAPDSNGASYAAGWEV 313
Cdd:PRK03642 335 TTSSKEDATFGLGWRV 350
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
835-968 |
2.28e-25 |
|
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: 103.11 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 835 PIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQY---YSAILSDFHVFDR--------- 902
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrkeIGYVFQDPQLFPRltvrenlrl 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005564688 903 ---LYGINTEGMKAEIDHYLELLQLSDKVGIEDGRFTTTqLSTGQKKRLALLVTYLEDRPILLFDEWAA 968
Cdd:pfam00005 83 gllLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGT-LSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
812-1019 |
2.62e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 105.28 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDG---DFTGFGIGPidmefnsGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA--PEEL 886
Cdd:cd03263 1 LQIRNLTKTYKKGTKpavDDLSLNVYK-------GEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtdRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 NQY------YSAILSDF----HV--FDRLYGINTEGMKAEIDHYLELLQLSDKvgiEDGRftTTQLSTGQKKRLALLVTY 954
Cdd:cd03263 74 RQSlgycpqFDALFDELtvreHLrfYARLKGLPKSEIKEEVELLLRVLGLTDK---ANKR--ARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005564688 955 LEDRPILLFDEWAADQDPGYRRFFYeELLPQMRaKGKCIIAITHD-DQYFHLADKLIVMEMGTVKM 1019
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIW-DLILEVR-KGRSIILTTHSmDEAEALCDRIAIMSDGKLRC 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
812-1012 |
3.13e-25 |
|
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: 104.86 E-value: 3.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFTGFGigPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQYYs 891
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALE--DISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 892 aILSDFHVFDRL-------YGINTEGM-----KAEIDHYLELLQLSdkvGIEDGRftTTQLSTGQKKRLALLVTYLEDRP 959
Cdd:cd03293 78 -VFQQDALLPWLtvldnvaLGLELQGVpkaeaRERAEELLELVGLS---GFENAY--PHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 960 ILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVM 1012
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDiDEAVFLADRVVVL 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
813-1017 |
2.06e-24 |
|
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: 101.36 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 813 QLQNVSYKYKNKdgdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIApeelnQYYSA 892
Cdd:cd03214 1 EVENLSVGYGGR------TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA-----SLSPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 893 ILSdfhvfdRLYGIntegmkaeidhyleLLQLSDKVGIED--GRFTTTqLSTGQKKRLALLVTYLEDRPILLFDEWAADQ 970
Cdd:cd03214 70 ELA------RKIAY--------------VPQALELLGLAHlaDRPFNE-LSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1005564688 971 DPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03214 129 DIAHQIELLELLRRLARERGKTVVMVLHDlNLAARYADRVILLKDGRI 176
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
812-1017 |
2.86e-24 |
|
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: 100.55 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKdgdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA--PEELNQY 889
Cdd:cd03230 1 IEVRNLSKRYGKK------TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKkePEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 890 YSAILSDFHVFDRLYGIntegmkaeidhylELLqlsdkvgiedgrftttQLSTGQKKRLALLVTYLEDRPILLFDEWAAD 969
Cdd:cd03230 75 IGYLPEEPSLYENLTVR-------------ENL----------------KLSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1005564688 970 QDPGYRRFFYEELLpQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03230 126 LDPESRREFWELLR-ELKKEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
809-1017 |
2.20e-23 |
|
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: 105.61 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 809 PICLQLQNVSYKYknkDGDftGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEE 885
Cdd:COG4988 334 PPSIELEDVSFSY---PGG--RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSdldPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 886 LNQYYSAILSDFHVFD-------RLYGIN-TEgmkAEIDHYLELLQLSD-----------KVGiEDGRftttQLSTGQKK 946
Cdd:COG4988 409 WRRQIAWVPQNPYLFAgtirenlRLGRPDaSD---EELEAALEAAGLDEfvaalpdgldtPLG-EGGR----GLSGGQAQ 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005564688 947 RLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELLPqmRAKGKCIIAITHDDQYFHLADKLIVMEMGTV 1017
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR--LAKGRTVILITHRLALLAQADRILVLDDGRI 549
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
836-1018 |
1.19e-22 |
|
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: 96.94 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEL--NQYYSAILSDFH-----VFDRLY-GI- 906
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERrkSIGYVMQDVDYQlftdsVREELLlGLk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 907 NTEGMKAEIDHYLELLQLSDKVgiEDGRFTttqLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFyEELLPQM 986
Cdd:cd03226 99 ELDAGNEQAETVLKDLDLYALK--ERHPLS---LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV-GELIREL 172
|
170 180 190
....*....|....*....|....*....|...
gi 1005564688 987 RAKGKCIIAITHDDQY-FHLADKLIVMEMGTVK 1018
Cdd:cd03226 173 AAQGKAVIVITHDYEFlAKVCDRVLLLANGAIV 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
812-1019 |
4.27e-22 |
|
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: 94.69 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFtgfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA--PEELNQY 889
Cdd:cd03247 1 LSINNVSFSYPEQEQQV----LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSdlEKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 890 YSAILSDFHVFDRlygintegmkaeidhylellQLSDKVGiedgrfttTQLSTGQKKRLALLVTYLEDRPILLFDEWAAD 969
Cdd:cd03247 77 ISVLNQRPYLFDT--------------------TLRNNLG--------RRFSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1005564688 970 QDPGYRRffyeELLPQM--RAKGKCIIAITHDDQYFHLADKLIVMEMGTVKM 1019
Cdd:cd03247 129 LDPITER----QLLSLIfeVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
812-1015 |
8.43e-22 |
|
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: 94.96 E-value: 8.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKN------KDGDFTgfgIGPidmefnsGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNG---KEIA 882
Cdd:cd03245 3 IEFRNVSFSYPNqeipalDNVSLT---IRA-------GEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 883 PEELNQYYSAILSDFHVF-----DRLYGINTEGMKAEIDHYLELLQLSDKVGI----------EDGRFtttqLSTGQKKR 947
Cdd:cd03245 73 PADLRRNIGYVPQDVTLFygtlrDNITLGAPLADDERILRAAELAGVTDFVNKhpngldlqigERGRG----LSGGQRQA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005564688 948 LALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELlpQMRAKGKCIIAITHDDQYFHLADKLIVMEMG 1015
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERL--RQLLGDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
812-1017 |
8.77e-22 |
|
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: 95.88 E-value: 8.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKdgdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELNQ 888
Cdd:COG1120 2 LEAENLSVGYGGR------PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAslsRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 Y--Y----SAILSDFHVFD----------RLYGINTEGMKAEIDHYLELLQLSDkvgIEDGRFTTtqLSTGQKKRLAL-- 950
Cdd:COG1120 76 RiaYvpqePPAPFGLTVRElvalgryphlGLFGRPSAEDREAVEEALERTGLEH---LADRPVDE--LSGGERQRVLIar 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005564688 951 -LVTyleDRPILLFDEWAADQDPGYRrffyEELLPQMRA----KGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:COG1120 151 aLAQ---EPPLLLLDEPTSHLDLAHQ----LEVLELLRRlareRGRTVVMVLHDlNLAARYADRLVLLKDGRI 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
811-1027 |
1.04e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 95.54 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 811 CLQLQNVSYKYKNK---DGdftgfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELN 887
Cdd:COG1121 6 AIELENLTVSYGGRpvlED---------VSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 888 -----QyYSAILSDF--HVFD----------RLYGINTEGMKAEIDHYLELLQLSD----KVGiedgrftttQLSTGQKK 946
Cdd:COG1121 77 igyvpQ-RAEVDWDFpiTVRDvvlmgrygrrGLFRRPSRADREAVDEALERVGLEDladrPIG---------ELSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 947 RLAL---LVTyleDRPILLFDEWAADQDPGYRRFFYeELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTVKMNKT 1022
Cdd:COG1121 147 RVLLaraLAQ---DPDLLLLDEPFAGVDAATEEALY-ELLRELRREGKTILVVTHDlGAVREYFDRVLLLNRGLVAHGPP 222
|
....*
gi 1005564688 1023 KEALS 1027
Cdd:COG1121 223 EEVLT 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
812-1026 |
1.56e-21 |
|
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: 94.67 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDgdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELNQ 888
Cdd:cd03295 1 IEFENVTKRYGGGK-----KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqdPVELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 YYSAILSDFHVFD------------RLYGINTEGMKAEIDhylELLQLsdkVGIEDGRFT---TTQLSTGQKKRLALLVT 953
Cdd:cd03295 76 KIGYVIQQIGLFPhmtveenialvpKLLKWPKEKIRERAD---ELLAL---VGLDPAEFAdryPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 954 YLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDiDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
812-1017 |
1.87e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 93.95 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFTGFGIgpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEEL-- 886
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRG--VSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslsERELar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 --NQYYSAILSDFHVFDRL------------YGINTEGMKAEIDHYLELLQLSDKVgiedgRFTTTQLSTGQKKRLAL-- 950
Cdd:COG1136 83 lrRRHIGFVFQFFNLLPELtalenvalplllAGVSRKERRERARELLERVGLGDRL-----DHRPSQLSGGQQQRVAIar 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005564688 951 -LVTyleDRPILLFDE--WAADQDPGyRRFFyeELLPQM-RAKGKCIIAITHDDQYFHLADKLIVMEMGTV 1017
Cdd:COG1136 158 aLVN---RPKLILADEptGNLDSKTG-EEVL--ELLRELnRELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
813-999 |
3.60e-21 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 92.98 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 813 QLQNVSYKYKNK----DGDFtgfgigpidmEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEE--- 885
Cdd:cd03235 1 EVEDLTVSYGGHpvleDVSF----------EVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkri 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 886 --LNQYYSaILSDF--HVFD----------RLYGINTEGMKAEIDHYLELLQLSDkvgIEDGRFttTQLSTGQKKRLAL- 950
Cdd:cd03235 71 gyVPQRRS-IDRDFpiSVRDvvlmglyghkGLFRRLSKADKAKVDEALERVGLSE---LADRQI--GELSGGQQQRVLLa 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1005564688 951 --LVTyleDRPILLFDEWAADQDPGYRRFFYeELLPQMRAKGKCIIAITHD 999
Cdd:cd03235 145 raLVQ---DPDLLLLDEPFAGVDPKTQEDIY-ELLRELRREGMTILVVTHD 191
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
812-1017 |
5.19e-21 |
|
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: 92.58 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKdgdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELN- 887
Cdd:cd03259 1 LELKGLSKTYGSV------RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTgvpPERRNi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 888 ----QYYsAILSDFHVFDRL-YGINTEGM-KAEI-DHYLELLQLsdkVGIED--GRFtTTQLSTGQKKRLALLVTYLEDR 958
Cdd:cd03259 75 gmvfQDY-ALFPHLTVAENIaFGLKLRGVpKAEIrARVRELLEL---VGLEGllNRY-PHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 959 PILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDqEEALALADRIAVMNEGRI 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
812-1017 |
7.42e-21 |
|
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: 92.17 E-value: 7.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNkdGDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELNQ 888
Cdd:cd03255 1 IELKNLSKTYGG--GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklsEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 YY----------SAILSDFHVFD------RLYGINTEGMKAEIdhyLELLqlsDKVGIEDgRFTT--TQLSTGQKKRLAL 950
Cdd:cd03255 79 FRrrhigfvfqsFNLLPDLTALEnvelplLLAGVPKKERRERA---EELL---ERVGLGD-RLNHypSELSGGQQQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 951 ---LVTyleDRPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHDDQYFHLADKLIVMEMGTV 1017
Cdd:cd03255 152 araLAN---DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
836-1026 |
8.30e-21 |
|
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: 92.74 E-value: 8.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELNQY---------YSAILSDFHVFD-- 901
Cdd:COG1127 24 VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglsEKELYELrrrigmlfqGGALFDSLTVFEnv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 902 ----RLYGINTEGMKAEI-DHYLELLQLSdkvGIEDgRFtTTQLSTGQKKRLAL---LVTyleDRPILLFDEWAADQDP- 972
Cdd:COG1127 104 afplREHTDLSEAEIRELvLEKLELVGLP---GAAD-KM-PSELSGGMRKRVALaraLAL---DPEILLYDEPTAGLDPi 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1005564688 973 GYRRFfyEELLPQMRAK-GKCIIAITHDDQY-FHLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:COG1127 176 TSAVI--DELIRELRDElGLTSVVVTHDLDSaFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
836-1026 |
1.20e-20 |
|
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: 92.18 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQYY------------SAILSDFHVFD-- 901
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYrlrrrmgmlfqsGALFDSLTVFEnv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 902 ----RLYGINTEGMKAEIdhYLELLQLsdkVGIE-DGRFTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPgYRR 976
Cdd:cd03261 99 afplREHTRLSEEEIREI--VLEKLEA---VGLRgAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP-IAS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1005564688 977 FFYEELLPQM-RAKGKCIIAITHD-DQYFHLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:cd03261 173 GVIDDLIRSLkKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
812-1018 |
1.24e-20 |
|
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: 91.49 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGdftgfgIGPIDMEFNSGEIVFIaGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI--APEELNQY 889
Cdd:cd03264 1 LQLENLTKRYGKKRA------LDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlkQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 890 YSAILSDFHVFDR------------LYGINTEGMKAEIDHYLELLQLSD----KVGiedgrftttQLSTGQKKRLALLVT 953
Cdd:cd03264 74 IGYLPQEFGVYPNftvrefldyiawLKGIPSKEVKARVDEVLELVNLGDrakkKIG---------SLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005564688 954 YLEDRPILLFDEWAADQDPGYR-RFfyEELLPQMrAKGKCIIAITH---DDQYfhLADKLIVMEMGTVK 1018
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERiRF--RNLLSEL-GEDRIVILSTHiveDVES--LCNQVAVLNKGKLV 208
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
836-1017 |
1.37e-20 |
|
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: 92.71 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAP---EELNQ----YYSAILSDFHVFDRL----- 903
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrKELRElrrkKISMVFQSFALLPHRtvlen 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 904 --YGINTEGMKAEIDHY--LELLQLsdkVGIED-GRFTTTQLSTGQKKRLAL---LVTyleDRPILLFDEWAADQDPGYR 975
Cdd:cd03294 123 vaFGLEVQGVPRAEREEraAEALEL---VGLEGwEHKYPDELSGGMQQRVGLaraLAV---DPDILLMDEAFSALDPLIR 196
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1005564688 976 RFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03294 197 REMQDELLRLQAELQKTIVFITHDlDEALRLGDRIAIMKDGRL 239
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
836-1017 |
6.17e-20 |
|
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: 87.87 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIapeelnqyysAILSDFHvfdrlygintegmkaei 915
Cdd:cd03216 19 VSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV----------SFASPRD----------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 916 dhylellqlSDKVGIEdgrfTTTQLSTGQKKRLALLVTYLEDRPILLFDE-WAADQDPGYRRFFyeELLPQMRAKGKCII 994
Cdd:cd03216 72 ---------ARRAGIA----MVYQLSVGERQMVEIARALARNARLLILDEpTAALTPAEVERLF--KVIRRLRAQGVAVI 136
|
170 180
....*....|....*....|....
gi 1005564688 995 AITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03216 137 FISHRlDEVFEIADRVTVLRDGRV 160
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
836-1017 |
6.47e-20 |
|
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: 89.80 E-value: 6.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELNQYY-------SAILSDFHVFD---- 901
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITglpPHEIARLGigrtfqiPRLFPELTVLEnvmv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 902 ------RLYGINTEGMKAEIDHYLELLQLSDKVGIEDGRFTTT-QLSTGQKKRLAL---LVTyledRP-ILLFDEWAADQ 970
Cdd:cd03219 99 aaqartGSGLLLARARREEREARERAEELLERVGLADLADRPAgELSYGQQRRLEIaraLAT----DPkLLLLDEPAAGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1005564688 971 DPGYRRFFyEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03219 175 NPEETEEL-AELIRELRERGITVLLVEHDmDVVMSLADRVTVLDQGRV 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
815-1022 |
7.29e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.92 E-value: 7.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 815 QNVSYKYKNKDGDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEL-------- 886
Cdd:PRK13633 8 KNVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwdirnka 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 --------NQYYSAILSDFHVF--DRLyGINTEGMKAEIDHYLEllqlsdKVGI-EDGRFTTTQLSTGQKKRLAlLVTYL 955
Cdd:PRK13633 88 gmvfqnpdNQIVATIVEEDVAFgpENL-GIPPEEIRERVDESLK------KVGMyEYRRHAPHLLSGGQKQRVA-IAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005564688 956 EDRP-ILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHDDQYFHLADKLIVMEMGTVKMNKT 1022
Cdd:PRK13633 160 AMRPeCIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
812-1026 |
1.80e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.79 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFTgfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEL----- 886
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYT---LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 ----------NQYYSAILSDfhvfDRLYGINTEG-----MKAEIDHYLELLQLSDKVGIEDGRftttqLSTGQKKRLAlL 951
Cdd:PRK13650 82 kigmvfqnpdNQFVGATVED----DVAFGLENKGipheeMKERVNEALELVGMQDFKEREPAR-----LSGGQKQRVA-I 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 952 VTYLEDRP-ILLFDEWAADQDPGYRRffyeELLPQMRA----KGKCIIAITHDDQYFHLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:PRK13650 152 AGAVAMRPkIIILDEATSMLDPEGRL----ELIKTIKGirddYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
836-1019 |
3.05e-19 |
|
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: 87.59 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNqyySAILSDFHVFD------RLYGINTE 909
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLG---GGFNPELTGREniylngRLLGLSRK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 910 GMKAEIDHYLELLQLsdkvgiedGRFTTTQL---STGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELLpQM 986
Cdd:cd03220 118 EIDEKIDEIIEFSEL--------GDFIDLPVktySSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLR-EL 188
|
170 180 190
....*....|....*....|....*....|....
gi 1005564688 987 RAKGKCIIAITHDDQYF-HLADKLIVMEMGTVKM 1019
Cdd:cd03220 189 LKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRF 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
812-1017 |
3.37e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.89 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYknkdGDFT-GFgigpiDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQYY 890
Cdd:COG3840 2 LRLDDLTYRY----GDFPlRF-----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 891 SAILSD----FH---VFDRLY-GIN-----TEGMKAEIDHYLEllqlsdKVGIED-GRFTTTQLSTGQKKRLALLVTYLE 956
Cdd:COG3840 73 VSMLFQennlFPhltVAQNIGlGLRpglklTAEQRAQVEQALE------RVGLAGlLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005564688 957 DRPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDpEDAARIADRVLLVADGRI 208
|
|
| PRK10662 |
PRK10662 |
beta-lactam binding protein AmpH; Provisional |
46-272 |
3.51e-19 |
|
beta-lactam binding protein AmpH; Provisional
Pssm-ID: 236732 [Multi-domain] Cd Length: 378 Bit Score: 90.86 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 46 QAGIPGLSVVIVKGNETIYKkNYGYANTDKKRQVTNETLFELGSTSKAFTALAVLQLEKEGKIKLSDSLTKYvSWFEM-- 123
Cdd:PRK10662 45 GSGATGMALVVIDGNQRVFR-SYGETRPGNNVRPQLDSLIRIASITKLMTSEVLVKLADDGTVKLTDPLSKY-APPGArv 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 124 -EYKGKPyeITLYDLLHHTSGIPEKAIGyipitnGKdsiEKTIRNVMPI-----------GLNREPGSSFEYSTVNYDLL 191
Cdd:PRK10662 123 pTYNGQP--ITLLNLATHTSALPREQPG------GA---AHRPVFVWPTreqrwkwlstaKLKAAPGTQAAYSNLAFDLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 192 GLVIEKATNQSFERYVQDHVLSKLDLLSTyagrEMAPldNMAQgYKRNFlqsLPYDAPNYRGNTPA----GYFISNINDM 267
Cdd:PRK10662 192 ADALAKAAGKPYTQLLREKITRPLGMKDT----TFTP--SPDQ-CARLM---VGEKGASPCNNTLAaigsGGVYSTPGDM 261
|
....*
gi 1005564688 268 ERWLK 272
Cdd:PRK10662 262 MRWMQ 266
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
785-1017 |
5.55e-19 |
|
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: 91.50 E-value: 5.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 785 QMVKSVDHIKANEQIATTKEYLDVPIcLQLQNVSYKYK-NKDGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLI 863
Cdd:COG1123 235 QALAAVPRLGAARGRAAPAAAAAEPL-LEVRNLSKRYPvRGKGGVRA--VDDVSLTLRRGETLGLVGESGSGKSTLARLL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 864 TGLYEPNEGNVLLNGKEIA---PEELNQY-----------YSAILSDFHVFD------RLYGI-NTEGMKAEIDHYLELL 922
Cdd:COG1123 312 LGLLRPTSGSILFDGKDLTklsRRSLRELrrrvqmvfqdpYSSLNPRMTVGDiiaeplRLHGLlSRAERRERVAELLERV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 923 QLSDKVGiedGRFtTTQLSTGQKKRLAL---LVTyledRP-ILLFDEWAADQDP-GYRRFFyeELLPQMRAK-GKCIIAI 996
Cdd:COG1123 392 GLPPDLA---DRY-PHELSGGQRQRVAIaraLAL----EPkLLILDEPTSALDVsVQAQIL--NLLRDLQRElGLTYLFI 461
|
250 260
....*....|....*....|..
gi 1005564688 997 THD-DQYFHLADKLIVMEMGTV 1017
Cdd:COG1123 462 SHDlAVVRYIADRVAVMYDGRI 483
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
812-1016 |
6.16e-19 |
|
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: 85.32 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKdgdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELN---- 887
Cdd:cd03229 1 LELKNVSKRYGQK------TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElppl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 888 -QYYSAILSDFHVFDRLygintegmkaeidHYLELLQLSdkvgiedgrftttqLSTGQKKRLALLVTYLEDRPILLFDEW 966
Cdd:cd03229 75 rRRIGMVFQDFALFPHL-------------TVLENIALG--------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1005564688 967 AADQDPGYRRFFyEELLPQMRAK-GKCIIAITHD-DQYFHLADKLIVMEMGT 1016
Cdd:cd03229 128 TSALDPITRREV-RALLKSLQAQlGITVVLVTHDlDEAARLADRVVVLRDGK 178
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
834-1000 |
1.21e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 85.10 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 834 GPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIaPEELNQYYSAILsdfhvfdrlYGINTEGMKA 913
Cdd:TIGR01189 17 EGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEPHENIL---------YLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 914 EI--------------DHYLELLQLSDKVGIEDgrFTTT---QLSTGQKKRLALLVTYLEDRPILLFDEWAADQDP-GYR 975
Cdd:TIGR01189 87 ELsalenlhfwaaihgGAQRTIEDALAAVGLTG--FEDLpaaQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKaGVA 164
|
170 180
....*....|....*....|....*
gi 1005564688 976 RFfyEELLPQMRAKGKCIIAITHDD 1000
Cdd:TIGR01189 165 LL--AGLLRAHLARGGIVLLTTHQD 187
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
836-1026 |
1.89e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.90 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEL------------NQYYSAilsdfhvfdRL 903
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLELgagfhpeltgreNIYLNG---------RL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 904 YGINtegmKAEIDHYLEllqlsdkvGIED----GRFTTTQL---STGQKKRLAL-LVTYLE-DrpILLFDEWAADQDPGY 974
Cdd:COG1134 116 LGLS----RKEIDEKFD--------EIVEfaelGDFIDQPVktySSGMRARLAFaVATAVDpD--ILLVDEVLAVGDAAF 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 975 RRFFYEELLpQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTVKMN-KTKEAL 1026
Cdd:COG1134 182 QKKCLARIR-ELRESGRTVIFVSHSmGAVRRLCDRAIWLEKGRLVMDgDPEEVI 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
807-1012 |
2.58e-18 |
|
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: 89.65 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 807 DVPICLQLQNVSYKYKNKDGdftgfGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEL 886
Cdd:TIGR02857 317 APASSLEFSGVSVAYPGRRP-----ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 NQYYSAIL---SDFHVFD-------RLYgiNTEGMKAEIDHYLELLQLSD-----------KVGiEDGRftttQLSTGQK 945
Cdd:TIGR02857 392 DSWRDQIAwvpQHPFLFAgtiaeniRLA--RPDASDAEIREALERAGLDEfvaalpqgldtPIG-EGGA----GLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005564688 946 KRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRakGKCIIAITHDDQYFHLADKLIVM 1012
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
812-1015 |
2.68e-18 |
|
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: 84.64 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYknkdGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA--------- 882
Cdd:cd03269 1 LEVENVTKRF----GRVTA--LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiaarnrigy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 883 -PEELNQYYS-AILSDFHVFDRLYGINTEGMKAEIDHYLELLQLSDK--VGIEdgrftttQLSTGQKKRLALLVTYLEDR 958
Cdd:cd03269 75 lPEERGLYPKmKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYanKRVE-------ELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005564688 959 PILLFDEWAADQDPGYRRFFYEELLpQMRAKGKCIIAITHD-DQYFHLADKLIVMEMG 1015
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIR-ELARAGKTVILSTHQmELVEELCDRVLLLNKG 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
812-1017 |
5.17e-18 |
|
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: 88.42 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPN---EGNVLLNGKEIA---PEE 885
Cdd:COG1123 5 LEVRDLSVRYPGGDV----PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLelsEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 886 LNQYYSAILSDF-------HVFD------RLYGINTEGMKAEIdhyLELLqlsDKVGIED-GRFTTTQLSTGQKKRLALL 951
Cdd:COG1123 81 RGRRIGMVFQDPmtqlnpvTVGDqiaealENLGLSRAEARARV---LELL---EAVGLERrLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005564688 952 VTYLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRI 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
755-999 |
5.97e-18 |
|
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: 88.57 E-value: 5.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 755 VFLYMTGPVNEILGGIP----QLVNVRISWQRIQQMVKSVDHIKANEQIATTKEYLDVPiCLQLQNVSYKYKNKDGDFTG 830
Cdd:TIGR02868 275 VLVLLPLAAFEAFAALPaaaqQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKP-TLELRDLSAGYPGAPPVLDG 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 831 fgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQYYSAIL---SDFHVFDRLYGIN 907
Cdd:TIGR02868 354 -----VSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSvcaQDAHLFDTTVREN 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 908 T-----EGMKAEIDHYLELLQLSDKV-GIEDGRFTTTQ-----LSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRr 976
Cdd:TIGR02868 429 LrlarpDATDEELWAALERVGLADWLrALPDGLDTVLGeggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETA- 507
|
250 260
....*....|....*....|....*
gi 1005564688 977 ffyEELLPQMRA--KGKCIIAITHD 999
Cdd:TIGR02868 508 ---DELLEDLLAalSGRTVVLITHH 529
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
467-1017 |
3.04e-17 |
|
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: 86.72 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 467 VVLAIYAIAGvglAYVIHTFLNLCFPrQKGKSLLTLIVLGLIsgfgnafLIFVINEtfvrsnnlenglLFYFVLGIVMYV 546
Cdd:TIGR01193 166 IIVTLISIAG---SYYLQKIIDTYIP-HKMMGTLGIISIGLI-------IAYIIQQ------------ILSYIQIFLLNV 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 547 FSQRIIRTSIVSYTNELvyekrmeltdklLQTPYYKLELIEKGRIEATLNNDTEVISRSLNLLVTAGTSLLTLLFCFLYL 626
Cdd:TIGR01193 223 LGQRLSIDIILSYIKHL------------FELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 627 GVMNMYAFLLSLCIIFITAGVYSLIGRQADKVWNETRDIQNVYFRLIGDLRHGFKELRLHTGKRNDFREVMNESCNnyRV 706
Cdd:TIGR01193 291 VRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGD--YL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 707 KRTIGDIKFANVFVLGELLFIFVIGIVVFVFPEIFVNMPKETISN---YVIVFLYMTGPVNEILGGIPQLVNVRISWQRI 783
Cdd:TIGR01193 369 NKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQlitFNALLSYFLTPLENIINLQPKLQAARVANNRL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 784 QQmVKSVDHIKANEQIATTKEYLDVPIclQLQNVSYKYknkdgdftGFG---IGPIDMEFNSGEIVFIAGGNGSGKSTLS 860
Cdd:TIGR01193 449 NE-VYLVDSEFINKKKRTELNNLNGDI--VINDVSYSY--------GYGsniLSDISLTIKMNSKTTIVGMSGSGKSTLA 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 861 KLITGLYEPNEGNVLLNGKEIAP---EELNQYYSAILSDFHVFD------RLYGINTEGMKAEIDHYLELLQLSDKVGIE 931
Cdd:TIGR01193 518 KLLVGFFQARSGEILLNGFSLKDidrHTLRQFINYLPQEPYIFSgsilenLLLGAKENVSQDEIWAACEIAEIKDDIENM 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 932 DGRFTT------TQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELLPqmrAKGKCIIAITHDDQYFHL 1005
Cdd:TIGR01193 598 PLGYQTelseegSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN---LQDKTIIFVAHRLSVAKQ 674
|
570
....*....|..
gi 1005564688 1006 ADKLIVMEMGTV 1017
Cdd:TIGR01193 675 SDKIIVLDHGKI 686
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
812-1017 |
3.53e-17 |
|
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: 81.65 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFTG-----FGIGPidmefnsGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA--PE 884
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAvdgvsFTVKP-------GEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVkePA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 885 ELNQYYSAILSDFHVFDR------------LYGINTEGMKAEIDhylellQLSDKVGIE---DGRftTTQLSTGQKKRLA 949
Cdd:cd03266 75 EARRRLGFVSDSTGLYDRltarenleyfagLYGLKGDELTARLE------ELADRLGMEellDRR--VGGFSTGMRQKVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005564688 950 LLVTYLEDRPILLFDEWAADQDPGYRRFFYeELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALR-EFIRQLRALGKCILFSTHImQEVERLCDRVVVLHRGRV 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
812-1017 |
4.17e-17 |
|
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: 79.95 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYknkdGDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGkeiapEELNQYYS 891
Cdd:cd03246 1 LEVENVSFRY----PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG-----ADISQWDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 892 AILSDfHVfdrlyginteGMKAEIDhylELLqlsdkvgieDGRFTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQD 971
Cdd:cd03246 72 NELGD-HV----------GYLPQDD---ELF---------SGSIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1005564688 972 PGYRRFFYeELLPQMRAKGKCIIAITHDDQYFHLADKLIVMEMGTV 1017
Cdd:cd03246 129 VEGERALN-QAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
812-1026 |
4.59e-17 |
|
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: 81.51 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYkNKDGDFTgfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQYYS 891
Cdd:cd03251 1 VEFKNVTFRY-PGDGPPV---LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 892 AI---LSDFHVFDR------LYGiNTEGMKAEIDHYLELLQLSDKV-GIEDGRFTT-----TQLSTGQKKRLALLVTYLE 956
Cdd:cd03251 77 QIglvSQDVFLFNDtvaeniAYG-RPGATREEVEEAARAANAHEFImELPEGYDTVigergVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 957 DRPILLFDEWAADQDPGYRRFFYEELlpQMRAKGKCIIAITHDDQYFHLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAAL--ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEEL 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
812-1017 |
4.88e-17 |
|
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: 81.62 E-value: 4.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYknkdGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELN- 887
Cdd:cd03296 3 IEVRNVSKRF----GDFVA--LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATdvpVQERNv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 888 ----QYYsAILSDFHVFD----------RLYGINTEGMKAEIDHYLELLQLSdkvGIEDgRFtTTQLSTGQKKRLALLVT 953
Cdd:cd03296 77 gfvfQHY-ALFRHMTVFDnvafglrvkpRSERPPEAEIRAKVHELLKLVQLD---WLAD-RY-PAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005564688 954 YLEDRPILLFDEWAADQDPGYR---RFFYEELLPQMrakGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRkelRRWLRRLHDEL---HVTTVFVTHDqEEALEVADRVVVMNKGRI 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
812-1024 |
5.35e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 82.37 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEL----- 886
Cdd:PRK13635 6 IRVEHISFRYPDAAT----YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwdvrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 ----------NQYYSAILSDfhvfDRLYGINTEGMkaEIDHYLELLQLS-DKVGIEDgrFTTTQ---LSTGQKKRLAlLV 952
Cdd:PRK13635 82 qvgmvfqnpdNQFVGATVQD----DVAFGLENIGV--PREEMVERVDQAlRQVGMED--FLNREphrLSGGQKQRVA-IA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005564688 953 TYLEDRP-ILLFDEWAADQDPGYRrffyEELLPQMR----AKGKCIIAITHDDQYFHLADKLIVMEMGTVKMNKTKE 1024
Cdd:PRK13635 153 GVLALQPdIIILDEATSMLDPRGR----REVLETVRqlkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
812-1017 |
6.44e-17 |
|
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: 80.61 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFtgfgigpiDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI-APEELNQYY 890
Cdd:cd03298 1 VRLDKIRFSYGEQPMHF--------DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtAAPPADRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 891 SAILSDFHVFDRL-------YGIN-----TEGMKAEIDHYLELLQLSDKvgieDGRFTTtQLSTGQKKRLALLVTYLEDR 958
Cdd:cd03298 73 SMLFQENNLFAHLtveqnvgLGLSpglklTAEDRQAIEVALARVGLAGL----EKRLPG-ELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 959 PILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQpEDAKRLAQRVVFLDNGRI 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
812-1017 |
1.18e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 82.84 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYknkdGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELN- 887
Cdd:COG3842 6 LELENVSKRY----GDVTA--LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglpPEKRNv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 888 ----QYYsAIlsdF-H--VFDRL-YGINTEGM-KAEI----DHYLELLQLSDKvgieDGRFtTTQLSTGQKKRLAL---L 951
Cdd:COG3842 80 gmvfQDY-AL---FpHltVAENVaFGLRMRGVpKAEIrarvAELLELVGLEGL----ADRY-PHQLSGGQQQRVALaraL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005564688 952 VTyledRP-ILLFDEwaadqDPGYRRFFYEELLPQMRAKGKCIIAITHdDQY--FHLADKLIVMEMGTV 1017
Cdd:COG3842 151 AP----EPrVLLLDEplsalDAKLREEMREELRRLQRELGITFIYVTH-DQEeaLALADRIAVMNDGRI 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
836-1000 |
1.93e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.08 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA--PEELNQyysailsdfhvfDRLY-----GINT 908
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqRDEYHQ------------DLLYlghqpGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 909 EgMKAE--IDHYLELLQLSD---------KVGI---EDgrFTTTQLSTGQKKRLALLVTYLEDRPILLFDE--WAADQDp 972
Cdd:PRK13538 88 E-LTALenLRFYQRLHGPGDdealwealaQVGLagfED--VPVRQLSAGQQRRVALARLWLTRAPLWILDEpfTAIDKQ- 163
|
170 180
....*....|....*....|....*...
gi 1005564688 973 GYRRFfyEELLPQMRAKGKCIIAITHDD 1000
Cdd:PRK13538 164 GVARL--EALLAQHAEQGGMVILTTHQD 189
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
812-1017 |
2.64e-16 |
|
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: 79.20 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYknkdGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELN---- 887
Cdd:cd03300 1 IELENVSKFY----GGFVA--LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHkrpv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 888 ----QYYsAILSDFHVFD------RLYGINTEGMKAEIDHYLELLQLSdkvGIEDGRftTTQLSTGQKKRLALLVTYLED 957
Cdd:cd03300 75 ntvfQNY-ALFPHLTVFEniafglRLKKLPKAEIKERVAEALDLVQLE---GYANRK--PSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005564688 958 RPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDqEEALTMSDRIAVMNKGKI 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
809-1015 |
3.57e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.03 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 809 PICLQLQNVSYKYKNKdgdftgfgigPI--DMEFN--SGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI-AP 883
Cdd:PRK13536 39 TVAIDLAGVSKSYGDK----------AVvnGLSFTvaSGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 884 EELNQYYSAILSDFH-------------VFDRLYGINTEGMKAEIDHYLELLQLSDKVgieDGRftTTQLSTGQKKRLAL 950
Cdd:PRK13536 109 ARLARARIGVVPQFDnldleftvrenllVFGRYFGMSTREIEAVIPSLLEFARLESKA---DAR--VSDLSGGMKRRLTL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005564688 951 LVTYLEDRPILLFDEWAADQDPGYRRFFYEElLPQMRAKGKCIIAITH-DDQYFHLADKLIVMEMG 1015
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWER-LRSLLARGKTILLTTHfMEEAERLCDRLCVLEAG 248
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
812-1026 |
6.69e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 6.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFTGfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEiapeelnqyyS 891
Cdd:PRK13644 2 IRLENVSYSYPDGTPALEN-----INLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID----------T 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 892 AILSDFHVFDRLYGI---NTE----GMKAEIDHY----------LELLQLSDK----VGIEDGRFTTTQ-LSTGQKKRLA 949
Cdd:PRK13644 67 GDFSKLQGIRKLVGIvfqNPEtqfvGRTVEEDLAfgpenlclppIEIRKRVDRalaeIGLEKYRHRSPKtLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005564688 950 LLVTYLEDRPILLFDEWAADQDPGYRRFFYEElLPQMRAKGKCIIAITHDDQYFHLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLER-IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
809-1017 |
7.48e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 76.82 E-value: 7.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 809 PICLQLQNVSYKYKNKDGDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGL--YEPNEGNVLLNGKEIAPEEL 886
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 NQYYSAILSDFHVFDRLYGINTEGMKAEIdhylellqlsdkvgiedgrfttTQLSTGQKKRLALLVTYLEDRPILLFDEW 966
Cdd:cd03213 81 RKIIGYVPQDDILHPTLTVRETLMFAAKL----------------------RGLSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1005564688 967 AADQDPGyRRFFYEELLPQMRAKGKCIIAITHDDQY--FHLADKLIVMEMGTV 1017
Cdd:cd03213 139 TSGLDSS-SALQVMSLLRRLADTGRTIICSIHQPSSeiFELFDKLLLLSQGRV 190
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
812-1017 |
9.11e-16 |
|
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: 77.92 E-value: 9.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFT---GfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQ 888
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPvlkD-----VSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 YYSAI-------LSDFHVFDRLYGINTEGMKA--EIDHYLELLQLSDKVGIEDG---RFtTTQLSTGQKKRLAL---LVT 953
Cdd:COG1124 77 FRRRVqmvfqdpYASLHPRHTVDRILAEPLRIhgLPDREERIAELLEQVGLPPSfldRY-PHQLSGGQRQRVAIaraLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005564688 954 yledRP-ILLFDEWAADQDPGYRRffyE--ELLPQMRAK-GKCIIAITHDDQY-FHLADKLIVMEMGTV 1017
Cdd:COG1124 156 ----EPeLLLLDEPTSALDVSVQA---EilNLLKDLREErGLTYLFVSHDLAVvAHLCDRVAVMQNGRI 217
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
812-1017 |
9.28e-16 |
|
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: 77.76 E-value: 9.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNkdgdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELN- 887
Cdd:cd03299 1 LKVENLSKDWKE-------FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITnlpPEKRDi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 888 ----QYYsAILSDFHVFDRL-YGI-NTEGMKAEIDHylELLQLSDKVGIED--GRFTTTqLSTGQKKRLALLVTYLEDRP 959
Cdd:cd03299 74 syvpQNY-ALFPHMTVYKNIaYGLkKRKVDKKEIER--KVLEIAEMLGIDHllNRKPET-LSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1005564688 960 ILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKL 208
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
812-1017 |
1.23e-15 |
|
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: 77.53 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKnKDGDFTgfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELNQ 888
Cdd:cd03252 1 ITFEHVRFRYK-PDGPVI---LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAladPAWLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 YYSAILSDFHVFDRLYGINT----EGMKAEI-----------DHYLELLQLSDKVGIEDGrfttTQLSTGQKKRLALLVT 953
Cdd:cd03252 77 QVGVVLQENVLFNRSIRDNIaladPGMSMERvieaaklagahDFISELPEGYDTIVGEQG----AGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005564688 954 YLEDRPILLFDEWAADQDpgyrrffYEE---LLPQMRA--KGKCIIAITHDDQYFHLADKLIVMEMGTV 1017
Cdd:cd03252 153 LIHNPRILIFDEATSALD-------YESehaIMRNMHDicAGRTVIIIAHRLSTVKNADRIIVMEKGRI 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
836-1017 |
2.37e-15 |
|
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: 77.00 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI---APEELNQ------------------------ 888
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHRIARlgiartfqnprlfpeltvlenvlv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 ---------YYSAILSDFHVFDRLygintEGMKAEIDHYLELLQLSDKVGIEdgrftTTQLSTGQKKRLAL---LVTyle 956
Cdd:COG0411 103 aaharlgrgLLAALLRLPRARREE-----REARERAEELLERVGLADRADEP-----AGNLSYGQQRRLEIaraLAT--- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005564688 957 dRP-ILLFDEWAADQDPGyrrffyE-----ELLPQMRAK-GKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:COG0411 170 -EPkLLLLDEPAAGLNPE------EteelaELIRRLRDErGITILLIEHDmDLVMGLADRIVVLDFGRV 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
836-1000 |
3.17e-15 |
|
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: 75.22 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIApEELNQYYSAIlsdfhvfdrLYGINTEGMKAEI 915
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-FQRDSIARGL---------LYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 916 ---------------DHYLELLQLSDKVGIEDGRFttTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQD-PGYRRFfy 979
Cdd:cd03231 89 svlenlrfwhadhsdEQVEEALARVGLNGFEDRPV--AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkAGVARF-- 164
|
170 180
....*....|....*....|.
gi 1005564688 980 EELLPQMRAKGKCIIAITHDD 1000
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTHQD 185
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
814-1017 |
3.70e-15 |
|
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: 76.08 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 814 LQNVSYKYKNKDGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI---APEELNQYY 890
Cdd:cd03258 4 LKNVSKVFGDTGGKVTA--LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 891 SAI---------LSDFHVFD------RLYGINTEGMKAEIDHYLELLQLSDKvgiedGRFTTTQLSTGQKKRLAL---LV 952
Cdd:cd03258 82 RRIgmifqhfnlLSSRTVFEnvalplEIAGVPKAEIEERVLELLELVGLEDK-----ADAYPAQLSGGQKQRVGIaraLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005564688 953 TyleDRPILLFDEWAADQDPgyrrffyE------ELLPQMRAK-GKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03258 157 N---NPKVLLCDEATSALDP-------EttqsilALLRDINRElGLTIVLITHEmEVVKRICDRVAVMEKGEV 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
812-1017 |
3.80e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNK---DGdftgfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEE 885
Cdd:PRK13548 3 LEARNLSVRLGGRtllDD---------VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwsPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 886 LNQY------YSAILSDFHVFD--RL----YGINTEGMKAEIDHYLELlqlsdkVGIED--GRFtTTQLSTGQKKR---- 947
Cdd:PRK13548 74 LARRravlpqHSSLSFPFTVEEvvAMgrapHGLSRAEDDALVAAALAQ------VDLAHlaGRD-YPQLSGGEQQRvqla 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 948 --LALLVTYLEDRPILLFDEWAADQDPGY--------RRFfyeellpqMRAKGKCIIAITHD----DQYfhlADKLIVME 1013
Cdd:PRK13548 147 rvLAQLWEPDGPPRWLLLDEPTSALDLAHqhhvlrlaRQL--------AHERGLAVIVVLHDlnlaARY---ADRIVLLH 215
|
....
gi 1005564688 1014 MGTV 1017
Cdd:PRK13548 216 QGRL 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
812-1017 |
3.95e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 75.47 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKN-----KDgdftgfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---P 883
Cdd:COG2884 2 IRFENVSKRYPGgrealSD----------VSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 884 EELN----------QYYSaILSDFHVFD------RLYGINTEGMKAEIDHYLELLQLSDKvgiedGRFTTTQLSTGQKKR 947
Cdd:COG2884 72 REIPylrrrigvvfQDFR-LLPDRTVYEnvalplRVTGKSRKEIRRRVREVLDLVGLSDK-----AKALPHELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005564688 948 LAL---LVTyledRP-ILLFDEWAADQDPGY-RRFFyeELLPQMRAKGKCIIAITHDDqyfHLADKL----IVMEMGTV 1017
Cdd:COG2884 146 VAIaraLVN----RPeLLLADEPTGNLDPETsWEIM--ELLEEINRRGTTVLIATHDL---ELVDRMpkrvLELEDGRL 215
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
812-1017 |
4.18e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 77.88 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYknkdGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKE----IAPEELN 887
Cdd:COG1118 3 IEVRNISKRF----GSFTL--LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlftnLPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 888 -----QYYSAilsdF-H--VFD------RLYGINTEGMKAEIDHYLELLQLSdkvGIEDgRFtTTQLSTGQKKRLAL--- 950
Cdd:COG1118 77 vgfvfQHYAL----FpHmtVAEniafglRVRPPSKAEIRARVEELLELVQLE---GLAD-RY-PSQLSGGQRQRVALara 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 951 LVTyledRP-ILLFDEwaadqdP-G----YRRffyeellPQMRA---------KGKCIIaITHD-DQYFHLADKLIVMEM 1014
Cdd:COG1118 148 LAV----EPeVLLLDE------PfGaldaKVR-------KELRRwlrrlhdelGGTTVF-VTHDqEEALELADRVVVMNQ 209
|
...
gi 1005564688 1015 GTV 1017
Cdd:COG1118 210 GRI 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
812-1024 |
4.68e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 4.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYkNKDGDFTgfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEL----- 886
Cdd:PRK13648 8 IVFKNVSFQY-QSDASFT---LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFeklrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 ----------NQYYSAILSdfhvFDRLYGIN-----TEGMKAEIDHYLELLQLSDKVGIEdgrftTTQLSTGQKKRLALL 951
Cdd:PRK13648 84 higivfqnpdNQFVGSIVK----YDVAFGLEnhavpYDEMHRRVSEALKQVDMLERADYE-----PNALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 952 VTYLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHDDQYFHLADKLIVMEMGTV-KMNKTKE 1024
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVyKEGTPTE 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
813-1017 |
6.46e-15 |
|
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: 75.34 E-value: 6.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 813 QLQNVSYKYKNKDGDFTGfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNG---KEIAPEELNQY 889
Cdd:cd03254 4 EFENVNFSYDEKKPVLKD-----INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 890 YSAILSDFHVFDR------LYGINTEGMKaEIDHYLELLQLSDKV-GIEDGRFTT-----TQLSTGQKKRLALLVTYLED 957
Cdd:cd03254 79 IGVVLQDTFLFSGtimeniRLGRPNATDE-EVIEAAKEAGAHDFImKLPNGYDTVlgengGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005564688 958 RPILLFDEWAADQDPGYRRFFYEELLPQMraKGKCIIAITHddqyfHL-----ADKLIVMEMGTV 1017
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAH-----RLstiknADKILVLDDGKI 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
812-1026 |
1.11e-14 |
|
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: 74.91 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFTGfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELNQ 888
Cdd:cd03256 1 IEVENLSKTYPNGKKALKD-----VSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 YYS---AILSDFHVFDRLYGI---------------NTEGM--KAEIDHYLELLqlsDKVGIEDGRFT-TTQLSTGQKKR 947
Cdd:cd03256 76 LRRqigMIFQQFNLIERLSVLenvlsgrlgrrstwrSLFGLfpKEEKQRALAAL---ERVGLLDKAYQrADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 948 LALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHDDQYF-HLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
812-1017 |
1.42e-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: 73.83 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKdgdftgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELN- 887
Cdd:cd03301 1 VELENVTKRFGNV------TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTdlpPKDRDi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 888 ----QYYsAILSDFHVFDRL-YGINTEGM-KAEID-------HYLELLQLSDKvgiedgrfTTTQLSTGQKKRLALLVTY 954
Cdd:cd03301 75 amvfQNY-ALYPHMTVYDNIaFGLKLRKVpKDEIDervrevaELLQIEHLLDR--------KPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 955 LEDRPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqVEAMTMADRIAVMNDGQI 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
841-1000 |
1.71e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.37 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 841 NSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIapeELNQYYSAI------------LS-----DFhvFDRL 903
Cdd:PRK13539 26 AAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEAChylghrnamkpaLTvaenlEF--WAAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 904 YGiNTEGMkaeIDHYLELLQLSDkvgIEDGRFTTtqLSTGQKKRLA---LLVTYledRPILLFDEWAADQDPGYRRFFyE 980
Cdd:PRK13539 101 LG-GEELD---IAAALEAVGLAP---LAHLPFGY--LSAGQKRRVAlarLLVSN---RPIWILDEPTAALDAAAVALF-A 167
|
170 180
....*....|....*....|
gi 1005564688 981 ELLPQMRAKGKCIIAITHDD 1000
Cdd:PRK13539 168 ELIRAHLAQGGIVIAATHIP 187
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
426-1024 |
4.12e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 76.68 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 426 WLHMVL-VVAIYGLMIYALYQLPNLLFGGLP----------WAFIkVW-----APSTVVLAIYAIAGV----------GL 479
Cdd:TIGR00958 67 LLAAVKpLVAALCLATPSLSSLRALAFWEALdpavrvalglWSWF-VWsygaaLPAAALWAVLSSAGAsekeaeqgqsET 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 480 AYVIHTFLNLCfpRQKGKSLLTLIVLGLISGFGNAFLIFVINE---TFVRSNN---LENGLLFYFVLGIVMYVFSQriIR 553
Cdd:TIGR00958 146 ADLLFRLLGLS--GRDWPWLISAFVFLTLSSLGEMFIPFYTGRvidTLGGDKGppaLASAIFFMCLLSIASSVSAG--LR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 554 TSIVSYTNELVYEK-RMELTDKLLQTPYYKLELIEKGRIEATLNNDTEVISRSL----NLLVTAGTSLLTLLFCFLYLGV 628
Cdd:TIGR00958 222 GGSFNYTMARINLRiREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLslnvNVLLRNLVMLLGLLGFMLWLSP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 629 MNMYAFLLSLCIIFITAGVYsliGRQADKVWNETRDiqnvyfrligdlrhgfkelrlHTGKRND--------FREVMNES 700
Cdd:TIGR00958 302 RLTMVTLINLPLVFLAEKVF---GKRYQLLSEELQE---------------------AVAKANQvaeealsgMRTVRSFA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 701 CNNYRVKR---------TIG---DIKFANVFVLGELLFIFVIGIVVFVFPEIfVNMPKETISNYVIVFLYmtgpvNEILG 768
Cdd:TIGR00958 358 AEEGEASRfkealeetlQLNkrkALAYAGYLWTTSVLGMLIQVLVLYYGGQL-VLTGKVSSGNLVSFLLY-----QEQLG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 769 -GIPQLVNVrisWQRIQQMVKsvdhikANEQIAttkEYLDVPICLQL---------------QNVSYKYKN-------KD 825
Cdd:TIGR00958 432 eAVRVLSYV---YSGMMQAVG------ASEKVF---EYLDRKPNIPLtgtlaplnlegliefQDVSFSYPNrpdvpvlKG 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 826 GDFTgfgigpidmeFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIapEELNQYY-----SAILSDFHVF 900
Cdd:TIGR00958 500 LTFT----------LHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL--VQYDHHYlhrqvALVGQEPVLF 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 901 DR------LYGINTEGMkAEI----------DHYLELLQLSDKVGIEDGrfttTQLSTGQKKRLALLVTYLEDRPILLFD 964
Cdd:TIGR00958 568 SGsvreniAYGLTDTPD-EEImaaakaanahDFIMEFPNGYDTEVGEKG----SQLSGGQKQRIAIARALVRKPRVLILD 642
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005564688 965 EWAADQDPGYRRFFYEEllpqMRAKGKCIIAITHDDQYFHLADKLIVMEMGT-VKMNKTKE 1024
Cdd:TIGR00958 643 EATSALDAECEQLLQES----RSRASRTVLLIAHRLSTVERADQILVLKKGSvVEMGTHKQ 699
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
836-1017 |
4.24e-14 |
|
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: 72.56 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPE-----ELNQYYSAILSDFHVFDRLYGIN--T 908
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDkkninELRQKVGMVFQQFNLFPHLTVLEniT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 909 EGM-------KAE-IDHYLELLqlsDKVGIEDgRFTT--TQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRff 978
Cdd:cd03262 99 LAPikvkgmsKAEaEERALELL---EKVGLAD-KADAypAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVG-- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1005564688 979 yeELLPQMRA---KGKCIIAITHDDQY-FHLADKLIVMEMGTV 1017
Cdd:cd03262 173 --EVLDVMKDlaeEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
812-1017 |
1.28e-13 |
|
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: 71.49 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKN-----KDGDFTgfgIGPidmefnsGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEL 886
Cdd:cd03253 1 IEFENVTFAYDPgrpvlKDVSFT---IPA-------GKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 NQYYSAI---------LSDFHVFDRLYG--------INTEGMKAEIDHylELLQLSD----KVGiEDGrfttTQLSTGQK 945
Cdd:cd03253 71 DSLRRAIgvvpqdtvlFNDTIGYNIRYGrpdatdeeVIEAAKAAQIHD--KIMRFPDgydtIVG-ERG----LKLSGGEK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 946 KRLALLVTYLEDRPILLFDEWAADQDPGYRRffyeELLPQMR--AKGKCIIAITHDDQYFHLADKLIVMEMGTV 1017
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTER----EIQAALRdvSKGRTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
833-972 |
1.34e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.03 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 833 IGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQYYS------------AILSDFHVF 900
Cdd:PRK13543 27 FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAylghlpglkadlSTLENLHFL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005564688 901 DRLYGINTEGMKAEIdhyLELLQLSdkvGIEDGrfTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDP 972
Cdd:PRK13543 107 CGLHGRRAKQMPGSA---LAIVGLA---GYEDT--LVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
812-1017 |
1.39e-13 |
|
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: 71.06 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGdftgfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYE-----PNEGNVLLNGKEI----- 881
Cdd:cd03260 1 IELRDLNVYYGDKHA------LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydldv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 882 APEELNQ-----YYSAILSDFHVFD------RLYGI-NTEGMKAEIDHYLELLQLSDKVgieDGRFTTTQLSTGQKKRLA 949
Cdd:cd03260 75 DVLELRRrvgmvFQKPNPFPGSIYDnvayglRLHGIkLKEELDERVEEALRKAALWDEV---KDRLHALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 950 LLVTyLEDRP-ILLFDEWAADQDPGYRRFFyEELLPQMRAKgKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03260 152 LARA-LANEPeVLLLDEPTSALDPISTAKI-EELIAELKKE-YTIVIVTHNmQQAARVADRTAFLLNGRL 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
812-965 |
1.49e-13 |
|
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: 70.71 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGdftgfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA-PEELNQYY 890
Cdd:cd03268 1 LKTNDLTKTYGKKRV------LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQkNIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 891 SAIL------------SDFHVFDRLYGINtegmKAEIDHYLELLQLSDkvgieDGRFTTTQLSTGQKKRLALLVTYLEDR 958
Cdd:cd03268 75 GALIeapgfypnltarENLRLLARLLGIR----KKRIDEVLDVVGLKD-----SAKKKVKGFSLGMKQRLGIALALLGNP 145
|
....*..
gi 1005564688 959 PILLFDE 965
Cdd:cd03268 146 DLLILDE 152
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
812-1022 |
1.81e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.00 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYkNKDGDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELN---- 887
Cdd:PRK13637 3 IKIENLTHIY-MEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 888 --------QY------YSAILSDFHVFDRLYGINTEGMKAEIDHYLELLQLSDKVGIEDGRFtttQLSTGQKKRLALLVT 953
Cdd:PRK13637 82 rkkvglvfQYpeyqlfEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPF---ELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 954 YLEDRPILLFDEWAADQDPGYRrffyEELLPQMRA----KGKCIIAITHD-DQYFHLADKLIVMEMGTVKMNKT 1022
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGR----DEILNKIKElhkeYNMTIILVSHSmEDVAKLADRIIVMNKGKCELQGT 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
836-1017 |
1.89e-13 |
|
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: 70.51 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQ--YY----------SAILSDFHVFD-- 901
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipYLrrkigvvfqdFRLLPDRNVYEnv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 902 ----RLYGINTEGMKAEIDHYLELLQLSDKVgiedgRFTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRF 977
Cdd:cd03292 100 afalEVTGVPPREIRKRVPAALELVGLSHKH-----RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1005564688 978 FYeELLPQMRAKGKCIIAITHDDQYFH-LADKLIVMEMGTV 1017
Cdd:cd03292 175 IM-NLLKKINKAGTTVVVATHAKELVDtTRHRVIALERGKL 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
835-1017 |
1.92e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 69.77 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 835 PIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELNQYYSAILSDfhvfDRLyginTEGM 911
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrsPRDAIRAGIAYVPE----DRK----REGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 912 kaeidhyleLLQLSdkvgIEDGRFTTTQLSTG--QKkrlALLVTYLEDRP-ILLFDEWAADQDPGYRRFFYEELLpQMRA 988
Cdd:cd03215 90 ---------VLDLS----VAENIALSSLLSGGnqQK---VVLARWLARDPrVLILDEPTRGVDVGAKAEIYRLIR-ELAD 152
|
170 180 190
....*....|....*....|....*....|
gi 1005564688 989 KGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03215 153 AGKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
836-1017 |
2.71e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.51 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLL-----NGKEIAPEELNQYYSAILSDFHVFDRL------- 903
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdglkvNDPKVDERLIRQEAGMVFQQFYLFPHLtalenvm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 904 YG-INTEGMKAEIDHYL--ELLqlsDKVGIED-GRFTTTQLSTGQKKRLAlLVTYLEDRP-ILLFDEWAADQDPGYRrff 978
Cdd:PRK09493 100 FGpLRVRGASKEEAEKQarELL---AKVGLAErAHHYPSELSGGQQQRVA-IARALAVKPkLMLFDEPTSALDPELR--- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1005564688 979 yEELLPQMRA---KGKCIIAITHDDQYFH-LADKLIVMEMGTV 1017
Cdd:PRK09493 173 -HEVLKVMQDlaeEGMTMVIVTHEIGFAEkVASRLIFIDKGRI 214
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
834-999 |
2.99e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.64 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 834 GPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYePNEGNVLLNGKEIA---PEEL---------NQYYSAILSDFHVFD 901
Cdd:COG4138 13 GPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSdwsAAELarhraylsqQQSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 902 rLY---GINTEGMKAEIDHYLELLQLSDKVgiedGRfTTTQLSTG--QKKRLA--LLVTYLEDRP---ILLFDEWAADQD 971
Cdd:COG4138 92 -LHqpaGASSEAVEQLLAQLAEALGLEDKL----SR-PLTQLSGGewQRVRLAavLLQVWPTINPegqLLLLDEPMNSLD 165
|
170 180
....*....|....*....|....*...
gi 1005564688 972 PGYRRFFYeELLPQMRAKGKCIIAITHD 999
Cdd:COG4138 166 VAQQAALD-RLLRELCQQGITVVMSSHD 192
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
812-1027 |
3.07e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.40 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYkNKDGDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQ--- 888
Cdd:PRK13641 3 IKFENVDYIY-SPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 -----------------YYSAILSDFHVFDRLYGINTEGMKAEIDHYLELLQLSDKVgIEDGRFtttQLSTGQKKRLALL 951
Cdd:PRK13641 82 klrkkvslvfqfpeaqlFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDL-ISKSPF---ELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005564688 952 VTYLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRAkGKCIIAITHD-DQYFHLADKLIVMEMGT-VKMNKTKEALS 1027
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNmDDVAEYADDVLVLEHGKlIKHASPKEIFS 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
812-1017 |
3.80e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.89 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKnKDGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEL----- 886
Cdd:PRK13642 5 LEVENLVFKYE-KESDVNQ--LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwnlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 ----------NQYYSAILSDfhvfDRLYGINTEGMKAE-----IDHYLELLQLSDKVGIEDGRftttqLSTGQKKRLAlL 951
Cdd:PRK13642 82 kigmvfqnpdNQFVGATVED----DVAFGMENQGIPREemikrVDEALLAVNMLDFKTREPAR-----LSGGQKQRVA-V 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005564688 952 VTYLEDRP-ILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHDDQYFHLADKLIVMEMGTV 1017
Cdd:PRK13642 152 AGIIALRPeIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
812-1016 |
5.24e-13 |
|
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: 69.04 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFTgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKeIA-----P--- 883
Cdd:cd03250 1 ISVEDASFTWDSGEQETS-FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IAyvsqePwiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 884 -----------EELN-QYYSAILS------DFHVFDRlyGINTEgmkaeidhylellqlsdkVGiEDGrfttTQLSTGQK 945
Cdd:cd03250 79 ngtirenilfgKPFDeERYEKVIKacalepDLEILPD--GDLTE------------------IG-EKG----INLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005564688 946 KRLALLVTYLEDRPILLFDE--WAADQDPGyrRFFYEELLPQMRAKGKCIIAITHDDQYFHLADKLIVMEMGT 1016
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDplSAVDAHVG--RHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
831-1021 |
5.82e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 71.29 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 831 FG----IGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQ------YYS-AILSDFHV 899
Cdd:PRK11432 16 FGsntvIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQrdicmvFQSyALFPHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 900 FDRL-YGINTEGM-KAEIDHYL-ELLQLSDKVGIEDgRFTTtQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRR 976
Cdd:PRK11432 96 GENVgYGLKMLGVpKEERKQRVkEALELVDLAGFED-RYVD-QISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1005564688 977 FFYE---ELLPQMrakGKCIIAITHDD-QYFHLADKLIVMEMGTVkMNK 1021
Cdd:PRK11432 174 SMREkirELQQQF---NITSLYVTHDQsEAFAVSDTVIVMNKGKI-MQI 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
812-1017 |
1.13e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 68.96 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNK---DGdftgfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVL-LNGKEIAPE--- 884
Cdd:COG1119 4 LELRNVTVRRGGKtilDD---------ISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRGGEdvw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 885 -----------ELNQYYS-------AILSDFhvFD--RLYGINTEGMKAEIDHYLELLQLSDKvgiEDGRFTTtqLSTGQ 944
Cdd:COG1119 75 elrkriglvspALQLRFPrdetvldVVLSGF--FDsiGLYREPTDEQRERARELLELLGLAHL---ADRPFGT--LSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 945 KKRLAL---LVTyleDRPILLFDEWAADQDPGYRRFFyEELLPQMRAKGKC-IIAITHddqyfHLAD------KLIVMEM 1014
Cdd:COG1119 148 QRRVLIaraLVK---DPELLILDEPTAGLDLGARELL-LALLDKLAAEGAPtLVLVTH-----HVEEippgitHVLLLKD 218
|
...
gi 1005564688 1015 GTV 1017
Cdd:COG1119 219 GRV 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
836-1017 |
1.19e-12 |
|
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: 68.51 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGkEIAPEELNQYYSAI----------------LSDFHV 899
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIgvvfgqktqlwwdlpvIDSFYL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 900 FDRLYGINTEGMKAEIDHYLELLQLSDKVGIEdgrftTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFY 979
Cdd:cd03267 119 LAAIYDLPPARFKKRLDELSELLDLEELLDTP-----VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193
|
170 180 190
....*....|....*....|....*....|....*....
gi 1005564688 980 EELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03267 194 NFLKEYNRERGTTVLLTSHYmKDIEALARRVLVIDKGRL 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
827-1017 |
1.37e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.83 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 827 DFTGFGIGPID--MEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAP---EELNQYYS---------- 891
Cdd:PRK10070 36 EKTGLSLGVKDasLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdAELREVRRkkiamvfqsf 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 892 AILSDFHVFDRL-YGINTEGMKAEiDHYLELLQLSDKVGIED-GRFTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAAD 969
Cdd:PRK10070 116 ALMPHMTVLDNTaFGMELAGINAE-ERREKALDALRQVGLENyAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1005564688 970 QDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEV 243
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
813-1017 |
1.38e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.21 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 813 QLQNVSYKYKNKDGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELNQY 889
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHA--LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalsEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 890 YSAI---------LSDFHVFD------RLYGINtegmKAEID-HYLELLQLsdkVGIEDGR-FTTTQLSTGQKKRLAL-- 950
Cdd:PRK11153 81 RRQIgmifqhfnlLSSRTVFDnvalplELAGTP----KAEIKaRVTELLEL---VGLSDKAdRYPAQLSGGQKQRVAIar 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005564688 951 -LVTyledRP-ILLFDEWAADQDPGYRRFFYeELLPQM-RAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:PRK11153 154 aLAS----NPkVLLCDEATSALDPATTRSIL-ELLKDInRELGLTIVLITHEmDVVKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
812-1027 |
1.48e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.99 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFTGfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEL----- 886
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKG-----LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkwvrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 ----------NQYYSAILSDfhvfDRLYG-INTEGMKAEIDHYLEllQLSDKVGIEDGRFTTT-QLSTGQKKRLALLVTY 954
Cdd:PRK13647 80 kvglvfqdpdDQVFSSTVWD----DVAFGpVNMGLDKDEVERRVE--EALKAVRMWDFRDKPPyHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 955 LEDRPILLFDEWAADQDPGYRRFFYeELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTVKMNKTKEALS 1027
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLM-EILDRLHNQGKTVIVATHDvDLAAEWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
812-1017 |
1.76e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.11 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFTGfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI---------- 881
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKG-----ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrkglmkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 882 ---------APEelNQYYSA-ILSDFHVFDRLYGINTEGMKAEIDHYLEllqlsdKVGIEDGRFTTTQ-LSTGQKKRLAL 950
Cdd:PRK13636 81 resvgmvfqDPD--NQLFSAsVYQDVSFGAVNLKLPEDEVRKRVDNALK------RTGIEHLKDKPTHcLSFGQKKRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005564688 951 LVTYLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHDDQYFHL-ADKLIVMEMGTV 1017
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLyCDNVFVMKEGRV 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
812-999 |
2.20e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 68.98 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNK---DGdftgfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA------ 882
Cdd:COG4152 2 LELKGLTKRFGDKtavDD---------VSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDpedrrr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 883 ----PEE---------LNQ-YYsailsdfhvFDRLYGINTEGMKAEIDHYLELLQLSDKVG--IEDgrftttqLSTGQKK 946
Cdd:COG4152 73 igylPEErglypkmkvGEQlVY---------LARLKGLSKAEAKRRADEWLERLGLGDRANkkVEE-------LSKGNQQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1005564688 947 RLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELLpQMRAKGKCIIAITHD 999
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIR-ELAAKGTTVIFSSHQ 188
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
814-1017 |
2.32e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.88 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 814 LQNVSYKYKNKDgDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPE--------- 884
Cdd:PRK13645 9 LDNVSYTYAKKT-PFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkkikevkr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 885 ------------ELNQYYSAILSDFHVFDRLYGINTEGMKAEIDHYLELLQLSDkvgiEDGRFTTTQLSTGQKKRLALLV 952
Cdd:PRK13645 88 lrkeiglvfqfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPE----DYVKRSPFELSGGQKRRVALAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005564688 953 TYLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
814-1026 |
2.44e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.89 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 814 LQNVSYKYkNKDGDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQ----- 888
Cdd:PRK13634 5 FQKVEHRY-QYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkpl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 ---------------YYSAILSDFHVFDRLYGINTEGMKAEIDHYLELLQLSDKVgIEDGRFtttQLSTGQKKRLALLVT 953
Cdd:PRK13634 84 rkkvgivfqfpehqlFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEEL-LARSPF---ELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 954 YLEDRPILLFDEWAADQDPGYRR----FFYEellpQMRAKGKCIIAITH--DD--QYfhlADKLIVMEMGTVKMNKTKEA 1025
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKemmeMFYK----LHKEKGLTTVLVTHsmEDaaRY---ADQIVVMHKGTVFLQGTPRE 232
|
.
gi 1005564688 1026 L 1026
Cdd:PRK13634 233 I 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
812-975 |
2.47e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.68 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFtgfgigpiDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKE---IAPEElnQ 888
Cdd:PRK10771 2 LKLTDITWLYHHLPMRF--------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhttTPPSR--R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 YYSAILSDFHVFDRL-------YGINTeGMKAEIDHYLELLQLSDKVGIED--GRFtTTQLSTGQKKRLALLVTYLEDRP 959
Cdd:PRK10771 72 PVSMLFQENNLFSHLtvaqnigLGLNP-GLKLNAAQREKLHAIARQMGIEDllARL-PGQLSGGQRQRVALARCLVREQP 149
|
170
....*....|....*.
gi 1005564688 960 ILLFDEWAADQDPGYR 975
Cdd:PRK10771 150 ILLLDEPFSALDPALR 165
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
812-1017 |
2.77e-12 |
|
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: 67.53 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAP--EELNQY 889
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKA--LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 890 Y----SAILSD-FHVFD---RLYGINTEGMKAEIDHY------LELLQLSDKVGIEDGRFTT--TQLSTGQKKRLAL--- 950
Cdd:cd03257 80 RrkeiQMVFQDpMSSLNprmTIGEQIAEPLRIHGKLSkkearkEAVLLLLVGVGLPEEVLNRypHELSGGQRQRVAIara 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005564688 951 LVTyledRP-ILLFDEWAADQDPGYRRFFyEELLPQMRAK-GKCIIAITHDdqyF----HLADKLIVMEMGTV 1017
Cdd:cd03257 160 LAL----NPkLLIADEPTSALDVSVQAQI-LDLLKKLQEElGLTLLFITHD---LgvvaKIADRVAVMYAGKI 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
812-1017 |
3.20e-12 |
|
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: 67.11 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDG-----DFTgfgigpidMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEl 886
Cdd:cd03248 12 VKFQNVTFAYPTRPDtlvlqDVS--------FTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 NQYY----SAILSDFHVFDR------LYGINTEGM--------KAEIDHYLELLQL--SDKVGiEDGrfttTQLSTGQKK 946
Cdd:cd03248 83 HKYLhskvSLVGQEPVLFARslqdniAYGLQSCSFecvkeaaqKAHAHSFISELASgyDTEVG-EKG----SQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005564688 947 RLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELL--PQMRAkgkcIIAITHDDQYFHLADKLIVMEMGTV 1017
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYdwPERRT----VLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
836-1017 |
3.55e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.29 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGK---EIAPEELN-----QYYsAILSDFHVFDRL-YGI 906
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAERGvgmvfQSY-ALYPHLSVAENMsFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 907 NTEGM-KAEID----HYLELLQLSDkvgIEDGRftTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRrffyee 981
Cdd:PRK11000 101 KLAGAkKEEINqrvnQVAEVLQLAH---LLDRK--PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR------ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1005564688 982 llPQMRAK--------GKCIIAITHDD-QYFHLADKLIVMEMGTV 1017
Cdd:PRK11000 170 --VQMRIEisrlhkrlGRTMIYVTHDQvEAMTLADKIVVLDAGRV 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
794-1015 |
5.86e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.44 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 794 KANEQIATTKeyldvPIcLQLQNVSYKYKNKDGdftgfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGN 873
Cdd:PRK09452 3 KLNKQPSSLS-----PL-VELRGISKSFDGKEV------ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 874 VLLNGKEIA--PEE---LN---QYYsAILSDFHVFDRL-YGINTEGM-KAEID-HYLELLQLsdkVGIED-GRFTTTQLS 941
Cdd:PRK09452 71 IMLDGQDIThvPAEnrhVNtvfQSY-ALFPHMTVFENVaFGLRMQKTpAAEITpRVMEALRM---VQLEEfAQRKPHQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005564688 942 TGQKKRLAL---LVtyleDRP-ILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMG 1015
Cdd:PRK09452 147 GGQQQRVAIaraVV----NKPkVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqEEALTMSDRIVVMRDG 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
836-1012 |
5.90e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPE---------------ELNqyysaILSDFHVF 900
Cdd:COG1129 23 VSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsprdaqaagiaiihqELN-----LVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 901 D---------RLYGINTEGMKAEIDHYLELLQLS----DKVGiedgrftttQLSTGQKKRL----ALLVtyleDRPILLF 963
Cdd:COG1129 98 EniflgreprRGGLIDWRAMRRRARELLARLGLDidpdTPVG---------DLSVAQQQLVeiarALSR----DARVLIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1005564688 964 DE-WAADQDPGYRRFFyeELLPQMRAKGKCIIAITHD-DQYFHLADKLIVM 1012
Cdd:COG1129 165 DEpTASLTEREVERLF--RIIRRLKAQGVAIIYISHRlDEVFEIADRVTVL 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
812-1026 |
6.47e-12 |
|
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: 66.24 E-value: 6.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYknkdGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELN---- 887
Cdd:cd03265 1 IEVENLVKKY----GDFEA--VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvrrr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 888 -----QYYSA--ILSDF---HVFDRLYGINTEGMKAEIDHYLELLQLSDKvgiEDGRFTTtqLSTGQKKRLALLVTYLED 957
Cdd:cd03265 75 igivfQDLSVddELTGWenlYIHARLYGVPGAERRERIDELLDFVGLLEA---ADRLVKT--YSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 958 RPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
836-1017 |
7.61e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.19 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI----APEE----LNQYYsAILSDFHVFDRL-YGI 906
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsrlhARDRkvgfVFQHY-ALFRHMTVFDNIaFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 907 ---------NTEGMKAEIDHYLELLQLSDKVgiedGRFtTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYR-- 975
Cdd:PRK10851 100 tvlprrerpNAAAIKAKVTQLLEMVQLAHLA----DRY-PAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRke 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1005564688 976 -----RFFYEELlpqmraKGKCIIaITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:PRK10851 175 lrrwlRQLHEEL------KFTSVF-VTHDqEEAMEVADRVVVMSQGNI 215
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
812-1017 |
7.83e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.58 E-value: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGdftgfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELNQ 888
Cdd:PRK11231 3 LRTENLTVGYGTKRI------LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmlsSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 YYsAILSDFHV------FDRL--YG----INTEGMKAEIDHYL--------ELLQLSDKvgiedgrfTTTQLSTGQKKRL 948
Cdd:PRK11231 77 RL-ALLPQHHLtpegitVRELvaYGrspwLSLWGRLSAEDNARvnqameqtRINHLADR--------RLTDLSGGQRQRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005564688 949 ALLVTYLEDRPILLFDEWAADQDPGYRrffYE--ELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQ---VElmRLMRELNTQGKTVVTVLHDlNQASRYCDHLVVLANGHV 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
812-1017 |
9.69e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 66.69 E-value: 9.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKnKDGDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQ--- 888
Cdd:PRK13649 3 INLQNVSYTYQ-AGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 -----------------YYSAILSDFHVFDRLYGINTEGMKAEIDHYLELlqlsdkVGIEDGRFTTT--QLSTGQKKRLA 949
Cdd:PRK13649 82 qirkkvglvfqfpesqlFEETVLKDVAFGPQNFGVSQEEAEALAREKLAL------VGISESLFEKNpfELSGGQMRRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005564688 950 LLVTYLEDRPILLFDEWAADQDPGYRRFFYeELLPQMRAKGKCIIAITH-DDQYFHLADKLIVMEMGTV 1017
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELM-TLFKKLHQSGMTIVLVTHlMDDVANYADFVYVLEKGKL 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
812-1017 |
1.24e-11 |
|
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: 65.37 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGdfTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNE---GNVLLNGKEIAPEELNQ 888
Cdd:cd03234 4 LPWWDVGLKAKNWNK--YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 ---------------------YYSAILsdfhvfdRLYGINTEGMKAEIDHYLELLQLSDKVgIEDGRFttTQLSTGQKKR 947
Cdd:cd03234 82 cvayvrqddillpgltvretlTYTAIL-------RLPRKSSDAIRKKRVEDVLLRDLALTR-IGGNLV--KGISGGERRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005564688 948 LALLVTYLEDRPILLFDEWAADQDPgyrrFFYEELLPQMR--AKGKCIIAIT-HD--DQYFHLADKLIVMEMGTV 1017
Cdd:cd03234 152 VSIAVQLLWDPKVLILDEPTSGLDS----FTALNLVSTLSqlARRNRIVILTiHQprSDLFRLFDRILLLSSGEI 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
812-1017 |
1.25e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.31 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKN------KDgdftgfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA--P 883
Cdd:PRK11160 339 LTLNNVSFTYPDqpqpvlKG----------LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdyS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 884 EE-LNQYYSAILSDFHVF-----DRLyginTEGMKAEIDHylELLQLSDKVGIED---------------GRftttQLST 942
Cdd:PRK11160 409 EAaLRQAISVVSQRVHLFsatlrDNL----LLAAPNASDE--ALIEVLQQVGLEKlleddkglnawlgegGR----QLSG 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005564688 943 GQKKRLALLVTYLEDRPILLFDEWAADQDPGY-RRFFyeELLPQMrAKGKCIIAITHDDQYFHLADKLIVMEMGTV 1017
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQIL--ELLAEH-AQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
598-1018 |
1.44e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.51 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 598 DTE-VISRSLNLLVTA---GTSLLTLLFcflylgVMNMYAFLLSLcIIFITAGVYSLIGRQADKVWNE-TRDIQNVyfrl 672
Cdd:PRK11176 131 DSEqVASSSSGALITVvreGASIIGLFI------MMFYYSWQLSL-ILIVIAPIVSIAIRVVSKRFRNiSKNMQNT---- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 673 IGDLR-------HGFKELRLHTGKRNDfREVMNESCNNYRVK-------RTIGD--IKFANVFVLGELLFIFVigivvfv 736
Cdd:PRK11176 200 MGQVTtsaeqmlKGHKEVLIFGGQEVE-TKRFDKVSNRMRQQgmkmvsaSSISDpiIQLIASLALAFVLYAAS------- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 737 FPEIFVNMPKETISnyvIVFLYMTGpvneILGGIPQLVNVRISWQR----IQQMVKSVDhiKANEQIATTKEYLDVPICL 812
Cdd:PRK11176 272 FPSVMDTLTAGTIT---VVFSSMIA----LMRPLKSLTNVNAQFQRgmaaCQTLFAILD--LEQEKDEGKRVIERAKGDI 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 813 QLQNVSYKYKNKDGDftgfGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEL----NQ 888
Cdd:PRK11176 343 EFRNVTFTYPGKEVP----ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLaslrNQ 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 YysAILS-DFHVFDRL------YGINTEGMKAEIDHYLELLQLSDKV-GIEDGRFTT-----TQLSTGQKKRLALLVTYL 955
Cdd:PRK11176 419 V--ALVSqNVHLFNDTianniaYARTEQYSREQIEEAARMAYAMDFInKMDNGLDTVigengVLLSGGQRQRIAIARALL 496
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005564688 956 EDRPILLFDEWAADQDPGYRRFFY---EELlpqmrAKGKCIIAITHDDQYFHLADKLIVMEMGTVK 1018
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQaalDEL-----QKNRTSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
819-1013 |
2.26e-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: 65.12 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 819 YKYKNKDGDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA--PEELNQYYSAILSD 896
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykPQYIKADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 897 FhvfdrLYGInTEGM------KAEIDHYLELLQLSDKvgiedgrfTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQ 970
Cdd:cd03237 81 L-----LSSI-TKDFythpyfKTEIAKPLQIEQILDR--------EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1005564688 971 DPGYR-------RFFYEEllpqmraKGKCIIAITHdDQYF--HLADKLIVME 1013
Cdd:cd03237 147 DVEQRlmaskviRRFAEN-------NEKTAFVVEH-DIIMidYLADRLIVFE 190
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
812-1015 |
2.44e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 65.98 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNK---DGdftgfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIaPEELNQ 888
Cdd:PRK13537 8 IDFRNVEKRYGDKlvvDG---------LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-PSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 ---------YYSAILSDFHV------FDRLYGINTEGMKAEIDHYLELLQLSDKVgieDGRftTTQLSTGQKKRLALLVT 953
Cdd:PRK13537 78 arqrvgvvpQFDNLDPDFTVrenllvFGRYFGLSAAAARALVPPLLEFAKLENKA---DAK--VGELSGGMKRRLTLARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005564688 954 YLEDRPILLFDEWAADQDPGYRRFFYEELLPQMrAKGKCIIAITH-DDQYFHLADKLIVMEMG 1015
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHfMEEAERLCDRLCVIEEG 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
812-965 |
3.42e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 65.87 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELNQ 888
Cdd:COG1135 2 IELENLSKTFPTKGGPVTA--LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalsERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 YYSAI---------LSDFHVFD------RLYGINtegmKAEIDH-YLELLQLsdkVGIED-GRFTTTQLSTGQKKRLAL- 950
Cdd:COG1135 80 ARRKIgmifqhfnlLSSRTVAEnvalplEIAGVP----KAEIRKrVAELLEL---VGLSDkADAYPSQLSGGQKQRVGIa 152
|
170
....*....|....*...
gi 1005564688 951 --LVTyledRP-ILLFDE 965
Cdd:COG1135 153 raLAN----NPkVLLCDE 166
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
836-1017 |
4.18e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYE--PNEGNVLLNGKEIAPEelnqyySAILSDFhvfdrlyginteGMKA 913
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGRE------ASLIDAI------------GRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 914 EIDHYLELLQLsdkVGIEDG---RFTTTQLSTGQKKR--LALLvtyLEDRP-ILLFDEWAADQDPGYRRFFYEELLPQMR 987
Cdd:COG2401 111 DFKDAVELLNA---VGLSDAvlwLRRFKELSTGQKFRfrLALL---LAERPkLLVIDEFCSHLDRQTAKRVARNLQKLAR 184
|
170 180 190
....*....|....*....|....*....|..
gi 1005564688 988 AKGKCIIAIT-HDDQYFHLA-DKLIVMEMGTV 1017
Cdd:COG2401 185 RAGITLVVAThHYDVIDDLQpDLLIFVGYGGV 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
812-1016 |
4.97e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 64.75 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKnKDGDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNG---------KEIA 882
Cdd:PRK13643 2 IKFEKVNYTYQ-PNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 883 P-----------EELNQYYSAILSDFHVFDRLYGINTEGMKAEIDHYLELLQLSDKVGiEDGRFtttQLSTGQKKRLALL 951
Cdd:PRK13643 81 PvrkkvgvvfqfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFW-EKSPF---ELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005564688 952 VTYLEDRPILLFDEWAADQDPGyRRFFYEELLPQMRAKGKCIIAITH--DD-----QYFHLADKLIVMEMGT 1016
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPK-ARIEMMQLFESIHQSGQTVVLVTHlmDDvadyaDYVYLLEKGHIISCGT 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
836-1017 |
5.61e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.20 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEElnqyysAI----------LSDFHVF-- 900
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsPRD------AIalgigmvhqhFMLVPNLtv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 901 ----------DRLYGINTEGMKAEIDhylellQLSDKVG--------IEDgrftttqLSTGQKKRLALLVTYLEDRPILL 962
Cdd:COG3845 98 aenivlglepTKGGRLDRKAARARIR------ELSERYGldvdpdakVED-------LSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005564688 963 FDE-------WAADQdpgyrrFFyeELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:COG3845 165 LDEptavltpQEADE------LF--EILRRLAAEGKSIIFITHKlREVMAIADRVTVLRRGKV 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
836-1018 |
6.40e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.28 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNG-------KEI--APEELNQYYsailsdfhVFD--RL- 903
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGIclPPEKRRIGY--------VFQdaRLf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 904 ----------YGINtEGMKAEIDHYLELLqlsdkvGIED--GRFTTTqLSTGQKKRLALLVTYLEDRPILLFDEWAADQD 971
Cdd:PRK11144 89 phykvrgnlrYGMA-KSMVAQFDKIVALL------GIEPllDRYPGS-LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1005564688 972 PGYRRffyeELLP--QMRAK--GKCIIAITHD-DQYFHLADKLIVMEMGTVK 1018
Cdd:PRK11144 161 LPRKR----ELLPylERLAReiNIPILYVSHSlDEILRLADRVVVLEQGKVK 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
836-1024 |
6.49e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.19 E-value: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELNQYYS------AILSDfHVFDRL--- 903
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlkPEIYRQQVSycaqtpTLFGD-TVYDNLifp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 904 YGIntEGMKAEIDHYLELLqlsDKVGIEDGRFT--TTQLSTGQKKRLALLVTyLEDRP-ILLFDEWAADQDPGYRRFFYE 980
Cdd:PRK10247 105 WQI--RNQQPDPAIFLDDL---ERFALPDTILTknIAELSGGEKQRISLIRN-LQFMPkVLLLDEITSALDESNKHNVNE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1005564688 981 ELLPQMRAKGKCIIAITHDDQYFHLADKLIVMEMGTVKMNKTKE 1024
Cdd:PRK10247 179 IIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAGEMQEARY 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
812-972 |
6.94e-11 |
|
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: 63.33 E-value: 6.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNK---DGdftgfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQ 888
Cdd:cd03218 1 LRAENLSKRYGKRkvvNG---------VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 -------YY---SAILSDFHVFDRLYGI------NTEGMKAEIDHYLELLQLS---DKVGIedgrftttQLSTGQKKRLA 949
Cdd:cd03218 72 rarlgigYLpqeASIFRKLTVEENILAVleirglSKKEREEKLEELLEEFHIThlrKSKAS--------SLSGGERRRVE 143
|
170 180
....*....|....*....|....*..
gi 1005564688 950 L---LVTyledRP-ILLFDEWAADQDP 972
Cdd:cd03218 144 IaraLAT----NPkFLLLDEPFAGVDP 166
|
|
| PRK13128 |
PRK13128 |
D-aminopeptidase; Reviewed |
50-353 |
7.64e-11 |
|
D-aminopeptidase; Reviewed
Pssm-ID: 171868 [Multi-domain] Cd Length: 518 Bit Score: 66.03 E-value: 7.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 50 PGLSVVIVKGNETIYKKNYGYANTDKKRQVTNETLFELGSTSKAFTALAVLQLEKEGKIkLSDSLTKYVSWFEmeyKGKP 129
Cdd:PRK13128 23 PGGAVAVVKDGEVVLRHAWGFADLARRKAMTPETRMPICSVSKQFTCAVLLDCIGEPEM-LDAALAAYLDQFE---DPRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 130 yeiTLYDLLHHTSGIPEkaigYIPIT--NGKDsIEKTIRNVMPIGLNR-------EPGSSFEYSTVNYDLLGLVIEKATN 200
Cdd:PRK13128 99 ---AVRDLCNNQSGLRD----YWALTvlCGAA-PEGIFLPDQAQNLLRrlktthfAPGTHYSYCNGNFRILADLIEQHTG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 201 QSFeryvqdhvlskLDLLSTyagREMAPLdnmaqGYKRNFLQS---LPYDAPNYRGNTPAGYF--ISNI----------- 264
Cdd:PRK13128 171 RSL-----------ADLLAE---RIFAPA-----GMKTAELIPdtaLFDECTGYEGDTVRGFLpaINRIhwlgdagicas 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 265 -NDMERWlklqlgvekpRMFPEELINDSHKANRKVA-----PDSNGASYAAGWEVYQSGGGEIS-HGGSNPNYSSYIGFR 337
Cdd:PRK13128 232 lDDMIAW----------EQFIDRTRDDENGLYRRLSvpqtfADGAPAPYGFGLKFEETGGKRLTgHGGALRGWRCQRWHC 301
|
330
....*....|....*.
gi 1005564688 338 DEEQIGVVVLANLNSN 353
Cdd:PRK13128 302 ADERLSTIVMFNFEGN 317
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
812-1018 |
7.88e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.86 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYknkdGD---FTGFgigpiDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLnGK--EIApeel 886
Cdd:COG0488 316 LELEGLSKSY----GDktlLDDL-----SLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvKIG---- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 887 nqYYSAILSDFH----VFDRLYGINTEGMKAEIDHYLELL-----QLSDKVGiedgrftttQLSTGQKKRLALLVTYLED 957
Cdd:COG0488 382 --YFDQHQEELDpdktVLDELRDGAPGGTEQEVRGYLGRFlfsgdDAFKPVG---------VLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005564688 958 RPILLFDEWAADQDPGYRRFFyEELLpqMRAKGkCIIAITHdDQYF--HLADKLIVMEMGTVK 1018
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEAL-EEAL--DDFPG-TVLLVSH-DRYFldRVATRILEFEDGGVR 508
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
812-1013 |
8.71e-11 |
|
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: 60.93 E-value: 8.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGdftgfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVllngkeiapeelnqyys 891
Cdd:cd03221 1 IELENLSKTYGGKLL------LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 892 ailsdfhvfdrlyginTEGMKAEIDHYlellqlsdkvgiedgrfttTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQD 971
Cdd:cd03221 58 ----------------TWGSTVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1005564688 972 PGYRRFFYEELlpqmRAKGKCIIAITHdDQYF--HLADKLIVME 1013
Cdd:cd03221 103 LESIEALEEAL----KEYPGTVILVSH-DRYFldQVATKIIELE 141
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
833-1013 |
1.04e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 62.50 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 833 IGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPN---EGNVLLNGKEIAPEELNQYYSAIL-SDFHVFDRLY---- 904
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGILfQDDLLFPHLSvgen 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 905 -------GINTEGMKAEIDHYLELLQLSdkvGIEDgRFTTTqLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRF 977
Cdd:COG4136 97 lafalppTIGRAQRRARVEQALEEAGLA---GFAD-RDPAT-LSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQ 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 1005564688 978 FYEELLPQMRAKGkcIIAI--THDDQYFHLADKLIVME 1013
Cdd:COG4136 172 FREFVFEQIRQRG--IPALlvTHDEEDAPAAGRVLDLG 207
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
836-1018 |
1.07e-10 |
|
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: 62.51 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELNQYYSAILSDFHVFD---RL----YG 905
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkigLHDLRSRISIIPQDPVLFSgtiRSnldpFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 906 INTEgmkAEIDHYLELLQLSDKVGIEDGRFTTT------QLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPgyrrfFY 979
Cdd:cd03244 103 EYSD---EELWQALERVGLKEFVESLPGGLDTVveeggeNLSVGQRQLLCLARALLRKSKILVLDEATASVDP-----ET 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1005564688 980 EELLPQM---RAKGKCIIAITHddqyfHL-----ADKLIVMEMGTVK 1018
Cdd:cd03244 175 DALIQKTireAFKDCTVLTIAH-----RLdtiidSDRILVLDKGRVV 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
836-885 |
1.09e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.16 E-value: 1.09e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGL--YEPNEGNVLLNGKEI---APEE 885
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDIlelSPDE 73
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
836-1017 |
1.79e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.72 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGK--------------EIA-----PEElNQYYSAILSD 896
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldyskrgllalrqQVAtvfqdPEQ-QIFYTDIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 897 FHVFDRLYGINTEGMKAEIDhylELLQLSDKVGIedgRFTTTQ-LSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYR 975
Cdd:PRK13638 99 IAFSLRNLGVPEAEITRRVD---EALTLVDAQHF---RHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1005564688 976 RFFYeELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:PRK13638 173 TQMI-AIIRRIVAQGNHVIISSHDiDLIYEISDAVYVLRQGQI 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
836-1026 |
2.05e-10 |
|
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: 61.68 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI---APEELNQY---YS----AILSDFHVFDRL-- 903
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglPPHERARAgigYVpegrRIFPELTVEENLll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 904 --YGINTEGMKAEIDHYLELL-----QLSDKVGiedgrftttQLSTGQKKRLAL---LVTyledRP-ILLFDE------- 965
Cdd:cd03224 99 gaYARRRAKRKARLERVYELFprlkeRRKQLAG---------TLSGGEQQMLAIaraLMS----RPkLLLLDEpseglap 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005564688 966 -WAADqdpgyrrffYEELLPQMRAKGKCIIAIthdDQYFHLA----DKLIVMEMGTVKMNKTKEAL 1026
Cdd:cd03224 166 kIVEE---------IFEAIRELRDEGVTILLV---EQNARFAleiaDRAYVLERGRVVLEGTAAEL 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
811-1010 |
2.12e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.75 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 811 CLQLQNVSYKYKNKDGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---PEELN 887
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEV--LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtldADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 888 Q----YYSAILSDFHVFDRLY------------GINTEGMKAEIDHYLELLQLSDKVGiedgrFTTTQLSTGQKKRLALL 951
Cdd:PRK10535 82 QlrreHFGFIFQRYHLLSHLTaaqnvevpavyaGLERKQRLLRAQELLQRLGLEDRVE-----YQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 952 VTYLEDRPILLFDE--WAADQDPGyrrffyEE---LLPQMRAKGKCIIAITHDDQYFHLADKLI 1010
Cdd:PRK10535 157 RALMNGGQVILADEptGALDSHSG------EEvmaILHQLRDRGHTVIIVTHDPQVAAQAERVI 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
810-1022 |
2.32e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.33 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 810 ICLQLQNVSYKYKNK-DGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNV-----LLNGKEIAP 883
Cdd:PRK13631 20 IILRVKNLYCVFDEKqENELVA--LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 884 EELNQYYSAILSDFH--------VF--------------DRLYGINTEGMKAEIDH-----YLELLQLSDKVgIEDGRFt 936
Cdd:PRK13631 98 ELITNPYSKKIKNFKelrrrvsmVFqfpeyqlfkdtiekDIMFGPVALGVKKSEAKklakfYLNKMGLDDSY-LERSPF- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 937 ttQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDP-GYRRFFyeELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEM 1014
Cdd:PRK13631 176 --GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPkGEHEMM--QLILDAKANNKTVFVITHTmEHVLEVADEVIVMDK 251
|
....*...
gi 1005564688 1015 GTVKMNKT 1022
Cdd:PRK13631 252 GKILKTGT 259
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
839-1027 |
3.66e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.91 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 839 EFNSGEIVFIAGGNGSGKSTLSKLITGLYEPN---EGNVLLNGKEIAPEELNQYYSAILSD------FHVFDRLY----- 904
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISAYVQQDdlfiptLTVREHLMfqahl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 905 ----GINTEGMKAEIDHYLELLQLSD----KVGIEDgrfTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDpGYRR 976
Cdd:TIGR00955 127 rmprRVTKKEKRERVDEVLQALGLRKcantRIGVPG---RVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD-SFMA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 977 FFYEELLPQMRAKGKCIIAITHDDQY--FHLADKLIVMEMG-TVKMNKTKEALS 1027
Cdd:TIGR00955 203 YSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGrVAYLGSPDQAVP 256
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
836-1015 |
3.85e-10 |
|
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: 64.26 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI-------------APEELNQYYSAILSDFHVF-D 901
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnldavrqslgmCPQHNILFHHLTVAEHILFyA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 902 RLYGINTEGMKAEIDHYLELLQLSDKVGIEdgrftTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEE 981
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLEDTGLHHKRNEE-----AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190
....*....|....*....|....*....|....
gi 1005564688 982 LLpQMRAKGKCIIAITHDDQYFHLADKLIVMEMG 1015
Cdd:TIGR01257 1104 LL-KYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
836-1026 |
5.07e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.14 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA-------------PEELNQYYSAILSDFHVFDr 902
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQHFN- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 903 LYGINT---EGMKAEIdhylELLQLS------------DKVGIED---GRFtTTQLSTGQKKRLALLVTYLEDRPILLFD 964
Cdd:PRK10619 103 LWSHMTvleNVMEAPI----QVLGLSkqeareravkylAKVGIDEraqGKY-PVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005564688 965 EWAADQDPgyrRFFYEEL--LPQMRAKGKCIIAITHDDQYF-HLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:PRK10619 178 EPTSALDP---ELVGEVLriMQQLAEEGKTMVVVTHEMGFArHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
811-1017 |
6.20e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.17 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 811 CLQLQNVSykyKNKDGDFtgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGK---EIAPEELN 887
Cdd:PRK11650 3 GLKLQAVR---KSYDGKT--QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnELEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 888 -----QYYsAILSDFHVFDRL-YGINTEGM-KAEIDH-------YLELLQLSDKvgiedgrfTTTQLSTGQKKRLALlvt 953
Cdd:PRK11650 78 iamvfQNY-ALYPHMSVRENMaYGLKIRGMpKAEIEErvaeaarILELEPLLDR--------KPRELSGGQRQRVAM--- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005564688 954 yleDRPI------LLFDEWAADQDPGYRrffyeellPQMRAK--------GKCIIAITHDD-QYFHLADKLIVMEMGTV 1017
Cdd:PRK11650 146 ---GRAIvrepavFLFDEPLSNLDAKLR--------VQMRLEiqrlhrrlKTTSLYVTHDQvEAMTLADRVVVMNGGVA 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
813-965 |
7.32e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 62.67 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 813 QLQNVSYKYKNKdgdftGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAP---EELNQY 889
Cdd:PRK13657 336 EFDDVSFSYDNS-----RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvtrASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 890 YSAILSDFHVFDRLYGIN-----TEGMKAEIDHYLELLQLSDKVGIEDGRFTT------TQLSTGQKKRLALLVTYLEDR 958
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNirvgrPDATDEEMRAAAERAQAHDFIERKPDGYDTvvgergRQLSGGERQRLAIARALLKDP 490
|
....*..
gi 1005564688 959 PILLFDE 965
Cdd:PRK13657 491 PILILDE 497
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
837-1017 |
8.53e-10 |
|
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: 60.25 E-value: 8.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 837 DMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQYYS--AILS-DFHVFDR------LYGIN 907
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSqiGLVSqEPVLFDGtiaeniRYGKP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 908 --TEGM------KAEIDHYLELL--QLSDKVGiEDGrfttTQLSTGQKKRLALLVTYLEDRPILLFDEW--AADQDpgyr 975
Cdd:cd03249 103 daTDEEveeaakKANIHDFIMSLpdGYDTLVG-ERG----SQLSGGQKQRIAIARALLRNPKILLLDEAtsALDAE---- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1005564688 976 rffyEELLPQ----MRAKGKCIIAITHDDQYFHLADKLIVMEMGTV 1017
Cdd:cd03249 174 ----SEKLVQealdRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQV 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
836-972 |
8.91e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.48 E-value: 8.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIApeELNQYY-SAILSdfHVF-DRLYGinT-EGM- 911
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--KLPEYKrAKYIG--RVFqDPMMG--TaPSMt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 912 ----------------------KAEIDHYLELL---------QLSDKVGiedgrftttQLSTGQKKRLALLVTYLEDRPI 960
Cdd:COG1101 99 ieenlalayrrgkrrglrrgltKKRRELFRELLatlglglenRLDTKVG---------LLSGGQRQALSLLMATLTKPKL 169
|
170
....*....|..
gi 1005564688 961 LLFDEWAADQDP 972
Cdd:COG1101 170 LLLDEHTAALDP 181
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
836-1024 |
1.36e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.08 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGL--YEPNEGNVLLNGKEIApeELNQYYSAILSDFHVFDRLYGIntEGMKa 913
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDIT--DLPPEERARLGIFLAFQYPPEI--PGVK- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 914 eIDHYLellqlsdkvgiedgRFTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFyEELLPQMRAKGKCI 993
Cdd:cd03217 94 -NADFL--------------RYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV-AEVINKLREEGKSV 157
|
170 180 190
....*....|....*....|....*....|...
gi 1005564688 994 IAITHDDQYFHL--ADKLIVMEMGTVKMNKTKE 1024
Cdd:cd03217 158 LIITHYQRLLDYikPDRVHVLYDGRIVKSGDKE 190
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
812-1017 |
1.75e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.18 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKnKDGDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQYYS 891
Cdd:PRK13646 3 IRFDNVSYTYQ-KGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 892 AI---------LSDFHVFD-----------RLYGINTEGMKAEIDHYLELLQLSDKVgIEDGRFtttQLSTGQKKRLALL 951
Cdd:PRK13646 82 PVrkrigmvfqFPESQLFEdtvereiifgpKNFKMNLDEVKNYAHRLLMDLGFSRDV-MSQSPF---QMSGGQMRKIAIV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005564688 952 VTYLEDRPILLFDEWAADQDPGYRRFFYeELLPQMRAK-GKCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVM-RLLKSLQTDeNKTIILVSHDmNEVARYADEVIVMKEGSI 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
812-1015 |
1.81e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.71 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGdftgfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI----APEELN 887
Cdd:PRK11248 2 LQISHLYADYGGKPA------LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegpgAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 888 QYYSAILSDFHVFDRL-YGINTEGM-KAEIDHY-LELLQlsdKVGIE--DGRFtTTQLSTGQKKRLALLVTYLEDRPILL 962
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVaFGLQLAGVeKMQRLEIaHQMLK---KVGLEgaEKRY-IWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 963 FDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMG 1015
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDiEEAVFMATELVLLSPG 205
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
836-965 |
1.84e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.49 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEElNQYYSAI---------------LSD-FHV 899
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRR-KEFARRIgvvfgqrsqlwwdlpAIDsFRL 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005564688 900 FDRLYGINTEGMKAEIDHYLELLQLSDKVGIedgrfTTTQLSTGQKKRLALLVTYLEDRPILLFDE 965
Cdd:COG4586 120 LKAIYRIPDAEYKKRLDELVELLDLGELLDT-----PVRQLSLGQRMRCELAAALLHRPKILFLDE 180
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
812-999 |
1.93e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKnkdgdftgfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYePNEGNVLLNGKEIAPEELNQ--Y 889
Cdd:PRK03695 1 MQLNDVAVSTR----------LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAElaR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 890 YSAILSD-------FHVFDRLY-----GINTEGMKAEIDHYLELLQLSDKVgiedGRfTTTQLSTGQKKRLALLVTYLED 957
Cdd:PRK03695 70 HRAYLSQqqtppfaMPVFQYLTlhqpdKTRTEAVASALNEVAEALGLDDKL----GR-SVNQLSGGEWQRVRLAAVVLQV 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1005564688 958 RP-------ILLFDEWAADQDPGYRRFFYeELLPQMRAKGKCIIAITHD 999
Cdd:PRK03695 145 WPdinpagqLLLLDEPMNSLDVAQQAALD-RLLSELCQQGIAVVMSSHD 192
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
755-1027 |
2.70e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 755 VFLYMTGPVNEILGGIPQLVNVRISWQRIQQMVKSvdhikaNEQIATTKEYLDVPI-CLQLQNVSYKYKNKDGDFTgfgI 833
Cdd:PLN03232 563 LFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLS------EERILAQNPPLQPGApAISIKNGYFSWDSKTSKPT---L 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 834 GPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNE-GNVLLNGKEIAPEELNQYYSAILSDfhvfDRLYGINTEGMK 912
Cdd:PLN03232 634 SDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRE----NILFGSDFESER 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 913 -------AEIDHYLELLQLSDKVGI-EDGrfttTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELLP 984
Cdd:PLN03232 710 ywraidvTALQHDLDLLPGRDLTEIgERG----VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK 785
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1005564688 985 QmRAKGKCIIAITHDDQYFHLADKLIVMEMGTVKMNKTKEALS 1027
Cdd:PLN03232 786 D-ELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
836-999 |
5.17e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.58 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEE------LNQYYSAILSDFH------VFDR- 902
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnrevpfLRRQIGMIFQDHHllmdrtVYDNv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 903 -----LYGINTEGMKAEIDHYLellqlsDKVGIED-GRFTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQD----P 972
Cdd:PRK10908 101 aipliIAGASGDDIRRRVSAAL------DKVGLLDkAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalsE 174
|
170 180
....*....|....*....|....*..
gi 1005564688 973 GYRRFFYEellpqMRAKGKCIIAITHD 999
Cdd:PRK10908 175 GILRLFEE-----FNRVGVTVLMATHD 196
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
812-1027 |
7.44e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.17 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFTGfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIapeelnQYYS 891
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKG-----INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI------KYDK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 892 AILSDFH-----VF----DRLY---------------GINTEGMKAEIDHYLEllqlsdKVGIED-GRFTTTQLSTGQKK 946
Cdd:PRK13639 71 KSLLEVRktvgiVFqnpdDQLFaptveedvafgplnlGLSKEEVEKRVKEALK------AVGMEGfENKPPHHLSGGQKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 947 RLAlLVTYLEDRP-ILLFDEWAADQDP-GYRRFFyeELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTVKMNKT- 1022
Cdd:PRK13639 145 RVA-IAGILAMKPeIIVLDEPTSGLDPmGASQIM--KLLYDLNKEGITIIISTHDvDLVPVYADKVYVMSDGKIIKEGTp 221
|
....*
gi 1005564688 1023 KEALS 1027
Cdd:PRK13639 222 KEVFS 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
836-1017 |
9.82e-09 |
|
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: 56.53 E-value: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNsGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGK---------EIAPEE-----LNQYYsAILSDFHVFD 901
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkiNLPPQQrkiglVFQQY-ALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 902 RL-YGINTEGMKAEIDHYLELLQLSDKVGIEDGRftTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRrffyE 980
Cdd:cd03297 95 NLaFGLKRKRNREDRISVDELLDLLGLDHLLNRY--PAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR----L 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1005564688 981 ELLPQMRA-----KGKCIIaITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:cd03297 169 QLLPELKQikknlNIPVIF-VTHDlSEAEYLADRIVVMEDGRL 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
850-1017 |
1.04e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.50 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 850 GGNGSGKSTLSKLITGLYEPNEGN---VLLNGKEIAPEEL---------------NQYYSAILSD---FHVFDRlyGINT 908
Cdd:PRK13640 40 GHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVwdirekvgivfqnpdNQFVGATVGDdvaFGLENR--AVPR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 909 EGMKAEIDHYLELLQLSDKVGIEdgrftTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRA 988
Cdd:PRK13640 118 PEMIKIVRDVLADVGMLDYIDSE-----PANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKK 192
|
170 180
....*....|....*....|....*....
gi 1005564688 989 KGKCIIAITHDDQYFHLADKLIVMEMGTV 1017
Cdd:PRK13640 193 NNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
839-1013 |
1.20e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.03 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 839 EFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKeIA--PeelnQYysaILSDFH--VFDRLYGINTEGM--- 911
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-ISykP----QY---ISPDYDgtVEEFLRSANTDDFgss 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 912 --KAEIDHYLELLQLSDKvgiedgrfTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYR--------RFfyee 981
Cdd:COG1245 434 yyKTEIIKPLGLEKLLDK--------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavakairRF---- 501
|
170 180 190
....*....|....*....|....*....|....
gi 1005564688 982 llpqMRAKGKCIIAITHdDQYFH--LADKLIVME 1013
Cdd:COG1245 502 ----AENRGKTAMVVDH-DIYLIdyISDRLMVFE 530
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
847-973 |
1.65e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.58 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 847 FIA--GGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAP---EELNQYYSAILSDFHVF-DRLYGINTEGM---KAEIDH 917
Cdd:PRK10790 369 FVAlvGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlshSVLRQGVAMVQQDPVVLaDTFLANVTLGRdisEEQVWQ 448
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005564688 918 YLELLQLSDKV-GIEDGRFTT-----TQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPG 973
Cdd:PRK10790 449 ALETVQLAELArSLPDGLYTPlgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG 510
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
812-1018 |
1.88e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.36 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYK---------------NKDGDFTgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLL 876
Cdd:PRK13545 5 VKFEHVTKKYKmynkpfdklkdlffrSKDGEYH-YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 877 NGKE--IA-PEELNQYYSAIlSDFHVFDRLYGINTEGMKAEIDHYLELLQLsdkvgiedGRFTTTQL---STGQKKRLAL 950
Cdd:PRK13545 84 KGSAalIAiSSGLNGQLTGI-ENIELKGLMMGLTKEKIKEIIPEIIEFADI--------GKFIYQPVktySSGMKSRLGF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005564688 951 LVTYLEDRPILLFDEWAADQDpgyrRFFYEELLPQM---RAKGKCIIAITHD-DQYFHLADKLIVMEMGTVK 1018
Cdd:PRK13545 155 AISVHINPDILVIDEALSVGD----QTFTKKCLDKMnefKEQGKTIFFISHSlSQVKSFCTKALWLHYGQVK 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
812-1018 |
1.97e-08 |
|
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: 56.99 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFT---GfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPN---EGNVLLNGKEIA--- 882
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdG-----VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLkls 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 883 PEELNQY------------YSA---------ILSDfhVFDRLYGINTEGMKAEIdhyLELLqlsDKVGIED-----GRFt 936
Cdd:COG0444 77 EKELRKIrgreiqmifqdpMTSlnpvmtvgdQIAE--PLRIHGGLSKAEARERA---IELL---ERVGLPDperrlDRY- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 937 TTQLSTGQKKR----LALLVtyledRPILLFdewaADqdpgyrrffyE--------------ELLPQMRAK-GKCIIAIT 997
Cdd:COG0444 148 PHELSGGMRQRvmiaRALAL-----EPKLLI----AD----------EpttaldvtiqaqilNLLKDLQRElGLAILFIT 208
|
250 260
....*....|....*....|....*...
gi 1005564688 998 HDdq-yfHLADKLIVM------EMGTVK 1018
Cdd:COG0444 209 HDlgvvaEIADRVAVMyagrivEEGPVE 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
836-965 |
2.08e-08 |
|
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: 58.29 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIApeELNQYY--SAI--------LsdfhvF-DRL- 903
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR--DVTQASlrAAIgivpqdtvL-----FnDTIa 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005564688 904 ----YGiNTEGMKAEIDHYLELLQLSDKV-GIEDGRFTTT-----QLSTGQKKRLALLVTYLEDRPILLFDE 965
Cdd:COG5265 450 yniaYG-RPDASEEEVEAAARAAQIHDFIeSLPDGYDTRVgerglKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
812-1009 |
2.34e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.98 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKnkDGDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGkeiapEELNQYYS 891
Cdd:PRK11629 6 LQCDNLCKRYQ--EGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNG-----QPMSKLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 892 A------------------ILSDFHVFDR-----LYGinteGMK-AEI-DHYLELLQlsdKVGIED-GRFTTTQLSTGQK 945
Cdd:PRK11629 79 AakaelrnqklgfiyqfhhLLPDFTALENvamplLIG----KKKpAEInSRALEMLA---AVGLEHrANHRPSELSGGER 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 946 KRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHDdqyFHLADKL 1009
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHD---LQLAKRM 212
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
836-1007 |
5.41e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIApEELNQYYSAILSDFHVF----------DRLYG 905
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-KDLCTYQKQLCFVGHRSginpyltlreNCLYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 906 INTEGMKAEIDHYLELLQLSDKVGiedgrFTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEElLPQ 985
Cdd:PRK13540 99 IHFSPGAVGITELCRLFSLEHLID-----YPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITK-IQE 172
|
170 180
....*....|....*....|..
gi 1005564688 986 MRAKGKCIIAITHDDQYFHLAD 1007
Cdd:PRK13540 173 HRAKGGAVLLTSHQDLPLNKAD 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
836-1012 |
7.17e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 53.78 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLN-GKEIA--PE--ELNQYYSAILSDFHVFDR-----LYG 905
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAgGARVAyvPQrsEVPDSLPLTVRDLVAMGRwarrgLWR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 906 INTEGMKAEIDHYLELLQLSDkvgIEDGRFTTtqLSTGQKKRlALLVTYLEDRP-ILLFDEWAADQDPGYRRFFYeELLP 984
Cdd:NF040873 91 RLTRDDRAAVDDALERVGLAD---LAGRQLGE--LSGGQRQR-ALLAQGLAQEAdLLLLDEPTTGLDAESRERII-ALLA 163
|
170 180
....*....|....*....|....*...
gi 1005564688 985 QMRAKGKCIIAITHDDQYFHLADKLIVM 1012
Cdd:NF040873 164 EEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
827-1027 |
8.60e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 8.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 827 DFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---------------PEELNQ--- 888
Cdd:PRK15439 273 DLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINalstaqrlarglvylPEDRQSsgl 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 889 YYSAILSdFHVFDRLYG-----INTEGMKAEIDHYLELLqlsdkvGI--EDGRFTTTQLSTGQKKRLaLLVTYLEDRPIL 961
Cdd:PRK15439 353 YLDAPLA-WNVCALTHNrrgfwIKPARENAVLERYRRAL------NIkfNHAEQAARTLSGGNQQKV-LIAKCLEASPQL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005564688 962 LF-DEWAADQDPGYRRFFYeELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTVKMNKTKEALS 1027
Cdd:PRK15439 425 LIvDEPTRGVDVSARNDIY-QLIRSIAAQNVAVLFISSDlEEIEQMADRVLVMHQGEISGALTGAAIN 491
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
812-1015 |
9.88e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 55.23 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSykyKNKDGDFtgfGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIApeELNQYYS 891
Cdd:PRK11607 20 LEIRNLT---KSFDGQH---AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 892 AI---LSDFHVFDRL-------YGINTEGM-KAEI-DHYLELLQLsdkVGIED-GRFTTTQLSTGQKKRLALLVTyLEDR 958
Cdd:PRK11607 92 PInmmFQSYALFPHMtveqniaFGLKQDKLpKAEIaSRVNEMLGL---VHMQEfAKRKPHQLSGGQRQRVALARS-LAKR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1005564688 959 P-ILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMG 1015
Cdd:PRK11607 168 PkLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDqEEAMTMAGRIAIMNRG 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
812-1017 |
1.69e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.64 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDF---TGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI------- 881
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWFrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 882 -----------APEELN--QYYSAILsDFHVfdRLygiNTE--GMKAEIDHYLELLQlsdkVGI--EDGRFTTTQLSTGQ 944
Cdd:PRK15112 85 rsqrirmifqdPSTSLNprQRISQIL-DFPL--RL---NTDlePEQREKQIIETLRQ----VGLlpDHASYYPHMLAPGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 945 KKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAIT-HDDQYFHLADKLIVMEMGTV 1017
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
839-1013 |
1.95e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 839 EFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKeIA--PeelnQYysaILSDFH--VFDRLYGI----NTEG 910
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-ISykP----QY---IKPDYDgtVEDLLRSItddlGSSY 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 911 MKAEIDHYLELLQLSDKvgiedgrfTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYR--------RFfyeel 982
Cdd:PRK13409 433 YKSEIIKPLQLERLLDK--------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavakairRI----- 499
|
170 180 190
....*....|....*....|....*....|...
gi 1005564688 983 lpqMRAKGKCIIAITHdDQYFH--LADKLIVME 1013
Cdd:PRK13409 500 ---AEEREATALVVDH-DIYMIdyISDRLMVFE 528
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
848-1017 |
2.24e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.65 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 848 IAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEEL---------------NQYYSAILSDFHVFDRL-YGINTEGM 911
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIrevrkfvglvfqnpdDQIFSPTVEQDIAFGPInLGLDEETV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 912 KAEIDHYLELLqlsdkvGIEDGRFTTT-QLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRAKG 990
Cdd:PRK13652 115 AHRVSSALHML------GLEELRDRVPhHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYG 188
|
170 180
....*....|....*....|....*...
gi 1005564688 991 KCIIAITHD-DQYFHLADKLIVMEMGTV 1017
Cdd:PRK13652 189 MTVIFSTHQlDLVPEMADYIYVMDKGRI 216
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
836-1026 |
2.44e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.07 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIapEELNQYYSA---ILSDF-HVfdRLYG------ 905
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI--EGLPGHQIArmgVVRTFqHV--RLFRemtvie 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 906 ------------------INTEGM-KAEID------HYLELLQLSDKVGIEDGrftttQLSTGQKKRLAL---LVTyled 957
Cdd:PRK11300 100 nllvaqhqqlktglfsglLKTPAFrRAESEaldraaTWLERVGLLEHANRQAG-----NLAYGQQRRLEIarcMVT---- 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005564688 958 RP-ILLFDEWAADQDPGYRRFFyEELLPQMRAK-GKCIIAITHDDQY-FHLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:PRK11300 171 QPeILMLDEPAAGLNPKETKEL-DELIAELRNEhNVTVLLIEHDMKLvMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
836-1015 |
2.85e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.72 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITG--LYEPNEGNVLLNGK---EIAPEELNQyysaiLSDFHVFDrlYGINTEG 910
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGEsilDLEPEERAH-----LGIFLAFQ--YPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 911 M------------------KAEID--HYLELL-QLSDKVGIED---GRFTTTQLSTGQKKRLALLVTYLEDRPILLFDEW 966
Cdd:CHL00131 99 VsnadflrlaynskrkfqgLPELDplEFLEIInEKLKLVGMDPsflSRNVNEGFSGGEKKRNEILQMALLDSELAILDET 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1005564688 967 AADQDPGYRRFFYEElLPQMRAKGKCIIAITHddqYFHLADKLI-----VMEMG 1015
Cdd:CHL00131 179 DSGLDIDALKIIAEG-INKLMTSENSIILITH---YQRLLDYIKpdyvhVMQNG 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
836-1016 |
2.96e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKE---------------IAPEELnqyysAILSDFHVF 900
Cdd:PRK09700 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkldhklaaqlgigIIYQEL-----SVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 901 DRLY----------GINTegmkaeIDhYLELLQ----LSDKVGIE-DGRFTTTQLSTGQKKRLALLVTYLEDRPILLFDE 965
Cdd:PRK09700 99 ENLYigrhltkkvcGVNI------ID-WREMRVraamMLLRVGLKvDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1005564688 966 WAAD-QDPGYRRFFYeeLLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGT 1016
Cdd:PRK09700 172 PTSSlTNKEVDYLFL--IMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDGS 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
834-1015 |
3.31e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.08 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 834 GPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGlYEPNEGNVLLNGKEIAPEELNQYYSAI--------LsdFH--VFDRL 903
Cdd:PRK11174 367 GPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLswvgqnpqL--PHgtLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 904 YGINTEGMKAEIDHYLELLQLSDKV-GIEDGRFTTTQ-----LSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRF 977
Cdd:PRK11174 444 LLGNPDASDEQLQQALENAWVSEFLpLLPQGLDTPIGdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
170 180 190
....*....|....*....|....*....|....*...
gi 1005564688 978 FYEELLPQMRakGKCIIAITHDDQYFHLADKLIVMEMG 1015
Cdd:PRK11174 524 VMQALNAASR--RQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
841-1017 |
3.94e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 841 NSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAP---EELNQYYSAILSDFHVFDRLYGINT----EGMKA 913
Cdd:PTZ00243 1334 APREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAyglRELRRQFSMIPQDPVLFDGTVRQNVdpflEASSA 1413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 914 EIDHYLELLQLSDKVGIEDGRFTTTQL------STGQKKRLALLVTYLE-DRPILLFDEWAADQDPGYRRFFYEELLPQM 986
Cdd:PTZ00243 1414 EVWAALELVGLRERVASESEGIDSRVLeggsnySVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAF 1493
|
170 180 190
....*....|....*....|....*....|....*
gi 1005564688 987 RAkgKCIIAITHD----DQYfhlaDKLIVMEMGTV 1017
Cdd:PTZ00243 1494 SA--YTVITIAHRlhtvAQY----DKIIVMDHGAV 1522
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
836-1017 |
4.37e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.44 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVL-----------LNGKEIAPEELNQYYSAILSDFHVFDRLY 904
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarsLSQQKGLIRQLRQHVGFVFQNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 905 GINT--EG---MKAEIDHYLELL--QLSDKVGIEdGRFTT--TQLSTGQKKRLAlLVTYLEDRP-ILLFDEWAADQDPGy 974
Cdd:PRK11264 102 VLENiiEGpviVKGEPKEEATARarELLAKVGLA-GKETSypRRLSGGQQQRVA-IARALAMRPeVILFDEPTSALDPE- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1005564688 975 rrfFYEELLPQMRA---KGKCIIAITHDDQYFH-LADKLIVMEMGTV 1017
Cdd:PRK11264 179 ---LVGEVLNTIRQlaqEKRTMVIVTHEMSFARdVADRAIFMDQGRI 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
836-965 |
4.75e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.53 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLL-NGKEIApeELNQyySAILSDFH-VFDRLYGINTE--GM 911
Cdd:COG0488 17 VSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRIG--YLPQ--EPPLDDDLtVLDTVLDGDAElrAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 912 KAEIDHYLELLQLSDKVGIE-----------DG--------------RFTTTQ-------LSTGQKKRLAL---LVTyle 956
Cdd:COG0488 93 EAELEELEAKLAEPDEDLERlaelqeefealGGweaearaeeilsglGFPEEDldrpvseLSGGWRRRVALaraLLS--- 169
|
170
....*....|
gi 1005564688 957 dRP-ILLFDE 965
Cdd:COG0488 170 -EPdLLLLDE 178
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
836-1027 |
6.11e-07 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 53.27 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNV-LLNGKE------IAPEE----------LNQYYSaILSDFH 898
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEwvdmtkPGPDGrgrakryigiLHQEYD-LYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 899 VFDRLyginTEGMKAEID---------HYLELLQLSDKVGIEDGRFTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAAD 969
Cdd:TIGR03269 382 VLDNL----TEAIGLELPdelarmkavITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 970 QDPGYRRFFYEELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMGT-VKMNKTKEALS 1027
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKiVKIGDPEEIVE 517
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
812-883 |
8.82e-07 |
|
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: 51.28 E-value: 8.82e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005564688 812 LQLQNVSYKYKNKDGDFTgfgI-GPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAP 883
Cdd:COG4181 9 IELRGLTKTVGTGAGELT---IlKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA 78
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
820-1027 |
1.43e-06 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 52.11 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 820 KYKNKDGDFTGF-GIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGL--YEPNEGNVLLN------------------- 877
Cdd:TIGR03269 2 EVKNLTKKFDGKeVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 878 ----GKEIAPEELN--------------------QYYSAILSDFHVFDR----LYGINTEGMKAeIDHYLELLqlsDKVG 929
Cdd:TIGR03269 82 cpvcGGTLEPEEVDfwnlsdklrrrirkriaimlQRTFALYGDDTVLDNvleaLEEIGYEGKEA-VGRAVDLI---EMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 930 IEDgRFT--TTQLSTGQKKRLaLLVTYLEDRPILLF-DEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITHDDQYFH-L 1005
Cdd:TIGR03269 158 LSH-RIThiARDLSGGEKQRV-VLARQLAKEPFLFLaDEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEdL 235
|
250 260
....*....|....*....|..
gi 1005564688 1006 ADKLIVMEMGTVKMNKTKEALS 1027
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVV 257
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
826-998 |
1.51e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.43 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 826 GDFT-----GFGIGpidmefnSGEIV-FIaGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQ-----YYSAIL 894
Cdd:NF033858 277 GDFTavdhvSFRIR-------RGEIFgFL-GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATrrrvgYMSQAF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 895 S-----------DFHVfdRLYGINTEGMKAEIDhylELLQLSDKVGIEDGRftTTQLSTGQKKRLALLVTYLEDRPILLF 963
Cdd:NF033858 349 SlygeltvrqnlELHA--RLFHLPAAEIAARVA---EMLERFDLADVADAL--PDSLPLGIRQRLSLAVAVIHKPELLIL 421
|
170 180 190
....*....|....*....|....*....|....*
gi 1005564688 964 DEWAADQDPGYRRFFYEELLPQMRAKGKCIIAITH 998
Cdd:NF033858 422 DEPTSGVDPVARDMFWRLLIELSREDGVTIFISTH 456
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
836-1027 |
1.79e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 50.86 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNV--------------------------------LLNGKEIAP 883
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvleklviqktrfkkIKKIKEIRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 884 E--------ELNQYYSAILSDFHVFDRLYGINTEGMKAEIDHYLELLQLsDKVGIEDGRFtttQLSTGQKKRLALLVTYL 955
Cdd:PRK13651 106 RvgvvfqfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL-DESYLQRSPF---ELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005564688 956 EDRPILLFDEWAADQDP-GYRRFFyeELLPQMRAKGKCIIAITHD-DQYFHLADKLIVMEMG-TVKMNKTKEALS 1027
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPqGVKEIL--EIFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFKDGkIIKDGDTYDILS 254
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
812-972 |
2.14e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.01 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFTgfgigpIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNG-----------KE 880
Cdd:PRK11124 3 IQLNGINCFYGAHQALFD------ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 881 IApeELNQYYSAILSDFHVFD-------------RLYGINTEGMKAEIDHYLELLQLSDKVGiedgRFTTtQLSTGQKKR 947
Cdd:PRK11124 77 IR--ELRRNVGMVFQQYNLWPhltvqqnlieapcRVLGLSKDQALARAEKLLERLRLKPYAD----RFPL-HLSGGQQQR 149
|
170 180
....*....|....*....|....*
gi 1005564688 948 LALLVTYLEDRPILLFDEWAADQDP 972
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDP 174
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
724-1026 |
2.78e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.87 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 724 LLFIFVIGIVVFVFPEIFVNMPKETISnyVIVFLYMTGPVNEILGGIPQLVNVRISWQRIQQMVksvdhikaneqiatTK 803
Cdd:TIGR00957 553 LVALITFAVYVTVDENNILDAEKAFVS--LALFNILRFPLNILPMVISSIVQASVSLKRLRIFL--------------SH 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 804 EYLDvPICLQLQNVS----YKYKNKDGDFT-GFGIGP----IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNV 874
Cdd:TIGR00957 617 EELE-PDSIERRTIKpgegNSITVHNATFTwARDLPPtlngITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 875 LLNGK-EIAPEElnqyySAILSDFHVFDRLYG--INTEGMKAEIDHY-----LELLQLSDKVGI-EDGrfttTQLSTGQK 945
Cdd:TIGR00957 696 HMKGSvAYVPQQ-----AWIQNDSLRENILFGkaLNEKYYQQVLEACallpdLEILPSGDRTEIgEKG----VNLSGGQK 766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 946 KRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELL-PQMRAKGKCIIAITHDDQYFHLADKLIVMEMGTV-KMNKTK 1023
Cdd:TIGR00957 767 QRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKIsEMGSYQ 846
|
...
gi 1005564688 1024 EAL 1026
Cdd:TIGR00957 847 ELL 849
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
809-1012 |
4.21e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.41 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 809 PICLQLQNVSYKyknkdGDFTGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA------ 882
Cdd:COG3845 255 EVVLEVENLSVR-----DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITglspre 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 883 ---------PEE-----------------LNQYYSAILSDFHVFDRlygintegmkAEIDHYLEllQLSDKVGI--EDGR 934
Cdd:COG3845 330 rrrlgvayiPEDrlgrglvpdmsvaenliLGRYRRPPFSRGGFLDR----------KAIRAFAE--ELIEEFDVrtPGPD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 935 FTTTQLSTG--QKkrlALLVTYLEDRPILLFdewaADQ-----DPGYRRFFYEELLpQMRAKGKCIIAITHD-DQYFHLA 1006
Cdd:COG3845 398 TPARSLSGGnqQK---VILARELSRDPKLLI----AAQptrglDVGAIEFIHQRLL-ELRDAGAAVLLISEDlDEILALS 469
|
....*.
gi 1005564688 1007 DKLIVM 1012
Cdd:COG3845 470 DRIAVM 475
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
499-685 |
4.53e-06 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 49.74 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 499 LLTLIVLGLISGFGNafLIF------VINETFVRSNNLEN--GLLFYFVLGIVMYVFSQRIIrtsivSYTNE-LVYEKRM 569
Cdd:cd18551 1 LILALLLSLLGTAAS--LAQpllvknLIDALSAGGSSGGLlaLLVALFLLQAVLSALSSYLL-----GRTGErVVLDLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 570 ELTDKLLQTPYYKLELIEKGRIEATLNNDTEVISRSL-NLLVTAGTSLLTLLFCFLYLGVMNMYAFLLSLCIIFITAGVY 648
Cdd:cd18551 74 RLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELItSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLII 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1005564688 649 SLIGRQADKVwneTRDIQNVYFRLIGDLRHGFKELRL 685
Cdd:cd18551 154 LPLGRRIRKA---SKRAQDALGELSAALERALSAIRT 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
836-883 |
4.63e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.43 E-value: 4.63e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAP 883
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR 77
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
836-1013 |
4.98e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.38 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQYYS------------AILSDFHVFDRL 903
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrkrmsmlfqsgALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 904 YGINTE--GMKAEIDHYLELLQLsDKVGIED-GRFTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDP---GYRRF 977
Cdd:PRK11831 106 AYPLREhtQLPAPLLHSTVMMKL-EAVGLRGaAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPitmGVLVK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1005564688 978 FYEELlpqMRAKGKCIIAITHD--------DQYFHLADKLIVME 1013
Cdd:PRK11831 185 LISEL---NSALGVTCVVVSHDvpevlsiaDHAYIVADKKIVAH 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
835-1012 |
6.86e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.02 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 835 PIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA---------------PEE-------LNQ--YY 890
Cdd:COG1129 270 DVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdairagiayvPEDrkgeglvLDLsiRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 891 SAILSDFHVFDRLYGINTEGMKAEIDHYLELLQ-----LSDKVGiedgrftttQLSTG--QKkrlALLVTYLEDRP-ILL 962
Cdd:COG1129 350 NITLASLDRLSRGGLLDRRRERALAEEYIKRLRiktpsPEQPVG---------NLSGGnqQK---VVLAKWLATDPkVLI 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005564688 963 FDEwaadqdP------GYRRFFYeELLPQMRAKGKCIIAITHD-DQYFHLADKLIVM 1012
Cdd:COG1129 418 LDE------PtrgidvGAKAEIY-RLIRELAAEGKAVIVISSElPELLGLSDRILVM 467
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
836-885 |
1.12e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.86 E-value: 1.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGL--YEPNEGNVLLNGK---EIAPEE 885
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKdllELSPED 74
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
467-783 |
1.13e-05 |
|
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: 48.32 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 467 VVLAIYAIAGVGLAYVIHTFLNLcFPRQKGKSLLTLIVLGLIsgfgnafLIFVInetfvrsnnlenGLLFYFVLGIVMYV 546
Cdd:cd07346 6 LLLLLATALGLALPLLTKLLIDD-VIPAGDLSLLLWIALLLL-------LLALL------------RALLSYLRRYLAAR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 547 FSQRIIrtsivsytnelvYEKRMELTDKLLQTPYYKLELIEKGRIEATLNNDTEVISRSL-NLLVTAGTSLLTLLFCFLY 625
Cdd:cd07346 66 LGQRVV------------FDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVsSGLLQLLSDVLTLIGALVI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 626 LGVMNMYAFLLSLCIIFITAGVYSLIGRQADKVWnetRDIQNVYFRLIGDLRH---GFKELRLHTGKRNDFREVMNEScN 702
Cdd:cd07346 134 LFYLNWKLTLVALLLLPLYVLILRYFRRRIRKAS---REVRESLAELSAFLQEslsGIRVVKAFAAEEREIERFREAN-R 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 703 NYRVKRTIGDIKFANVFVLGELLFIFVIgIVVFVFPEIFVNMPKETISNYVIVFLY---MTGPVNEILGGIPQLVNVRIS 779
Cdd:cd07346 210 DLRDANLRAARLSALFSPLIGLLTALGT-ALVLLYGGYLVLQGSLTIGELVAFLAYlgmLFGPIQRLANLYNQLQQALAS 288
|
....
gi 1005564688 780 WQRI 783
Cdd:cd07346 289 LERI 292
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
843-1023 |
1.48e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 49.24 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 843 GEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAP--EELNQ------YYSAI------LSDFHVFDRLYGINT 908
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTniSDVHQnmgycpQFDAIddlltgREHLYLYARLRGVPA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 909 EGMKAEIDHYLELLQLSdkvgIEDGRFTTTqLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRa 988
Cdd:TIGR01257 2045 EEIEKVANWSIQSLGLS----LYADRLAGT-YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR- 2118
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1005564688 989 KGKCIIAITHD-DQYFHLADKLIVME------MGTVKMNKTK 1023
Cdd:TIGR01257 2119 EGRAVVLTSHSmEECEALCTRLAIMVkgafqcLGTIQHLKSK 2160
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
836-1015 |
1.62e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.14 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQYYSAILSDFHVFDRLYG--INTEGMKA 913
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDeyRYTSVIKA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 914 -EIDHYLELLQLSDKVGIEDGRFTttqLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEELLPQMRAKgKC 992
Cdd:TIGR01271 525 cQLEEDIALFPEKDKTVLGEGGIT---LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSN-KT 600
|
170 180
....*....|....*....|...
gi 1005564688 993 IIAITHDDQYFHLADKLIVMEMG 1015
Cdd:TIGR01271 601 RILVTSKLEHLKKADKILLLHEG 623
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
836-1026 |
2.62e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 46.80 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPEELNQYYS---AILSD-FHVFDRLY---GINT 908
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMReavAIVPEgRRVFSRMTveeNLAM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 909 EGMKAEIDHYLE----LLQLSDKVGIEDGRFTTTqLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYeELLP 984
Cdd:PRK11614 104 GGFFAERDQFQErikwVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIF-DTIE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1005564688 985 QMRAKGKCIIAITHD-DQYFHLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:PRK11614 182 QLREQGMTIFLVEQNaNQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
836-1017 |
3.22e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 47.53 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA--------------PEElnqyySAILSDFHV-- 899
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalsaraasrrvasvPQD-----TSLSFEFDVrq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 900 ------------FDRLyginTEGMKAEIDHYLE---LLQLSDKvgiedgrfTTTQLSTGQKKRLALLVTYLEDRPILLFD 964
Cdd:PRK09536 97 vvemgrtphrsrFDTW----TETDRAAVERAMErtgVAQFADR--------PVTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005564688 965 EWAADQDPgYRRFFYEELLPQMRAKGKCIIAITHDdqyFHLA----DKLIVMEMGTV 1017
Cdd:PRK09536 165 EPTASLDI-NHQVRTLELVRRLVDDGKTAVAAIHD---LDLAarycDELVLLADGRV 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
835-882 |
4.11e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 46.32 E-value: 4.11e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1005564688 835 PIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA 882
Cdd:PRK10575 29 PLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE 76
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
836-882 |
5.72e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 46.22 E-value: 5.72e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA 882
Cdd:PRK10419 31 VSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLA 77
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
463-653 |
5.81e-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: 46.26 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 463 APSTVVLAIYAIAGVGLAYVIHTFLNLCFpRQKGKSLLTLIVLGLISGFgnaflifvinetFVRSnnlenglLFYFVLGI 542
Cdd:cd18552 2 ALAILGMILVAATTAALAWLLKPLLDDIF-VEKDLEALLLVPLAIIGLF------------LLRG-------LASYLQTY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 543 VMYVFSQRIIRtsivsytnELvyekRMELTDKLLQTP--YYKLEliEKGRIEATLNNDTEVISRSL-NLLVTAGTSLLTL 619
Cdd:cd18552 62 LMAYVGQRVVR--------DL----RNDLFDKLLRLPlsFFDRN--SSGDLISRITNDVNQVQNALtSALTVLVRDPLTV 127
|
170 180 190
....*....|....*....|....*....|....
gi 1005564688 620 LFCFLYLGVMNMYAFLLSLCIIFITAGVYSLIGR 653
Cdd:cd18552 128 IGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGK 161
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
812-972 |
6.19e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 45.65 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGdftgfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA--------- 882
Cdd:PRK10895 4 LTAKNLAKAYKGRRV------VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplharar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 883 ------PEElnqyySAILSDFHVFDRLYGI-------NTEGMKAEIDHYLE---LLQLSDKVGiedgrfttTQLSTGQKK 946
Cdd:PRK10895 78 rgigylPQE-----ASIFRRLSVYDNLMAVlqirddlSAEQREDRANELMEefhIEHLRDSMG--------QSLSGGERR 144
|
170 180
....*....|....*....|....*.
gi 1005564688 947 RLALLVTYLEDRPILLFDEWAADQDP 972
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVDP 170
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
842-999 |
6.39e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.82 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 842 SGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNG------KEIAPEELNQYYSAILSDF------------------ 897
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdeilDEFRGSELQNYFTKLLEGDvkvivkpqyvdlipkavk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 898 -HVFDRLYGINTEGMKAEIDHYLELLQLSDKvgiedgrfTTTQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGyRR 976
Cdd:cd03236 105 gKVGELLKKKDERGKLDELVDQLELRHVLDR--------NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK-QR 175
|
170 180
....*....|....*....|...
gi 1005564688 977 FFYEELLPQMRAKGKCIIAITHD 999
Cdd:cd03236 176 LNAARLIRELAEDDNYVLVVEHD 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
836-1011 |
6.65e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI----APEELNQYYSAILSDFH------VFDRLY- 904
Cdd:PRK11288 23 ISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAALAAGVAIIYQELHlvpemtVAENLYl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 905 G--------INTEGMKAEIDHYLEllqlsdKVGIE-DGRFTTTQLSTGQKKRLALLVTYLEDRPILLFDE-----WAADQ 970
Cdd:PRK11288 103 GqlphkggiVNRRLLNYEAREQLE------HLGVDiDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEptsslSAREI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1005564688 971 DPGYRrffyeeLLPQMRAKGKCIIAITHD-DQYFHLADKLIV 1011
Cdd:PRK11288 177 EQLFR------VIRELRAEGRVILYVSHRmEEIFALCDAITV 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
836-881 |
6.75e-05 |
|
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: 46.74 E-value: 6.75e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYePN---EGNVLLNGKEI 881
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPL 67
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
806-883 |
1.26e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 806 LDVP---ICLQLQNVSykyknkdgdftGFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA 882
Cdd:PRK10762 249 LDKApgeVRLKVDNLS-----------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV 317
|
.
gi 1005564688 883 P 883
Cdd:PRK10762 318 T 318
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
837-999 |
1.39e-04 |
|
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: 45.70 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 837 DMEFN--SGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLnGKEIAPEELNQYYSAILSDFHVFDrlygintegmkaE 914
Cdd:TIGR03719 340 DLSFKlpPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDALDPNKTVWE------------E 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 915 IDHYLELLQLSdKVGIED----GRFTTT---------QLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRRFFYEE 981
Cdd:TIGR03719 407 ISGGLDIIKLG-KREIPSrayvGRFNFKgsdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEA 485
|
170
....*....|....*...
gi 1005564688 982 LLpqmrAKGKCIIAITHD 999
Cdd:TIGR03719 486 LL----NFAGCAVVISHD 499
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
842-1000 |
1.45e-04 |
|
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: 43.13 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 842 SGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLngkeIAPEELNQYYSAILSDFHVFDRLYgintegmkaeidhylel 921
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----IDGEDILEEVLDQLLLIIVGGKKA----------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 922 lqlsdkvgiedgrftttQLSTGQKKRLALLVTYLEDRPILLFDEWAADQDPGYRR-----FFYEELLPQMRAKGKCIIAI 996
Cdd:smart00382 60 -----------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAlllllEELRLLLLLKSEKNLTVILT 122
|
....
gi 1005564688 997 THDD 1000
Cdd:smart00382 123 TNDE 126
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
498-653 |
1.62e-04 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 44.56 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 498 SLLTLIVLGLISGFGNAFLIFVINETFVRSNNLENGLLFYFVLGIVMYVFSQR--IIRTSIVSYTNELVYEK-RMELTDK 574
Cdd:pfam00664 4 AILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFIlsFLQSYLLNHTGERLSRRlRRKLFKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 575 LLQTPYYKLELIEKGRIEATLNNDTEVISRSLNL-LVTAGTSLLTLLFCFLYLGVMNMYAFLLSLCIIFITAGVYSLIGR 653
Cdd:pfam00664 84 ILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEkLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAK 163
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
836-1012 |
2.27e-04 |
|
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: 43.08 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLskLITGLYEPNEgnvllngkeiapeelnqyySAILSDFHVFDRLYGINTEGMKAEI 915
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGK-------------------ARLISFLPKFSRNKLIFIDQLQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 916 DHYLELLQLsdkvgiedGRFTTTqLSTGQKKRLAlLVTYLEDRP---ILLFDEWAADQDPGYRRFFYEElLPQMRAKGKC 992
Cdd:cd03238 73 DVGLGYLTL--------GQKLST-LSGGELQRVK-LASELFSEPpgtLFILDEPSTGLHQQDINQLLEV-IKGLIDLGNT 141
|
170 180
....*....|....*....|
gi 1005564688 993 IIAITHDDQYFHLADKLIVM 1012
Cdd:cd03238 142 VILIEHNLDVLSSADWIIDF 161
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
812-888 |
2.83e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.33 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKDGDFTGfgIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPN---EGNVLLNGKEIA--PE-E 885
Cdd:PRK09473 13 LDVKDLRVTFSTPDGDVTA--VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILnlPEkE 90
|
...
gi 1005564688 886 LNQ 888
Cdd:PRK09473 91 LNK 93
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
836-881 |
2.85e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 2.85e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1005564688 836 IDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYePN---EGNVLLNGKEI 881
Cdd:PRK13549 24 VSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEEL 71
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
837-874 |
2.90e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 2.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1005564688 837 DMEFN--SGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNV 874
Cdd:PRK11819 342 DLSFSlpPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
850-881 |
2.95e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 2.95e-04
10 20 30
....*....|....*....|....*....|..
gi 1005564688 850 GGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI 881
Cdd:PRK10982 31 GENGAGKSTLLKCLFGIYQKDSGSILFQGKEI 62
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
839-882 |
3.46e-04 |
|
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: 42.56 E-value: 3.46e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1005564688 839 EFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA 882
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV 64
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
822-878 |
4.01e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 4.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005564688 822 KNKDGDFtgFGIGPIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNG 878
Cdd:PRK13546 31 KHKNKTF--FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
842-999 |
7.26e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 42.56 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 842 SGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEI-------------APEELNQYYSAILSDFHVFDRlYG--- 905
Cdd:PRK15056 32 GGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTrqalqknlvayvpQSEEVDWSFPVLVEDVVMMGR-YGhmg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 906 ---INTEGMKAEIDHYLEllqlsdKVGIEDGRFTTT-QLSTGQKKRLALLVTYLEDRPILLFDE--WAADQDPGYRRFfy 979
Cdd:PRK15056 111 wlrRAKKRDRQIVTAALA------RVDMVEFRHRQIgELSGGQKKRVFLARAIAQQGQVILLDEpfTGVDVKTEARII-- 182
|
170 180
....*....|....*....|
gi 1005564688 980 eELLPQMRAKGKCIIAITHD 999
Cdd:PRK15056 183 -SLLRELRDEGKTMLVSTHN 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
490-877 |
1.51e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 490 CFPRQKGKSLLTLIVLGLISGFGNAFLIFVINeTFVRSNNLE---NGLLFYFVL-GIVMYVFSQriirtsIVSYTNELVY 565
Cdd:PTZ00265 53 CLPASHRKLLGVSFVCATISGGTLPFFVSVFG-VIMKNMNLGenvNDIIFSLVLiGIFQFILSF------ISSFCMDVVT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 566 EKRME-LTDKLLQTPYYKLELIEKGRIEATLNNDTEVISRSLNLLVtaGTSLLTLL-----FCFLYLGVMNMYAfLLSLC 639
Cdd:PTZ00265 126 TKILKtLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGI--GTKFITIFtyasaFLGLYIWSLFKNA-RLTLC 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 640 IIFITAGVY--SLIGRQADKVWNETRDI-QNVYFRLIGDLRHGFKELRLHTGKRNDFREV-MNESC-NNYRVKRTIGD-- 712
Cdd:PTZ00265 203 ITCVFPLIYicGVICNKKVKINKKTSLLyNNNTMSIIEEALVGIRTVVSYCGEKTILKKFnLSEKLySKYILKANFMEsl 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 713 -IKFANVFVLGELLFIFVIGIVVFVfpeifvnmpkETISNYVIVFLYMTGPVNEILGGI-PQLVNVRISWQRIQQMVKSV 790
Cdd:PTZ00265 283 hIGMINGFILASYAFGFWYGTRIII----------SDLSNQQPNNDFHGGSVISILLGVlISMFMLTIILPNITEYMKSL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 791 DHIKANEQIATTK---------EYLDVPICLQLQNVSYKYKN-------KDGDFTgfgigpidmeFNSGEIVFIAGGNGS 854
Cdd:PTZ00265 353 EATNSLYEIINRKplvennddgKKLKDIKKIQFKNVRFHYDTrkdveiyKDLNFT----------LTEGKTYAFVGESGC 422
|
410 420
....*....|....*....|...
gi 1005564688 855 GKSTLSKLITGLYEPNEGNVLLN 877
Cdd:PTZ00265 423 GKSTILKLIERLYDPTEGDIIIN 445
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
770-1027 |
2.16e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 770 IPQLVNVRISWQRIQQMvksvdhIKANEQIATtkeyLDVPICLQLQNVSYK--YKNKDGDFTGFGIGPIDMEFNSGEIVF 847
Cdd:PLN03130 578 ITQAVNANVSLKRLEEL------LLAEERVLL----PNPPLEPGLPAISIKngYFSWDSKAERPTLSNINLDVPVGSLVA 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 848 IAGGNGSGKSTLSKLITGLYEP-NEGNVLLNGKEIAPEELNQYYSAILSDfhvfDRLYGINTEGMK-------AEIDHYL 919
Cdd:PLN03130 648 IVGSTGEGKTSLISAMLGELPPrSDASVVIRGTVAYVPQVSWIFNATVRD----NILFGSPFDPERyeraidvTALQHDL 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 920 ELLQLSDKVGI-EDGrfttTQLSTGQKKRLALLVTYLEDRPILLFDE--WAADQDPGYRRF---FYEELlpqmraKGKCI 993
Cdd:PLN03130 724 DLLPGGDLTEIgERG----VNISGGQKQRVSMARAVYSNSDVYIFDDplSALDAHVGRQVFdkcIKDEL------RGKTR 793
|
250 260 270
....*....|....*....|....*....|....
gi 1005564688 994 IAITHDDQYFHLADKLIVMEMGTVKMNKTKEALS 1027
Cdd:PLN03130 794 VLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELS 827
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
812-1026 |
3.20e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 40.66 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 812 LQLQNVSYKYKNKdgdftgfgIGPI----DMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAP---E 884
Cdd:cd03288 20 IKIHDLCVRYENN--------LKPVlkhvKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlplH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 885 ELNQYYSAILSDFHVFDRLYGINTEGMKAEID----HYLELLQLSDKV----GIEDGRFTT--TQLSTGQKKRLALLVTY 954
Cdd:cd03288 92 TLRSRLSIILQDPILFSGSIRFNLDPECKCTDdrlwEALEIAQLKNMVkslpGGLDAVVTEggENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005564688 955 LEDRPILLFDEWAADQDpgyrrFFYEELLPQ--MRA-KGKCIIAITHDDQYFHLADKLIVMEMGTVKMNKTKEAL 1026
Cdd:cd03288 172 VRKSSILIMDEATASID-----MATENILQKvvMTAfADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENL 241
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
843-882 |
3.21e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 3.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1005564688 843 GEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIA 882
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT 69
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
807-886 |
6.21e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 39.52 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 807 DVPIcLQLQNVSYKYknkdgdftGFGIGPIDMEFN--SGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAPE 884
Cdd:PRK11701 3 DQPL-LSVRGLTKLY--------GPRKGCRDVSFDlyPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLR 73
|
..
gi 1005564688 885 EL 886
Cdd:PRK11701 74 DL 75
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
830-874 |
6.26e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 6.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1005564688 830 GFGIGPI----DMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNV 874
Cdd:PRK15064 328 GFDNGPLfknlNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
827-899 |
6.69e-03 |
|
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: 39.17 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 827 DFTGFgigpidmeFNSGEIVFIAGGNGSGKSTLSKLITGLYEPN---EGNVLLNGKEIApEELNQYYSAIL----SDFHV 899
Cdd:cd03233 25 DFSGV--------VKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYK-EFAEKYPGEIIyvseEDVHF 95
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
835-883 |
7.04e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 40.28 E-value: 7.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1005564688 835 PIDMEFNSGEIVFIAGGNGSGKSTLSKLITGLYEPNEGNVLLNGKEIAP 883
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI 319
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
832-998 |
7.25e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.99 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 832 GIGPIDMEFNSGEIVFIaGGNGSGKSTLSKLITGLYEPNEGNVL------LNGKEIAPE-----ELNQYYSAILSDFHV- 899
Cdd:COG3593 13 SIKDLSIELSDDLTVLV-GENNSGKSSILEALRLLLGPSSSRKFdeedfyLGDDPDLPEieielTFGSLLSRLLRLLLKe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005564688 900 ------------FDRLYGINTEGMKAEIDHYLEL--------LQLSD----------KVGIEDG-RFTTTQLSTGQKKR- 947
Cdd:COG3593 92 edkeeleealeeLNEELKEALKALNELLSEYLKElldgldleLELSLdeledllkslSLRIEDGkELPLDRLGSGFQRLi 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005564688 948 -LALLVTYLE-----DRPILLFDEWAADQDPGYRRFFYEELLPQMRAKGKCIIAiTH 998
Cdd:COG3593 172 lLALLSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIIT-TH 227
|
|
| |
