|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
41-642 |
0e+00 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 652.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 41 ITEAQRFSHLPKRSAVNIEfIDLSYSVREGSWWRKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETGM 120
Cdd:TIGR00955 1 LTYSWRNSDVFGRVAQDGS-WKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 121 KGQ--ILVNGRPRDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEK--QEVKKELVNEILTALGLLECSYTRT- 195
Cdd:TIGR00955 80 KGSgsVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRvtKKEKRERVDEVLQALGLRKCANTRIg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 196 -----ISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSAKLFEMFDKLYI 270
Cdd:TIGR00955 160 vpgrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 271 LSQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASGEYGDLNPVlfRAVQNGMC-----------TMAEKKSSP 339
Cdd:TIGR00955 240 MAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGSENES--RERIEKICdsfavsdigrdMLVNTNLWS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 340 DKADSscpahCVTDVDHIESHTFATNTSTQFCILFKRTFICILRDTVLTHLRFMSHICIGVLIGLLYLHIGNDAGKVFNN 419
Cdd:TIGR00955 318 GKAGG-----LVKDSENMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 420 TGFLFFSMLFLMFAALMPTILTFPQEMSVFLREHLNYWYSLKAYYLAKTMADVPFQVICPIAYCSIVYWMTGQPPEATRF 499
Cdd:TIGR00955 393 NGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHF 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 500 LLFSALATATALVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYVSYVRYGFEGVILTIY 579
Cdd:TIGR00955 473 LTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQW 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024481026 580 AmEREDLECL----EDFCPFQKPIkILQELDVEEAKLYLDFLILGIFFIILRLLAYLVLRYKVKSER 642
Cdd:TIGR00955 553 S-DVDNIECTsantTGPCPSSGEV-ILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
55-280 |
2.28e-97 |
|
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: 296.38 E-value: 2.28e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 55 AVNIEFIDLSYSVRegsWWRKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRET-GMKGQILVNGRPRDL 133
Cdd:cd03213 1 GVTLSFRNLTVTVK---SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlGVSGEVLINGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 134 RTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKlsekqevkkelvneiltalgllecsytrtiSLSGGQRKRLAIALELV 213
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR------------------------------GLSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024481026 214 NNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 280
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
79-635 |
2.42e-83 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 275.22 E-value: 2.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 79 KTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETGMKGQILVNGRPRDLRTFRKMScYIMQDDMLLPHLTVLE 157
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFTGTILANNRKPTKQILKRTG-FVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 158 AMMVSANLKL--SEKQEVKKELVNEILTALGLLEC-------SYTRTISlsGGQRKRLAIALELVNNPPVMFFDEPTSGL 228
Cdd:PLN03211 160 TLVFCSLLRLpkSLTKQEKILVAESVISELGLTKCentiignSFIRGIS--GGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 229 DSASCFQVVSLMRSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADFIIE 308
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLD 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 309 VASGeYGDLNPVLFRA---VQNGMCTMAEKKSSPDKADSSCPAHCVTDVDH-IESHTFATNTS----------TQFCILF 374
Cdd:PLN03211 318 LANG-VCQTDGVSEREkpnVKQSLVASYNTLLAPKVKAAIEMSHFPQANARfVGSASTKEHRSsdrisistwfNQFSILL 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 375 KRTfICILRDTVLTHLRFMSHICIGVLIGLLYLHigNDAGKVFNNTGFLFFSMLFLMFAALMPTILTFPQEMSVFLREHL 454
Cdd:PLN03211 397 QRS-LKERKHESFNTLRVFQVIAAALLAGLMWWH--SDFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERA 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 455 NYWYSLKAYYLAKTMADVPFQVICPIAYCSIVYWMTGQPPEATRFLLFSALATATALVAQSLGLLIGAASTSLQVATFVG 534
Cdd:PLN03211 474 SGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIV 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 535 PVTAIPVLLFSGFFVSfkTIPTYLQWSSYVSYVRYGFEGVILTIYAMERED---LECLEDFCPFQKPIKILQELDVEEAK 611
Cdd:PLN03211 554 TVTMLAFVLTGGFYVH--KLPSCMAWIKYISTTFYSYRLLINVQYGEGKRIsslLGCSLPHGSDRASCKFVEEDVAGQIS 631
|
570 580
....*....|....*....|....
gi 2024481026 612 LYLDFLILGIFFIILRLLAYLVLR 635
Cdd:PLN03211 632 PATSVSVLIFMFVGYRLLAYLALR 655
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
53-580 |
2.92e-69 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 245.40 E-value: 2.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 53 RSAVNIEFIDLSYSVREGSWWR--------KRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETGM--KG 122
Cdd:TIGR00956 742 SDDVNDEKDMEKESGEDIFHWRnltyevkiKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitGG 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 123 QILVNGRPRDlRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEK--QEVKKELVNEILTALGLLecSYTRTI---- 196
Cdd:TIGR00956 822 DRLVNGRPLD-SSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSvsKSEKMEYVEEVIKLLEME--SYADAVvgvp 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 197 --SLSGGQRKRLAIALELVNNPP-VMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQ 273
Cdd:TIGR00956 899 geGLNVEQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQK 978
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 274 G-QCIFKGVV----TNLIPYLKGLGLH-CPTYHNPADFIIEVASGEYGD----------LNPVLFRAVQNGMCTM-AEKK 336
Cdd:TIGR00956 979 GgQTVYFGDLgensHTIINYFEKHGAPkCPEDANPAEWMLEVIGAAPGAhanqdyhevwRNSSEYQAVKNELDRLeAELS 1058
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 337 SSPDKADSSCPahcvtdvdhiesHTFATNTSTQFCILFKRTFICILRDTVLTHLRFMSHICIGVLIGLLYLHIGNDAGKV 416
Cdd:TIGR00956 1059 KAEDDNDPDAL------------SKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGTSLQGL 1126
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 417 FNNTGFLFfsMLFLMFAALMPTIL-TF-PQEMSVFLREHLNYWYSLKAYYLAKTMADVPFQVIC-PIAYCSIvYWMTGQP 493
Cdd:TIGR00956 1127 QNQMFAVF--MATVLFNPLIQQYLpPFvAQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAgTIFFFIW-YYPVGFY 1203
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 494 PEAT-------RFLLFSALATATALVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYVSY 566
Cdd:TIGR00956 1204 WNASktgqvheRGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSP 1283
|
570
....*....|....
gi 2024481026 567 VRYGFEGVILTIYA 580
Cdd:TIGR00956 1284 FTYLVQALLSTGLA 1297
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
68-280 |
1.18e-61 |
|
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: 204.43 E-value: 1.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 68 REGSWWR-------KRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETGMK-GQILVNGRPRDLRTFRK 138
Cdd:cd03234 2 RVLPWWDvglkaknWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGTTsGQILFNGQPRKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 139 MSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQ---EVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNN 215
Cdd:cd03234 82 CVAYVRQDDILLPGLTVRETLTYTAILRLPRKSsdaIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 216 PPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 280
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
58-280 |
2.92e-57 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 191.69 E-value: 2.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREgswwrKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETG-MKGQILVNGRPRDlRTF 136
Cdd:cd03232 4 LTWKNLNYTVPV-----KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvITGEILINGRPLD-KNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 137 RKMSCYIMQDDMLLPHLTVLEAMMVSANLklsekqevkkelvneiltalgllecsytRTISLSggQRKRLAIALELVNNP 216
Cdd:cd03232 78 QRSTGYVEQQDVHSPNLTVREALRFSALL----------------------------RGLSVE--QRKRLTIGVELAAKP 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 217 PVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQ-GQCIFKG 280
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
81-579 |
1.51e-55 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 204.69 E-value: 1.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 81 LLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGyRETG--MKGQILVNGRPRDLRTFRKMSCYIMQDDMLLPHLTVLEA 158
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG-RKTGgyIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 159 MMVSANLKLSekQEVKKE----LVNEILTalgLLECSYTR--------TISLSGGQRKRLAIALELVNNPPVMFFDEPTS 226
Cdd:PLN03140 974 LIYSAFLRLP--KEVSKEekmmFVDEVME---LVELDNLKdaivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 227 GLDSASCFQVVSLMRSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQ-GQCIFKGVV----TNLIPYLKGL-GL-HCPTY 299
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLgrnsHKIIEYFEAIpGVpKIKEK 1128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 300 HNPADFIIEVASgeygdlnpvLFRAVQNGMCTMAEKKSSP----DKA---DSSCPAHCVTDVdhieshTFATNTSTQFCI 372
Cdd:PLN03140 1129 YNPATWMLEVSS---------LAAEVKLGIDFAEHYKSSSlyqrNKAlvkELSTPPPGASDL------YFATQYSQSTWG 1193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 373 LFK----RTFICILRDTVLTHLRFMSHICIGVLIGLLYLHIG---NDAGKVFNNTGFLFFSMLFLMF---AALMPTILTf 442
Cdd:PLN03140 1194 QFKsclwKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGtkrSNANDLTMVIGAMYAAVLFVGInncSTVQPMVAV- 1272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 443 pqEMSVFLREHLNYWYSLKAYYLAKTMADVPFQVICPIAYCSIVYWMTGQPPEATRFLLFSALATATALVAQSLGLLIGA 522
Cdd:PLN03140 1273 --ERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVS 1350
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024481026 523 ASTSLQVAT-FVGPVTAIpVLLFSGFFVSFKTIPTYLQWSSYVSYVRYGFEGVILTIY 579
Cdd:PLN03140 1351 LTPNQQVAAiFAAAFYGL-FNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQY 1407
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
74-588 |
1.26e-53 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 198.79 E-value: 1.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 74 RKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRE---TGMKGQILVNGRPRD--LRTFRKMSCYIMQDDM 148
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhIGVEGVITYDGITPEeiKKHYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 149 LLPHLTVLEAMMVSANLK-------LSEKQEVKKELVNEILTALGLLECSYT-------RTISlsGGQRKRLAIALELVN 214
Cdd:TIGR00956 149 HFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKHIADVYMATYGLSHTRNTkvgndfvRGVS--GGERKRVSIAEASLG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 215 NPPVMFFDEPTSGLDSASCFQVVSLMRSLAQ-GGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLG 293
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 294 LHCPTYHNPADFIIEVASGEY-----GDLNPV---------LFRAVQNGMCTMAEKkSSPDKADSSCPAHCVTDVDHIES 359
Cdd:TIGR00956 307 FKCPDRQTTADFLTSLTSPAErqikpGYEKKVprtpqefetYWRNSPEYAQLMKEI-DEYLDRCSESDTKEAYRESHVAK 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 360 HTFATNTST--------QFCILFKRTFICILRDTVLTHLRFMSHICIGVLIGLLYLHIGNDAGKVFNNTGFLFFSMLFLM 431
Cdd:TIGR00956 386 QSKRTRPSSpytvsfsmQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAILFNA 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 432 FAALMPTILTFpqEMSVFLREHLNY-WYSLKAYYLAKTMADVPFQVICPIAYCSIVYWMTGQPPEATRFLLFSALATATA 510
Cdd:TIGR00956 466 FSSLLEIASMY--EARPIVEKHRKYaLYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICT 543
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024481026 511 LVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYVSYVRYGFEGviLTIYAMEREDLEC 588
Cdd:TIGR00956 544 LAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFES--LMVNEFHGRRFEC 619
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
373-575 |
8.27e-50 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 172.07 E-value: 8.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 373 LFKRTFICILRDTVLTHLRFMSHICIGVLIGLLYLHIGNDAGkVFNNTGFLFFSMLFLMFAALMPTILTFPQEMSVFLRE 452
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQG-GLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 453 HLNYWYSLKAYYLAKTMADVPFQVICPIAYCSIVYWMTGQPPEATRFLLFSALATATALVAQSLGLLIGAASTSLQVATF 532
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2024481026 533 VGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYVSYVRYGFEGVI 575
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALR 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
93-286 |
1.25e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.07 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRP--RDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK-LS 168
Cdd:COG1131 27 EIFGLLGPNGAGKTTTIRMLLGlLRPTS--GEVRVLGEDvaRDPAEVRRRIGYVPQEPALYPDLTVRENLRFFARLYgLP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 169 EKQevKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGR 248
Cdd:COG1131 105 RKE--ARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGK 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024481026 249 TIICTIHQPSAkLFEMFDKLYILSQGQCIFKGVVTNLI 286
Cdd:COG1131 183 TVLLSTHYLEE-AERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
59-275 |
5.82e-43 |
|
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: 153.78 E-value: 5.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 59 EFIDLSYSvregswwRKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRP---RDLRT 135
Cdd:cd03225 1 ELKNLSFS-------YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-TSGEVLVDGKDltkLSLKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 136 FRKMSCYIMQ--DDMLLpHLTVLEAMMVSA-NLKLSEKQEVKKelVNEILTALGLLECSYTRTISLSGGQRKRLAIALEL 212
Cdd:cd03225 73 LRRKVGLVFQnpDDQFF-GPTVEEEVAFGLeNLGLPEEEIEER--VEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024481026 213 VNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSaKLFEMFDKLYILSQGQ 275
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
58-280 |
4.54e-42 |
|
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: 151.72 E-value: 4.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGswwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGRP---RDL 133
Cdd:COG1122 1 IELENLSFSYPGG--------TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGlLKPT--SGEVLVDGKDitkKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 134 RTFRKMSCYIMQ--DDMLLpHLTVLEAMMVS-ANLKLSEKqEVKkELVNEILTALGLLECSYTRTISLSGGQRKRLAIAL 210
Cdd:COG1122 71 RELRRKVGLVFQnpDDQLF-APTVEEDVAFGpENLGLPRE-EIR-ERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 211 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 280
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADG 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
58-275 |
2.73e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 146.73 E-value: 2.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSwwrkrGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGyRETGMKGQILVNGRP------R 131
Cdd:COG1136 5 LELRNLTKSYGTGE-----GEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG-LDRPTSGEVLIDGQDisslseR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 132 DLRTFRKMSC-YIMQDDMLLPHLTVLEAMMVSANLKlSEKQEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIAL 210
Cdd:COG1136 79 ELARLRRRHIgFVFQFFNLLPELTALENVALPLLLA-GVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024481026 211 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLA-QGGRTIICTIHqpSAKLFEMFDKLYILSQGQ 275
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTH--DPELAARADRVIRLRDGR 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
93-275 |
1.89e-38 |
|
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: 141.47 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGyRETGMKGQILVNGRP------RDLRTFR--KMScYIMQDDMLLPHLTVLEAMMVSAN 164
Cdd:cd03255 31 EFVAIVGPSGSGKSTLLNILGG-LDRPTSGEVRVDGTDisklseKELAAFRrrHIG-FVFQSFNLLPDLTALENVELPLL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 165 LKLSEKQEvKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLA 244
Cdd:cd03255 109 LAGVPKKE-RRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELN 187
|
170 180 190
....*....|....*....|....*....|..
gi 2024481026 245 -QGGRTIICTIHQPSakLFEMFDKLYILSQGQ 275
Cdd:cd03255 188 kEAGTTIVVVTHDPE--LAEYADRIIELRDGK 217
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
75-574 |
5.45e-38 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 151.54 E-value: 5.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 75 KRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETGMK--GQILVNGRPRDLRTFRKMSCYIMQDDMLLPH 152
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKvsGEITYNGYRLNEFVPRKTSAYISQNDVHVGV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 153 LTVLEAMMVSAN--------------------------------LKLSEKQEVKKELVNE-ILTALGLLECSYT------ 193
Cdd:PLN03140 254 MTVKETLDFSARcqgvgtrydllselarrekdagifpeaevdlfMKATAMEGVKSSLITDyTLKILGLDICKDTivgdem 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 194 -RTISlsGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQ-GGRTIICTIHQPSAKLFEMFDKLYIL 271
Cdd:PLN03140 334 iRGIS--GGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFDDIILL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 272 SQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASGE-----YGDLN------PV-----LFRAVQNGMcTMAEK 335
Cdd:PLN03140 412 SEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKdqeqyWADRNkpyryiSVsefaeRFKSFHVGM-QLENE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 336 KSSPDKADSSCPAHCVTDvdhieshTFATNTSTQFCILFKRTFICILRDTVLTHLRFMSHICIGVLIGLLYL----HIGN 411
Cdd:PLN03140 491 LSVPFDKSQSHKAALVFS-------KYSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLrtemHTRN 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 412 DA-GKVFnnTGFLFFSMLFLMFAALMPTILTFpQEMSVFLRE-----HLNYWYSLKAYYLAktmadVPFQVICPIAYCSI 485
Cdd:PLN03140 564 EEdGALY--IGALLFSMIINMFNGFAELALMI-QRLPVFYKQrdllfHPPWTFTLPTFLLG-----IPISIIESVVWVVI 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 486 VYWMTGQPPEATRFLLFSALATATALVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYVS 565
Cdd:PLN03140 636 TYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVS 715
|
....*....
gi 2024481026 566 YVRYGFEGV 574
Cdd:PLN03140 716 PLSYGFNAL 724
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
75-277 |
2.51e-37 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 138.41 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 75 KRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGyrETGM-KGQILVNGRP--RDLRTFRKMSCYIMQDDMLLP 151
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTG--ELRPtSGTAYINGYSirTDRKAARQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 152 HLTVLEAMMVSANLK-LSEKQEvkKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 230
Cdd:cd03263 89 ELTVREHLRFYARLKgLPKSEI--KEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024481026 231 ASCFQVVSLMRSLaQGGRTIICTIHqpSAKLFEMF-DKLYILSQGQ--CI 277
Cdd:cd03263 167 ASRRAIWDLILEV-RKGRSIILTTH--SMDEAEALcDRIAIMSDGKlrCI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
58-280 |
3.61e-37 |
|
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: 138.40 E-value: 3.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSvregswwrkRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGRPR----- 131
Cdd:cd03261 1 IELRGLTKS---------FGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGlLRPD--SGEVLIDGEDIsglse 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 132 -DLRTFRKMSCYIMQDDMLLPHLTVLE--AMMVSANLKLSEkqEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAI 208
Cdd:cd03261 70 aELYRLRRRMGMLFQSGALFDSLTVFEnvAFPLREHTRLSE--EEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024481026 209 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL--AQGGRTIICTiHQPSAkLFEMFDKLYILSQGQCIFKG 280
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVT-HDLDT-AFAIADRIAVLYDGKIVAEG 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
93-282 |
1.90e-36 |
|
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: 136.53 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP--RDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEK 170
Cdd:COG4555 28 EITGLLGPNGAGKTTLLRMLAGL-LKPDSGSILIDGEDvrKEPREARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 171 QEVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTI 250
Cdd:COG4555 107 EELKKR-IEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTV 185
|
170 180 190
....*....|....*....|....*....|....
gi 2024481026 251 ICTIHQPS--AKLfemFDKLYILSQGQCIFKGVV 282
Cdd:COG4555 186 LFSSHIMQevEAL---CDRVVILHKGKVVAQGSL 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
77-280 |
3.85e-36 |
|
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: 135.77 E-value: 3.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 77 GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNG------RPRDLRTFRKMSCYIMQDDMLL 150
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL-VEPTSGSVLIDGtdinklKGKALRQLRRQIGMIFQQFNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 151 PHLTVLEAMMV---------SANLKLSEKQEVKKELvnEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFF 221
Cdd:cd03256 91 ERLSVLENVLSgrlgrrstwRSLFGLFPKEEKQRAL--AALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024481026 222 DEPTSGLDSASCFQVVSLMRSLAQG-GRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG 280
Cdd:cd03256 169 DEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDlAREY--ADRIVGLKDGRIVFDG 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
82-226 |
8.15e-35 |
|
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: 128.92 E-value: 8.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 82 LKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGyRETGMKGQILVNGRP---RDLRTFRKMSCYIMQDDMLLPHLTVLEA 158
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG-LLSPTEGTILLDGQDltdDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024481026 159 MMVSANLKLSEKQEVKKElVNEILTALGLLECSYTR----TISLSGGQRKRLAIALELVNNPPVMFFDEPTS 226
Cdd:pfam00005 80 LRLGLLLKGLSKREKDAR-AEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
94-280 |
1.49e-34 |
|
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: 130.39 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 94 LIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRP--RDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQ 171
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPPS-SGTIRIDGQDvlKQPQKLRRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 172 EVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQgGRTII 251
Cdd:cd03264 106 EVKAR-VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVI 183
|
170 180
....*....|....*....|....*....
gi 2024481026 252 CTIHQPSaKLFEMFDKLYILSQGQCIFKG 280
Cdd:cd03264 184 LSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
79-275 |
1.38e-33 |
|
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: 126.36 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 79 KTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRE-TgmKGQILVNGRP--RDLRTFRKMSCYIMQDDMLLPHLTV 155
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpD--SGEIKVLGKDikKEPEEVKRRIGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 156 LEammvsaNLKLSekqevkkelvneiltalgllecsytrtislsGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 235
Cdd:cd03230 91 RE------NLKLS-------------------------------GGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2024481026 236 VVSLMRSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQ 275
Cdd:cd03230 134 FWELLRELKKEGKTILLSSHILEE-AERLCDRVAILNNGR 172
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
93-285 |
4.26e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 127.48 E-value: 4.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGyRETGMKGQILVNG------RPRDLRTFRKMSCYIMQDDMLLPHLTVLEAMMV----- 161
Cdd:COG3638 30 EFVALIGPSGAGKSTLLRCLNG-LVEPTSGEILVDGqdvtalRGRALRRLRRRIGMIFQQFNLVPRLSVLTNVLAgrlgr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 162 ----SANLKLSEKQEvkKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 237
Cdd:COG3638 109 tstwRSLLGLFPPED--RERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVM 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024481026 238 SLMRSLAQ-GGRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKGVVTNL 285
Cdd:COG3638 187 DLLRRIAReDGITVVVNLHQVDlARRY--ADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
74-280 |
5.38e-33 |
|
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: 125.84 E-value: 5.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 74 RKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRET--GMKGQILVNGRPRD--LRTFRKMSCYIMQDDML 149
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvSVEGDIHYNGIPYKefAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 150 LPHLTVLEAMMVSANLKLSEkqevkkelvneiltalgllecsYTRTISlsGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:cd03233 95 FPTLTVRETLDFALRCKGNE----------------------FVRGIS--GGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024481026 230 SASCFQVVSLMRSLAQG-GRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 280
Cdd:cd03233 151 SSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
73-275 |
9.83e-33 |
|
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: 124.22 E-value: 9.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 73 WRKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP-----RDLRTFRKMSCYIMQDD 147
Cdd:cd03229 7 SKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL-EEPDSGSILIDGEDltdleDELPPLRRRIGMVFQDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 148 MLLPHLTVLEammvsaNLklsekqevkkelvneiltalgllecsytrTISLSGGQRKRLAIALELVNNPPVMFFDEPTSG 227
Cdd:cd03229 86 ALFPHLTVLE------NI-----------------------------ALGLSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024481026 228 LDSASCFQVVSLMRSL-AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQ 275
Cdd:cd03229 131 LDPITRREVRALLKSLqAQLGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
58-275 |
1.05e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 124.93 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYsvregswwrKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRPR---DL 133
Cdd:COG4619 1 LELEGLSF---------RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADlDPPTS--GEIYLDGKPLsamPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 134 RTFRKMSCYIMQDdmllphlTVLEAMMVSANLKLS---EKQEVKKELVNEILTALGL----LEcsyTRTISLSGGQRKRL 206
Cdd:COG4619 70 PEWRRQVAYVPQE-------PALWGGTVRDNLPFPfqlRERKFDRERALELLERLGLppdiLD---KPVERLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 207 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL-AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQ 275
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDP-EQIERVADRVLTLEAGR 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
61-255 |
2.25e-32 |
|
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: 123.91 E-value: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 61 IDLSYSVREGSwwrkrgykTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGRPRDLRTFRKM 139
Cdd:cd03226 3 ENISFSYKKGT--------EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlIKES--SGSILLNGKPIKAKERRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 140 SCYIMQD-DMLLPHLTVLEAMMVSANLkLSEKQEVkkelVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPV 218
Cdd:cd03226 73 IGYVMQDvDYQLFTDSVREELLLGLKE-LDAGNEQ----AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 2024481026 219 MFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIH 255
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
93-281 |
4.25e-32 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 124.33 E-value: 4.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNG------RPRDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSA--- 163
Cdd:TIGR02315 29 EFVAIIGPSGAGKSTLLRCINRL-VEPSSGSILLEGtditklRGKKLRKLRRRIGMIFQHYNLIERLTVLENVLHGRlgy 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 164 ----NLKLSEKQEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 239
Cdd:TIGR02315 108 kptwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDY 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2024481026 240 MRSLAQG-GRTIICTIHQPS-AKLFEmfDKLYILSQGQCIFKGV 281
Cdd:TIGR02315 188 LKRINKEdGITVIINLHQVDlAKKYA--DRIVGLKAGEIVFDGA 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
76-257 |
4.45e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 123.36 E-value: 4.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 76 RGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGyRETGMKGQILVNGRP--RDLRTFRKMSCYIMQDDMLLPHL 153
Cdd:COG4133 12 RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG-LLPPSAGEVLWNGEPirDAREDYRRRLAYLGHADGLKPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 154 TVLEAMMVSANLKlseKQEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 233
Cdd:COG4133 91 TVRENLRFWAALY---GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180
....*....|....*....|....
gi 2024481026 234 FQVVSLMRSLAQGGRTIICTIHQP 257
Cdd:COG4133 168 ALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
58-276 |
1.60e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.89 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSvregswwrkRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRPRDLRtfR 137
Cdd:COG1121 7 IELENLTVS---------YGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-TSGTVRLFGKPPRRA--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 138 KMSCYIMQD---DMLLPhLTVLEAMM------VSANLKLSEKQevkKELVNEILTALGLLECSyTRTIS-LSGGQRKRLA 207
Cdd:COG1121 75 RRIGYVPQRaevDWDFP-ITVRDVVLmgrygrRGLFRRPSRAD---REAVDEALERVGLEDLA-DRPIGeLSGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024481026 208 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQC 276
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRGLV 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
58-283 |
3.55e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 122.07 E-value: 3.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREgswwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRP------R 131
Cdd:COG1120 2 LEAENLSVGYGG---------RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-SGEVLLDGRDlaslsrR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 132 DLRtfRKMScYIMQDDMLLPHLTVLEAMM------VSANLKLSEKQEvkkELVNEILTALGLLECSYTRTISLSGGQRKR 205
Cdd:COG1120 72 ELA--RRIA-YVPQEPPAPFGLTVRELVAlgryphLGLFGRPSAEDR---EAVEEALERTGLEHLADRPVDELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 206 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG-GRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG--- 280
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNlAARY--ADRLVLLKDGRIVAQGppe 223
|
....
gi 2024481026 281 -VVT 283
Cdd:COG1120 224 eVLT 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
93-256 |
4.38e-31 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 120.71 E-value: 4.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTL---MNILagyrETGMKGQILVNG-----RPRDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSAN 164
Cdd:cd03262 27 EVVVIIGPSGSGKSTLlrcINLL----EEPDSGTIIIDGlkltdDKKNINELRQKVGMVFQQFNLFPHLTVLENITLAPI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 165 --LKLSEKQEVKKELvnEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRS 242
Cdd:cd03262 103 kvKGMSKAEAEERAL--ELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKD 180
|
170
....*....|....
gi 2024481026 243 LAQGGRTIICTIHQ 256
Cdd:cd03262 181 LAEEGMTMVVVTHE 194
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
55-280 |
8.71e-31 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 120.62 E-value: 8.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 55 AVNiefiDLSYSVREGswwrkrgyktllkclsgkfcqrELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGR---- 129
Cdd:cd03219 15 ALD----DVSFSVRPG----------------------EIHGLIGPNGAGKTTLFNLISGfLRPT--SGSVLFDGEditg 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 130 --PRDL------RTFRKMScyimqddmLLPHLTVLEAMMVSANLKLSE---------KQEVKKELVNEILTALGLLECSY 192
Cdd:cd03219 67 lpPHEIarlgigRTFQIPR--------LFPELTVLENVMVAAQARTGSglllararrEEREARERAEELLERVGLADLAD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 193 TRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSAkLFEMFDKLYILS 272
Cdd:cd03219 139 RPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLD 217
|
....*...
gi 2024481026 273 QGQCIFKG 280
Cdd:cd03219 218 QGRVIAEG 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
73-275 |
1.90e-30 |
|
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: 116.96 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 73 WRKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGRP---RDLRTFRKMSCYIMQddm 148
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGlLKPT--SGEILIDGKDiakLPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 149 llphltvleammvsanlklsekqevkkelvneiltalgllecsytrtisLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 228
Cdd:cd00267 81 -------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2024481026 229 DSASCFQVVSLMRSLAQGGRTIICTIHQPS-AKLFemFDKLYILSQGQ 275
Cdd:cd00267 112 DPASRERLLELLRELAEEGRTVIIVTHDPElAELA--ADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
75-280 |
2.23e-30 |
|
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: 117.54 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 75 KRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRPRDLRTFRKMSCYImqddmllphLT 154
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-SGEILLDGKDLASLSPKELARKI---------AY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 155 VLEAMmvsanlklsekqevkkELVNeiltALGLLECSYTrtiSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 234
Cdd:cd03214 78 VPQAL----------------ELLG----LAHLADRPFN---ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2024481026 235 QVVSLMRSLA-QGGRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG 280
Cdd:cd03214 135 ELLELLRRLArERGKTVVMVLHDLNlAARY--ADRVILLKDGRIVAQG 180
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
43-275 |
4.19e-30 |
|
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: 126.10 E-value: 4.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 43 EAQRFSHLPKRSAvNIEFIDLSYSVREGSwwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmK 121
Cdd:COG2274 460 EGRSKLSLPRLKG-DIELENVSFRYPGDS-------PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGlYEPT--S 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 122 GQILVNGRPR---DLRTFRKMSCYIMQDDMLLpHLTVLEammvsaNLKLSeKQEVKKELVNEILTALGLLEcsYTRT--- 195
Cdd:COG2274 530 GRILIDGIDLrqiDPASLRRQIGVVLQDVFLF-SGTIRE------NITLG-DPDATDEEIIEAARLAGLHD--FIEAlpm 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 196 ----------ISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQgGRTIICTIHQPSakLFEMF 265
Cdd:COG2274 600 gydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS--TIRLA 676
|
250
....*....|
gi 2024481026 266 DKLYILSQGQ 275
Cdd:COG2274 677 DRIIVLDKGR 686
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
89-280 |
8.10e-30 |
|
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: 117.21 E-value: 8.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 89 FCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGR------PRDlrtfRKMScYIMQDDMLLPHLTVLE--AMM 160
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGF-ETPQSGRVLINGVdvtaapPAD----RPVS-MLFQENNLFAHLTVEQnvGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 161 VSANLKLSEKQevkKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 240
Cdd:cd03298 95 LSPGLKLTAED---RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024481026 241 RSL-AQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 280
Cdd:cd03298 172 LDLhAETKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
93-251 |
1.85e-29 |
|
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: 122.70 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRP------RDLRTFRKMSCYIMQD--DMLLPHLTVLEAMMVSA 163
Cdd:COG1123 292 ETLGLVGESGSGKSTLARLLLGlLRPTS--GSILFDGKDltklsrRSLRELRRRVQMVFQDpySSLNPRMTVGDIIAEPL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 164 -NLKLSEKQEVKkELVNEILTALGLLECSYTRTI-SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMR 241
Cdd:COG1123 370 rLHGLLSRAERR-ERVAELLERVGLPPDLADRYPhELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLR 448
|
170
....*....|.
gi 2024481026 242 SL-AQGGRTII 251
Cdd:COG1123 449 DLqRELGLTYL 459
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
58-275 |
2.92e-29 |
|
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: 114.02 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSwwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGRPR---DL 133
Cdd:cd03228 1 IEFKNVSFSYPGRP-------KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRlYDPT--SGEILIDGVDLrdlDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 134 RTFRKMSCYIMQDDMLLpHLTVLEammvsaNLklsekqevkkelvneiltalgllecsytrtisLSGGQRKRLAIALELV 213
Cdd:cd03228 72 ESLRKNIAYVPQDPFLF-SGTIRE------NI--------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024481026 214 NNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQgGRTIICTIHQPSakLFEMFDKLYILSQGQ 275
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLS--TIRDADRIIVLDDGR 171
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
58-280 |
3.04e-29 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 116.23 E-value: 3.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSvregswwrkRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGR------P 130
Cdd:COG1127 6 IEVRNLTKS---------FGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGlLRPD--SGEILVDGQditglsE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 131 RDLRTFR-KMScYIMQDDMLLPHLTVLE--AMMVSANLKLSEKQevKKELVNEILTALGLLECSYTRTISLSGGQRKRLA 207
Cdd:COG1127 75 KELYELRrRIG-MLFQGGALFDSLTVFEnvAFPLREHTDLSEAE--IRELVLEKLELVGLPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024481026 208 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL--AQGGRTIICTiHQ-PSAklFEMFDKLYILSQGQCIFKG 280
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVT-HDlDSA--FAIADRVAVLADGKIIAEG 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
93-284 |
3.38e-29 |
|
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: 115.65 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRPrdLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQ 171
Cdd:cd03293 31 EFVALVGPSGCGKSTLLRIIAGlERPTS--GEVLVDGEP--VTGPGPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 172 EvKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV-VSLMRSLAQGGRTI 250
Cdd:cd03293 107 E-ARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLqEELLDIWRETGKTV 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 2024481026 251 ICTIHQpsakLFE---MFDKLYILSQGQCIFKGVVTN 284
Cdd:cd03293 186 LLVTHD----IDEavfLADRVVVLSARPGRIVAEVEV 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
58-255 |
4.43e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.15 E-value: 4.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGswwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGR-----PR 131
Cdd:COG2884 2 IRFENVSKRYPGG--------REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPT--SGQVLVNGQdlsrlKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 132 D----LRtfRKMScYIMQDDMLLPHLTVLEammvsaNLKLS------EKQEVKKElVNEILTALGLLECSYTRTISLSGG 201
Cdd:COG2884 72 ReipyLR--RRIG-VVFQDFRLLPDRTVYE------NVALPlrvtgkSRKEIRRR-VREVLDLVGLSDKAKALPHELSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024481026 202 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIH 255
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH 195
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
58-277 |
6.50e-29 |
|
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: 114.91 E-value: 6.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSWWRKrgyktLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRP------R 131
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVK-----ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP-TSGSIIFDGKDllklsrR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 132 DLRTFRKMSCYIMQDDM--LLPHLTV----LEAMMVsanLKLSEKQEVKKELVNEILTALGLLECSYTRTIS-LSGGQRK 204
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMssLNPRMTIgeqiAEPLRI---HGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHeLSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024481026 205 RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCI 277
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGV-VAKIADRVAVMYAGKIV 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
93-275 |
6.95e-29 |
|
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: 114.54 E-value: 6.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP-RDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQ 171
Cdd:cd03259 27 EFLALLGPSGCGKTTLLRLIAGL-ERPDSGEILIDGRDvTGVPPERRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 172 EVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL-AQGGRTI 250
Cdd:cd03259 106 EIRAR-VRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELqRELGITT 184
|
170 180
....*....|....*....|....*.
gi 2024481026 251 ICTIHQPS-AklFEMFDKLYILSQGQ 275
Cdd:cd03259 185 IYVTHDQEeA--LALADRIAVMNEGR 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
50-286 |
9.47e-29 |
|
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: 121.02 E-value: 9.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 50 LPKRSAVNIEFIDLSYSVREGswwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYREtGMKGQILVNGR 129
Cdd:COG4988 329 LPAAGPPSIELEDVSFSYPGG--------RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP-PYSGSILINGV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 130 PR---DLRTFRKMSCYIMQDDmLLPHLTVLEammvsaNLKLSeKQEVKKELVNEILTALGLLEcsYTRTIS--------- 197
Cdd:COG4988 400 DLsdlDPASWRRQIAWVPQNP-YLFAGTIRE------NLRLG-RPDASDEELEAALEAAGLDE--FVAALPdgldtplge 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 198 ----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTiHQPSakLFEMFDKLYILSQ 273
Cdd:COG4988 470 ggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLA--LLAQADRILVLDD 546
|
250
....*....|...
gi 2024481026 274 GQCIFKGVVTNLI 286
Cdd:COG4988 547 GRIVEQGTHEELL 559
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
93-255 |
1.59e-28 |
|
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: 113.27 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGyRETGMKGQILVNGRP------RDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK 166
Cdd:cd03292 28 EFVFLVGPSGAGKSTLLKLIYK-EELPTSGTIRVNGQDvsdlrgRAIPYLRRKIGVVFQDFRLLPDRNVYENVAFALEVT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 167 LSEKQEVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG 246
Cdd:cd03292 107 GVPPREIRKR-VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKA 185
|
....*....
gi 2024481026 247 GRTIICTIH 255
Cdd:cd03292 186 GTTVVVATH 194
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
77-256 |
4.79e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.88 E-value: 4.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 77 GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLM---NILagyrETGMKGQILV-----NGRPRDLRTFRKMSCYIMQDDM 148
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKL----EEITSGDLIVdglkvNDPKVDERLIRQEAGMVFQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 149 LLPHLTVLEAMMVSANLKLSEKQEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 228
Cdd:PRK09493 88 LFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180
....*....|....*....|....*...
gi 2024481026 229 DSASCFQVVSLMRSLAQGGRTIICTIHQ 256
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
93-257 |
9.10e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 111.77 E-value: 9.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGrpRDLRTF----RKMScYIMQDDMLLPHLTVLE--AMMVSANLK 166
Cdd:COG3840 26 ERVAILGPSGAGKSTLLNLIAGF-LPPDSGRILWNG--QDLTALppaeRPVS-MLFQENNLFPHLTVAQniGLGLRPGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 167 LSEKQevkKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG 246
Cdd:COG3840 102 LTAEQ---RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRE 178
|
170
....*....|..
gi 2024481026 247 -GRTIICTIHQP 257
Cdd:COG3840 179 rGLTVLMVTHDP 190
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
82-255 |
1.29e-27 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 110.21 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 82 LKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGRP-----RDLRTFRKMSCYIMQD-DMLLPHLT 154
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGlLRPQ--SGAVLIDGEPldysrKGLLERRQRVGLVFQDpDDQLFAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 155 VLEAMMVSA-NLKLSEkQEVKkELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 233
Cdd:TIGR01166 86 VDQDVAFGPlNLGLSE-AEVE-RRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|..
gi 2024481026 234 FQVVSLMRSLAQGGRTIICTIH 255
Cdd:TIGR01166 164 EQMLAILRRLRAEGMTVVISTH 185
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
66-275 |
1.61e-27 |
|
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: 111.43 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 66 SVREGSWWRKRgykTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP---RDLRTFRKMSCY 142
Cdd:COG1124 8 SVSYGQGGRRV---PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGL-ERPWSGEVTFDGRPvtrRRRKAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 143 IMQDDM--LLPHLTVLEAmmVSANLKLSEKQEVKKElVNEILTALGLLECSYTRTI-SLSGGQRKRLAIALELVNNPPVM 219
Cdd:COG1124 84 VFQDPYasLHPRHTVDRI--LAEPLRIHGLPDREER-IAELLEQVGLPPSFLDRYPhQLSGGQRQRVAIARALILEPELL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024481026 220 FFDEPTSGLDSASCFQVVSLMRSL-AQGGRTIICTIHQPSAKLFeMFDKLYILSQGQ 275
Cdd:COG1124 161 LLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAH-LCDRVAVMQNGR 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
55-280 |
2.39e-27 |
|
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: 111.28 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 55 AVNiefiDLSYSVREGswwrkrgyktllkclsgkfcqrELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGR---- 129
Cdd:COG0411 19 AVD----DVSLEVERG----------------------EIVGLIGPNGAGKTTLFNLITGfYRPTS--GRILFDGRditg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 130 --PRDL------RTFrkmscyimQDDMLLPHLTVLEAMMVSA-------------NLKLSEKQEVK-KELVNEILTALGL 187
Cdd:COG0411 71 lpPHRIarlgiaRTF--------QNPRLFPELTVLENVLVAAharlgrgllaallRLPRARREEREaRERAEELLERVGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 188 LECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG-GRTIICTIHQPSAkLFEMFD 266
Cdd:COG0411 143 ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDL-VMGLAD 221
|
250
....*....|....
gi 2024481026 267 KLYILSQGQCIFKG 280
Cdd:COG0411 222 RIVVLDFGRVIAEG 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
59-274 |
4.13e-27 |
|
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: 109.16 E-value: 4.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 59 EFIDLSYSvregswwrkRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG----YRetgmkGQILVNGRPrdLR 134
Cdd:cd03235 1 EVEDLTVS---------YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGllkpTS-----GSIRVFGKP--LE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 135 TFRKMSCYIMQD---DMLLPhLTVLEAMM------VSANLKLSEKQevkKELVNEILTALGLLECSyTRTIS-LSGGQRK 204
Cdd:cd03235 65 KERKRIGYVPQRrsiDRDFP-ISVRDVVLmglyghKGLFRRLSKAD---KAKVDEALERVGLSELA-DRQIGeLSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 205 RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQG 274
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRT 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
90-280 |
4.91e-27 |
|
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: 109.31 E-value: 4.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 90 CQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP-------RDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVS 162
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGL-EKPDGGTIVLNGTVlfdsrkkINLPPQQRKIGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 163 ANLKlseKQEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRS 242
Cdd:cd03297 100 LKRK---RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2024481026 243 LAQ--GGRTIICTiHQPSaKLFEMFDKLYILSQGQCIFKG 280
Cdd:cd03297 177 IKKnlNIPVIFVT-HDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
93-264 |
5.97e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 109.70 E-value: 5.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTL---MNILagyrETGMKGQILVNGRP-----RDLRTFRKMSCYIMQDDMLLPHLTVLE----AMM 160
Cdd:COG1126 28 EVVVIIGPSGSGKSTLlrcINLL----EEPDSGTITVDGEDltdskKDINKLRRKVGMVFQQFNLFPHLTVLEnvtlAPI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 161 VSanLKLSeKQEVKkELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 240
Cdd:COG1126 104 KV--KKMS-KAEAE-ERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVM 179
|
170 180
....*....|....*....|....
gi 2024481026 241 RSLAQGGRTIICTIHqpsaklfEM 264
Cdd:COG1126 180 RDLAKEGMTMVVVTH-------EM 196
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
77-280 |
8.36e-27 |
|
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: 108.46 E-value: 8.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 77 GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGR--PRDLRTFRKMSCyIMQDDMLLPHL 153
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlIKPDS--GEITFDGKsyQKNIEALRRIGA-LIEAPGFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 154 TVLEAMMVSANLKLsekqeVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 233
Cdd:cd03268 88 TARENLRLLARLLG-----IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2024481026 234 FQVVSLMRSLAQGGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 280
Cdd:cd03268 163 KELRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
51-229 |
1.51e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 109.02 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 51 PKRSAVNIEFIDLSYSVREGSwwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP 130
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGG-------VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGL-EKPTSGEVLVDGKP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 131 RDlRTFRKMScYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEvKKELVNEILTALGLLEC--SYTRTisLSGGQRKRLAI 208
Cdd:COG1116 75 VT-GPGPDRG-VVFQEPALLPWLTVLDNVALGLELRGVPKAE-RRERARELLELVGLAGFedAYPHQ--LSGGMRQRVAI 149
|
170 180
....*....|....*....|.
gi 2024481026 209 ALELVNNPPVMFFDEPTSGLD 229
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALD 170
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
93-286 |
1.80e-26 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 108.05 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGR------PRDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK 166
Cdd:cd03258 32 EIFGIIGRSGAGKSTLIRCINGL-ERPTSGSVLVDGTdltllsGKELRKARRRIGMIFQHFNLLSSRTVFENVALPLEIA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 167 LSEKQEVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG 246
Cdd:cd03258 111 GVPKAEIEER-VLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024481026 247 -GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKGVVTNLI 286
Cdd:cd03258 190 lGLTIVLITHEMEV-VKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
93-229 |
2.43e-26 |
|
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: 107.71 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP-RDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQ 171
Cdd:cd03300 27 EFFTLLGPSGCGKTTLLRLIAGF-ETPTSGEILLDGKDiTNLPPHKRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKA 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024481026 172 EVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:cd03300 106 EIKER-VAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
54-280 |
4.37e-26 |
|
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: 112.94 E-value: 4.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 54 SAVNIEFIDLSYSvregswWRKRGyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRP-RD 132
Cdd:COG4987 330 GGPSLELEDVSFR------YPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP-QSGSITLGGVDlRD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 133 LR--TFRKMSCYIMQDdmllPHL---TVLEammvsaNLKLSeKQEVKKELVNEILTALGL----------LEcsyTRT-- 195
Cdd:COG4987 402 LDedDLRRRIAVVPQR----PHLfdtTLRE------NLRLA-RPDATDEELWAALERVGLgdwlaalpdgLD---TWLge 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 196 --ISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQgGRTIICTIHQPSAklFEMFDKLYILSQ 273
Cdd:COG4987 468 ggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAG--LERMDRILVLED 544
|
....*..
gi 2024481026 274 GQCIFKG 280
Cdd:COG4987 545 GRIVEQG 551
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
93-280 |
9.42e-26 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 105.75 E-value: 9.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNG------RPRDLRtfRKMScYIMQDdmllPHL---TVLEammvs 162
Cdd:cd03245 31 EKVAIIGRVGSGKSTLLKLLAGlYKPTS--GSVLLDGtdirqlDPADLR--RNIG-YVPQD----VTLfygTLRD----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 163 aNLKLSeKQEVKKELVNEILTALGLLEC------SYTRTI-----SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 231
Cdd:cd03245 97 -NITLG-APLADDERILRAAELAGVTDFvnkhpnGLDLQIgergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024481026 232 SCFQVVSLMRSLAqGGRTIICTIHQPSakLFEMFDKLYILSQGQCIFKG 280
Cdd:cd03245 175 SEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
58-280 |
1.83e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.32 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSwwrkrgykTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGRP-----R 131
Cdd:PRK13639 2 LETRDLKYSYPDGT--------EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPT--SGEVLIKGEPikydkK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 132 DLRTFRKMSCYIMQ--DDMLL-PhlTVLEAMMVSA-NLKLSeKQEVKKElVNEILTALGLLECSYTRTISLSGGQRKRLA 207
Cdd:PRK13639 72 SLLEVRKTVGIVFQnpDDQLFaP--TVEEDVAFGPlNLGLS-KEEVEKR-VKEALKAVGMEGFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024481026 208 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQpsAKLFEMF-DKLYILSQGQCIFKG 280
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEG 219
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
78-275 |
2.02e-25 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 104.56 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 78 YKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRPR-DLRTFRKMSCYIMQDDMLLPHLTVL 156
Cdd:TIGR01277 10 YEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGF-IEPASGSIKVNDQSHtGLAPYQRPVSMLFQENNLFAHLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 157 E--AMMVSANLKLSEKQevkKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 234
Cdd:TIGR01277 89 QniGLGLHPGLKLNAEQ---QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2024481026 235 QVVSLMRSLA-QGGRTIICTIHQPSaKLFEMFDKLYILSQGQ 275
Cdd:TIGR01277 166 EMLALVKQLCsERQRTLLMVTHHLS-DARAIASQIAVVSQGK 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
74-280 |
2.48e-25 |
|
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: 104.28 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 74 RKR-GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGRPRDLRTFRKMScYIMQDDMLLP 151
Cdd:cd03269 7 TKRfGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPD--SGEVLFDGKPLDIAARNRIG-YLPEERGLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 152 HLTVLEAMMVSANLKLSEKQEVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 231
Cdd:cd03269 84 KMKVIDQLVYLAQLKGLKKEEARRR-IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024481026 232 SCFQVVSLMRSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKG 280
Cdd:cd03269 163 NVELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
93-274 |
3.85e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.83 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTL---MNILagyrETGMKGQILV-----------NGRPRDLRTFRKMSCYIMQDDMLLPHLTVLEA 158
Cdd:PRK11264 30 EVVAIIGPSGSGKTTLlrcINLL----EQPEAGTIRVgditidtarslSQQKGLIRQLRQHVGFVFQNFNLFPHRTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 159 MMVSANLKLSEKQEVKKELVNEILTALGLL--ECSYTRtiSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 236
Cdd:PRK11264 106 IIEGPVIVKGEPKEEATARARELLAKVGLAgkETSYPR--RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2024481026 237 VSLMRSLAQGGRTIICTIHQPS-----AKLFEMFDKLYILSQG 274
Cdd:PRK11264 184 LNTIRQLAQEKRTMVIVTHEMSfardvADRAIFMDQGRIVEQG 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
93-285 |
5.39e-25 |
|
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: 103.60 E-value: 5.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGY-RETGmkGQILVNGRP--RDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKlSE 169
Cdd:cd03265 27 EIFGLLGPNGAGKTTTIKMLTTLlKPTS--GRATVAGHDvvREPREVRRRIGIVFQDLSVDDELTGWENLYIHARLY-GV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 170 KQEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL-AQGGR 248
Cdd:cd03265 104 PGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGM 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024481026 249 TIICTIH-QPSAKlfEMFDKLYILSQGQCIFKGVVTNL 285
Cdd:cd03265 184 TILLTTHyMEEAE--QLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
58-327 |
6.73e-25 |
|
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: 108.84 E-value: 6.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSwwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGY--RETGMKGQILVNGRprDLRT 135
Cdd:COG1123 5 LEVRDLSVRYPGGD-------VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlpHGGRISGEVLLDGR--DLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 136 FR-----KMSCYIMQDDM--LLPhLTVLEAMM-VSANLKLSEKQevKKELVNEILTALGLLECSYTRTISLSGGQRKRLA 207
Cdd:COG1123 76 LSealrgRRIGMVFQDPMtqLNP-VTVGDQIAeALENLGLSRAE--ARARVLELLEAVGLERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 208 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL-AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQCIFKGVVTNL- 285
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPPEEIl 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2024481026 286 --------IPYLKGLGLHCPTYHNPADFIIEVA--SGEYGDLNPVLFRAVQN 327
Cdd:COG1123 232 aapqalaaVPRLGAARGRAAPAAAAAEPLLEVRnlSKRYPVRGKGGVRAVDD 283
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
82-256 |
2.25e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 82 LKCLSGkfcqrELIGIMGPSGAGKSTL---MNILagyrETGMKGQILVNGR---------PRDLRTFRKMSCYIMQDDML 149
Cdd:COG4161 23 LECPSG-----ETLVLLGPSGAGKSSLlrvLNLL----ETPDSGQLNIAGHqfdfsqkpsEKAIRLLRQKVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 150 LPHLTVLEAMmVSAN---LKLSEKQEVKKelVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTS 226
Cdd:COG4161 94 WPHLTVMENL-IEAPckvLGLSKEQAREK--AMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190
....*....|....*....|....*....|
gi 2024481026 227 GLDSASCFQVVSLMRSLAQGGRTIICTIHQ 256
Cdd:COG4161 171 ALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
93-257 |
2.26e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 107.89 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNIL-------AG-YRETGMKGQILVNGRPRDLRtfRKMSCYIMQDDMLLPHLTVLEAMMVSAN 164
Cdd:PRK10535 35 EMVAIVGASGSGKSTLMNILgcldkptSGtYRVAGQDVATLDADALAQLR--REHFGFIFQRYHLLSHLTAAQNVEVPAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 165 LKLSEKQEvKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLA 244
Cdd:PRK10535 113 YAGLERKQ-RLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR 191
|
170
....*....|...
gi 2024481026 245 QGGRTIICTIHQP 257
Cdd:PRK10535 192 DRGHTVIIVTHDP 204
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
58-258 |
2.76e-24 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 101.74 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSwwrkrGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP-----RD 132
Cdd:COG4181 9 IELRGLTKTVGTGA-----GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-DRPTSGTVRLAGQDlfaldED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 133 LR-TFRKMSC-YIMQDDMLLPHLTVLEAMMVSANLK-LSEKQEVKKELvneiLTALGL--LECSYTRTisLSGGQRKRLA 207
Cdd:COG4181 83 ARaRLRARHVgFVFQSFQLLPTLTALENVMLPLELAgRRDARARARAL----LERVGLghRLDHYPAQ--LSGGEQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024481026 208 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL-AQGGRTIICTIHQPS 258
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPA 208
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
91-258 |
3.52e-24 |
|
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: 106.60 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 91 QRELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRPR---DLRTFRKMSCYIMQddmlLPHLTvleAMMVSANLKL 167
Cdd:TIGR02857 347 PGERVALVGPSGAGKSTLLNLLLGFVDPT-EGSIAVNGVPLadaDADSWRDQIAWVPQ----HPFLF---AGTIAENIRL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 168 SEKqEVKKELVNEILTALGLLECSYTRTIS-----------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 236
Cdd:TIGR02857 419 ARP-DASDAEIREALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
170 180
....*....|....*....|..
gi 2024481026 237 VSLMRSLAQgGRTIICTIHQPS 258
Cdd:TIGR02857 498 LEALRALAQ-GRTVLLVTHRLA 518
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
93-280 |
1.17e-23 |
|
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: 99.82 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP-RDLRTFRKMS---CYIMQDDMLLPHLTVLEammvsaNLKLS 168
Cdd:cd03224 27 EIVALLGRNGAGKTTLLKTIMGL-LPPRSGSIRFDGRDiTGLPPHERARagiGYVPEGRRIFPELTVEE------NLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 169 E---KQEVKKELVNEILTALGLL-ECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLA 244
Cdd:cd03224 100 AyarRRAKRKARLERVYELFPRLkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELR 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024481026 245 QGGRTIIcTIHQPSAKLFEMFDKLYILSQGQCIFKG 280
Cdd:cd03224 180 DEGVTIL-LVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
57-280 |
2.08e-23 |
|
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: 99.22 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 57 NIEFIDLSYSVREGSWwrkrgyktLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRP---RDL 133
Cdd:cd03254 2 EIEFENVNFSYDEKKP--------VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDP-QKGQILIDGIDirdISR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 134 RTFRKMSCYIMQDDMLLPHlTVLEammvsaNLKLSeKQEVKKELVNEILTALGL------LECSYTRTIS-----LSGGQ 202
Cdd:cd03254 73 KSLRSMIGVVLQDTFLFSG-TIME------NIRLG-RPNATDEEVIEAAKEAGAhdfimkLPNGYDTVLGenggnLSQGE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024481026 203 RKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQgGRTIICTIHQPSAKLFEmfDKLYILSQGQCIFKG 280
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKNA--DKILVLDDGKIIEEG 219
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
43-280 |
2.39e-23 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 104.95 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 43 EAQRFSHLPKRSAvNIEFIDLSYSVREGSwwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmK 121
Cdd:TIGR03375 450 EGTRFLHRPRLQG-EIEFRNVSFAYPGQE-------TPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGlYQPT--E 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 122 GQILVNG------RPRDLRtfRKMScYIMQDDMLLpHLTVLEammvsaNLKLSeKQEVKKELVNEILTALGLLE------ 189
Cdd:TIGR03375 520 GSVLLDGvdirqiDPADLR--RNIG-YVPQDPRLF-YGTLRD------NIALG-APYADDEEILRAAELAGVTEfvrrhp 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 190 CSYTRTI-----SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAqGGRTIICTIHQPSakLFEM 264
Cdd:TIGR03375 589 DGLDMQIgergrSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTS--LLDL 665
|
250
....*....|....*.
gi 2024481026 265 FDKLYILSQGQCIFKG 280
Cdd:TIGR03375 666 VDRIIVMDNGRIVADG 681
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
75-280 |
4.61e-23 |
|
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: 98.62 E-value: 4.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 75 KRGYKTLLKCLS-----GKFCQreligIMGPSGAGKSTLMNILAGYRETGMKGQILVNGRPR---DLRTFRKMSCYI--- 143
Cdd:COG1119 12 RRGGKTILDDISwtvkpGEHWA-----ILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRggeDVWELRKRIGLVspa 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 144 MQDDmLLPHLTVLEaMMVSA-------NLKLSEKQEvkkELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNP 216
Cdd:COG1119 87 LQLR-FPRDETVLD-VVLSGffdsiglYREPTDEQR---ERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 217 PVMFFDEPTSGLDSASCFQVVSLMRSLAQ-GGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 280
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVLVTHHVEE-IPPGITHVLLLKDGRVVAAG 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
82-256 |
6.46e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.16 E-value: 6.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 82 LKCLSGkfcqrELIGIMGPSGAGKSTLMNILaGYRETGMKGQILVNGR---------PRDLRTFRKMSCYIMQDDMLLPH 152
Cdd:PRK11124 23 LDCPQG-----ETLVLLGPSGAGKSSLLRVL-NLLEMPRSGTLNIAGNhfdfsktpsDKAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 153 LTVLE-----AMMVsanLKLSEKQEVKKELvnEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSG 227
Cdd:PRK11124 97 LTVQQnlieaPCRV---LGLSKDQALARAE--KLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180
....*....|....*....|....*....
gi 2024481026 228 LDSASCFQVVSLMRSLAQGGRTIICTIHQ 256
Cdd:PRK11124 172 LDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
93-275 |
8.07e-23 |
|
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: 95.75 E-value: 8.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRP---RDLRTFRKMSCYIMQDDMLLPHlTVLEAMmvsanlklse 169
Cdd:cd03246 29 ESLAIIGPSGSGKSTLARLILGLLRPT-SGRVRLDGADisqWDPNELGDHVGYLPQDDELFSG-SIAENI---------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 170 kqevkkelvneiltalgllecsytrtisLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRT 249
Cdd:cd03246 97 ----------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGAT 148
|
170 180
....*....|....*....|....*.
gi 2024481026 250 IICTIHQPSakLFEMFDKLYILSQGQ 275
Cdd:cd03246 149 RIVIAHRPE--TLASADRILVLEDGR 172
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
93-280 |
2.02e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.39 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGY----RETGMKGQILVN-----GR-PRDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVS 162
Cdd:PRK09984 31 EMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRtvqreGRlARDIRKSRANTGYIFQQFNLVNRLSVLENVLIG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 163 A-------NLKLSEKQEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 235
Cdd:PRK09984 111 AlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024481026 236 VVSLMRSLAQG-GRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 280
Cdd:PRK09984 191 VMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDG 235
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
76-257 |
2.21e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 95.71 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 76 RGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRPRDLRTFRKMSCYIMQDDMLLPHLTV 155
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-AAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 156 LEAMMVSANLKLSEKQEVKkelvnEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 235
Cdd:PRK13539 91 AENLEFWAAFLGGEELDIA-----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|...
gi 2024481026 236 VVSLMRS-LAQGGRTIICTiHQP 257
Cdd:PRK13539 166 FAELIRAhLAQGGIVIAAT-HIP 187
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
73-275 |
2.39e-22 |
|
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: 95.78 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 73 WRKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGR------PRDlrtfRKMScYIMQD 146
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL-EEPTSGRIYIGGRdvtdlpPKD----RDIA-MVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 147 DMLLPHLTVLEAMMVSANLKLSEKQEVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTS 226
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDER-VREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024481026 227 GLDSASCFQVVSLMRSLAQG-GRTIICTIH-QPSAklFEMFDKLYILSQGQ 275
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRlGTTTIYVTHdQVEA--MTMADRIAVMNDGQ 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
77-286 |
2.39e-22 |
|
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: 96.07 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 77 GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGR-----PRDLRTfRKMSCYIMQDDMLL 150
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlVKPD--SGKILLDGQditklPMHKRA-RLGIGYLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 151 PHLTVLEAMMVSANLKLSEKQEVKKELvNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 230
Cdd:cd03218 88 RKLTVEENILAVLEIRGLSKKEREEKL-EELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024481026 231 ASCFQVVSLMRSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKGVVTNLI 286
Cdd:cd03218 167 IAVQDIQKIIKILKDRGIGVLITDHNVRETL-SITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
93-229 |
4.01e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 98.25 E-value: 4.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP-RDLRTFRKMSCYIMQDDMLLPHLTVLEammvsaN----LKL 167
Cdd:COG3842 32 EFVALLGPSGCGKTTLLRMIAGF-ETPDSGRILLDGRDvTGLPPEKRNVGMVFQDYALFPHLTVAE------NvafgLRM 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024481026 168 S--EKQEVkKELVNEILTALGL--LECSYTRTisLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:COG3842 105 RgvPKAEI-RARVAELLELVGLegLADRYPHQ--LSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
82-280 |
5.07e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 95.68 E-value: 5.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 82 LKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGyrETGMKGQILVNGRP------RDLRTFRkmsCYIMQDDMLLPHLTV 155
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG--LLPGQGEILLNGRPlsdwsaAELARHR---AYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 156 LEAMMVSANLKLSEkqEVKKELVNEILTALGlLECSYTRTIS-LSGG--QRKRLAIALELV---NNPP--VMFFDEPTSG 227
Cdd:COG4138 87 FQYLALHQPAGASS--EAVEQLLAQLAEALG-LEDKLSRPLTqLSGGewQRVRLAAVLLQVwptINPEgqLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 228 LDSAScfQVV--SLMRSLAQGGRTIICTIHQPSAKLFEMfDKLYILSQGQCIFKG 280
Cdd:COG4138 164 LDVAQ--QAAldRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQGKLVASG 215
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
93-285 |
5.30e-22 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 97.08 E-value: 5.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGY-RETGmkGQILVNG-----RPRDLR-----TFRKMSCYimqDDmllphLTVLEAMMV 161
Cdd:TIGR01188 20 EVFGFLGPNGAGKTTTIRMLTTLlRPTS--GTARVAGydvvrEPRKVRrsigiVPQYASVD---ED-----LTGRENLEM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 162 SANLK-LSEKqeVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 240
Cdd:TIGR01188 90 MGRLYgLPKD--EAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2024481026 241 RSLAQGGRTIICTIHQpsakLFE---MFDKLYILSQGQCIFKGVVTNL 285
Cdd:TIGR01188 168 RALKEEGVTILLTTHY----MEEadkLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
93-231 |
5.96e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.03 E-value: 5.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYReTGMKGQILVNG----------RPRDLrtfrkmscyIMQDDMLLPHLTVLE--AMM 160
Cdd:PRK10771 26 ERVAILGPSGAGKSTLLNLIAGFL-TPASGSLTLNGqdhtttppsrRPVSM---------LFQENNLFSHLTVAQniGLG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024481026 161 VSANLKLSEKQevkKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 231
Cdd:PRK10771 96 LNPGLKLNAAQ---REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
93-230 |
7.82e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 97.14 E-value: 7.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGR-------PRDlrtfRKMScYIMQDDMLLPHLTVLEammvsaN- 164
Cdd:COG1118 29 ELVALLGPSGSGKTTLLRIIAGL-ETPDSGRIVLNGRdlftnlpPRE----RRVG-FVFQHYALFPHMTVAE------Ni 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024481026 165 ------LKLSEKQevKKELVNEILTALGL--LECSYTRTisLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 230
Cdd:COG1118 97 afglrvRPPSKAE--IRARVEELLELVQLegLADRYPSQ--LSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
58-280 |
9.18e-22 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 95.60 E-value: 9.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSWWRKRGyktlLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGR------P 130
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKA----LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGlLKPT--SGTVTIDGRditakkK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 131 RDLRTFRKMSCYIMQddmlLPH-----LTVLEAMM-VSANLKLSEKqEVKkELVNEILTALGLLECSYTRT-ISLSGGQR 203
Cdd:TIGR04521 75 KKLKDLRKKVGLVFQ----FPEhqlfeETVYKDIAfGPKNLGLSEE-EAE-ERVKEALELVGLDEEYLERSpFELSGGQM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024481026 204 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQ-GGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 280
Cdd:TIGR04521 149 RRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSME-DVAEYADRVIVMHKGKIVLDG 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
76-231 |
9.95e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 93.70 E-value: 9.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 76 RGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETG--MKGQILVNGRPRD-LRTFRKMSCYIMQDDMLLPH 152
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsASGEVLLNGRRLTaLPAEQRRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 153 LTVLE--AMMVSANLKLSEkqevKKELVNEILTALGLLECsYTRTI-SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:COG4136 91 LSVGEnlAFALPPTIGRAQ----RRARVEQALEEAGLAGF-ADRDPaTLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
..
gi 2024481026 230 SA 231
Cdd:COG4136 166 AA 167
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
93-229 |
1.18e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 96.68 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGR------PRDlrtfRKMScyiM--QDDMLLPHLTVLEammvsaN 164
Cdd:COG3839 30 EFLVLLGPSGCGKSTLLRMIAGL-EDPTSGEILIGGRdvtdlpPKD----RNIA---MvfQSYALYPHMTVYE------N 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 165 ----LKLS--EKQEVKKElVNEILTALG---LLEcsytRTIS-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:COG3839 96 iafpLKLRkvPKAEIDRR-VREAAELLGledLLD----RKPKqLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
76-255 |
1.36e-21 |
|
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: 93.78 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 76 RGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETGMK----GQILVNGR--------PRDLRTFRKMscyI 143
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdeGEVLLDGKdiydldvdVLELRRRVGM---V 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 144 MQDDMLLPhLTVLEAMMVSANLKLSEKQEVKKELVNEILTALGLLECSYTRTI--SLSGGQRKRLAIALELVNNPPVMFF 221
Cdd:cd03260 87 FQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190
....*....|....*....|....*....|....
gi 2024481026 222 DEPTSGLDSASCFQVVSLMRSLAQgGRTIICTIH 255
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAELKK-EYTIVIVTH 198
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
76-257 |
2.00e-21 |
|
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: 92.56 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 76 RGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRPRD-LRTFRKMSC-YIMQDDMLLPHL 153
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP-LAGRVLLNGGPLDfQRDSIARGLlYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 154 TVLEammvsaNLK----LSEKQEVKKELVNEILTALGLLECSYtrtisLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:cd03231 89 SVLE------NLRfwhaDHSDEQVEEALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*...
gi 2024481026 230 SASCFQVVSLMRSLAQGGRTIICTIHQP 257
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
93-255 |
3.38e-21 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 93.33 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTL---MNILagyrETGMKGQILVNG-------------RPRDLRTFRKMS---CYIMQDDMLLPHL 153
Cdd:COG4598 35 DVISIIGSSGSGKSTFlrcINLL----ETPDSGEIRVGGeeirlkpdrdgelVPADRRQLQRIRtrlGMVFQSFNLWSHM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 154 TVLEAMM-----VsanLKLSeKQEVKkELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 228
Cdd:COG4598 111 TVLENVIeapvhV---LGRP-KAEAI-ERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSAL 185
|
170 180
....*....|....*....|....*..
gi 2024481026 229 DSASCFQVVSLMRSLAQGGRTIICTIH 255
Cdd:COG4598 186 DPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
81-253 |
3.50e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 92.96 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 81 LLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP---------RDLRTfRKMScYIMQDDMLLP 151
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-DTPTSGDVIFNGQPmsklssaakAELRN-QKLG-FIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 152 HLTVLE--AM-MVSANLKLSEKQEVKKELvneiLTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 228
Cdd:PRK11629 101 DFTALEnvAMpLLIGKKKPAEINSRALEM----LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180
....*....|....*....|....*..
gi 2024481026 229 DSASCFQVVSLMRSL--AQGGRTIICT 253
Cdd:PRK11629 177 DARNADSIFQLLGELnrLQGTAFLVVT 203
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
97-229 |
7.80e-21 |
|
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: 92.01 E-value: 7.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 97 IMGPSGAGKSTLMNILAGYRETGmKGQILVNGRprDLRTF----RKMScYIMQDDMLLPHLTVLEAMMVSANLKLSEKQE 172
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKPD-SGKILLNGK--DITNLppekRDIS-YVPQNYALFPHMTVYKNIAYGLKKRKVDKKE 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024481026 173 VKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:cd03299 106 IERK-VLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
74-256 |
1.55e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.57 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 74 RKR-GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILaGYRETGMKGQILVNG------RPRD----------LRTF 136
Cdd:PRK10619 12 HKRyGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGSIVVNGqtinlvRDKDgqlkvadknqLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 137 RKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKKELVNEILTALGLLECSYTR-TISLSGGQRKRLAIALELVNN 215
Cdd:PRK10619 91 RTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024481026 216 PPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQ 256
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
93-274 |
2.37e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.17 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNG-RPRDLRTFRKMSCYIMQDDMLLPHLTVLEAMmvSANLKLS--E 169
Cdd:PRK11000 30 EFVVFVGPSGCGKSTLLRMIAGL-EDITSGDLFIGEkRMNDVPPAERGVGMVFQSYALYPHLSVAENM--SFGLKLAgaK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 170 KQEVKK--ELVNEILTALGLLEcsyTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV-VSLMRSLAQG 246
Cdd:PRK11000 107 KEEINQrvNQVAEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMrIEISRLHKRL 183
|
170 180
....*....|....*....|....*....
gi 2024481026 247 GRTIICTIH-QPSAklFEMFDKLYILSQG 274
Cdd:PRK11000 184 GRTMIYVTHdQVEA--MTLADKIVVLDAG 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
77-280 |
2.51e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.84 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 77 GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAgyR-ETGMKGQILVNGRPRDLRTFRKMSCYIMqddmLLP-HLT 154
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA--RlLTPQSGTVFLGDKPISMLSSRQLARRLA----LLPqHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 155 VLEAMMV--------SANL----KLSEKQEvkkELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFD 222
Cdd:PRK11231 87 TPEGITVrelvaygrSPWLslwgRLSAEDN---ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024481026 223 EPTSGLDSASCFQVVSLMRSLAQGGRTIICTIH---QPSaklfEMFDKLYILSQGQCIFKG 280
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVMAQG 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
93-286 |
2.62e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 92.45 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTL---MNILagyrETGMKGQILVNGR------PRDLRTFRK---MscyIMQDDMLLPHLTVLEamm 160
Cdd:COG1135 32 EIFGIIGYSGAGKSTLircINLL----ERPTSGSVLVDGVdltalsERELRAARRkigM---IFQHFNLLSSRTVAE--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 161 vsaN----LKLS--EKQEVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 234
Cdd:COG1135 102 ---NvalpLEIAgvPKAEIRKR-VAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024481026 235 QVVSLMRSL-AQGGRTIICTIHqpsaklfEM------FDKLYILSQGQCIFKGVVTNLI 286
Cdd:COG1135 178 SILDLLKDInRELGLTIVLITH-------EMdvvrriCDRVAVLENGRIVEQGPVLDVF 229
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
97-275 |
3.19e-20 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 92.17 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 97 IMGPSGAGKSTLMNILAGYrETGMKGQILVNG-----RPRDLRTFRKMscyiMQDDMLLPHLTVLEAmmVSANLKL-SEK 170
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGF-EQPDSGSIMLDGedvtnVPPHLRHINMV----FQSYALFPHMTVEEN--VAFGLKMrKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 171 QEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV-VSLMRSLAQGGRT 249
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqLELKTIQEQLGIT 153
|
170 180
....*....|....*....|....*.
gi 2024481026 250 IICTIHQPSAKLfEMFDKLYILSQGQ 275
Cdd:TIGR01187 154 FVFVTHDQEEAM-TMSDRIAIMRKGK 178
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
93-275 |
3.32e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.85 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRP-RD--LRTFRKMSCYIMQDDMLLpHLTVLEammvsaNLKLSe 169
Cdd:COG1132 367 ETVALVGPSGSGKSTLVNLLLRFYDPT-SGRILIDGVDiRDltLESLRRQIGVVPQDTFLF-SGTIRE------NIRYG- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 170 KQEVKKELVNEILTALGL------LECSY-----TRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 238
Cdd:COG1132 438 RPDATDEEVEEAAKAAQAhefieaLPDGYdtvvgERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQE 517
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024481026 239 LMRSLAQgGRTIIcTI-HQPSAklFEMFDKLYILSQGQ 275
Cdd:COG1132 518 ALERLMK-GRTTI-VIaHRLST--IRNADRILVLDDGR 551
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
93-280 |
5.22e-20 |
|
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: 89.60 E-value: 5.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRprDLRTF------RKMScyIMQDDMLLPHLTVLEAMM------ 160
Cdd:cd03251 29 ETVALVGPSGSGKSTLVNLIPRFYDVD-SGRILIDGH--DVRDYtlaslrRQIG--LVSQDVFLFNDTVAENIAygrpga 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 161 ----VSANLKLSEKQEVKKELVNEILTALGllecsyTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 236
Cdd:cd03251 104 treeVEEAARAANAHEFIMELPEGYDTVIG------ERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2024481026 237 VSLMRSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 280
Cdd:cd03251 178 QAALERLMK-NRTTFVIAHRLST--IENADRIVVLEDGKIVERG 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
74-275 |
5.70e-20 |
|
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: 89.67 E-value: 5.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 74 RKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGR------PRDLRtfRKMScYIMQDD 147
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP-TSGEIFIDGEdireqdPVELR--RKIG-YVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 148 MLLPHLTVLEAmmVSANLKLSE-KQEVKKELVNEILTALGLLECSYTRTIS--LSGGQRKRLAIALELVNNPPVMFFDEP 224
Cdd:cd03295 85 GLFPHMTVEEN--IALVPKLLKwPKEKIRERADELLALVGLDPAEFADRYPheLSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 225 TSGLDSASCFQVVSLMRSLAQG-GRTIICTIHQpsakLFEMF---DKLYILSQGQ 275
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLQQElGKTIVFVTHD----IDEAFrlaDRIAIMKNGE 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
93-280 |
9.84e-20 |
|
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: 88.19 E-value: 9.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNG-----RPRDLRtfRKMScyIMQDDM-LLPHLTVLEAMMVSANLK 166
Cdd:cd03266 32 EVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDGfdvvkEPAEAR--RRLG--FVSDSTgLYDRLTARENLEYFAGLY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 167 LSEKQEVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG 246
Cdd:cd03266 107 GLKGDELTAR-LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024481026 247 GRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKG 280
Cdd:cd03266 186 GKCILFSTHimQEVERL---CDRVVVLHRGRVVYEG 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
96-251 |
1.00e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 96 GIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRPRDLRTFRK-------MscyIMQDDMLLPHLTVLEammvsaNLKL 167
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGvYQPDS--GEILLDGEPVRFRSPRDaqaagiaI---IHQELNLVPNLSVAE------NIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 168 SeKQEVKKELVN---------EILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 238
Cdd:COG1129 103 G-REPRRGGLIDwramrrrarELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFR 181
|
170
....*....|...
gi 2024481026 239 LMRSLAQGGRTII 251
Cdd:COG1129 182 IIRRLKAQGVAII 194
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
72-280 |
1.10e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.30 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 72 WWRKRGyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRP-----RDLRTFRKMSCYIMQD 146
Cdd:PRK13638 8 WFRYQD-EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRP-QKGAVLWQGKPldyskRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 147 -DMLLPHLTVLEAMMVS-ANLKLSEKQEVKKelVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEP 224
Cdd:PRK13638 86 pEQQIFYTDIDSDIAFSlRNLGVPEAEITRR--VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024481026 225 TSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 280
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHG 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
76-229 |
1.46e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 76 RGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGyRETGMKGQILvngRPRDLRtfrkMScYIMQDDMLLPHLTV 155
Cdd:COG0488 8 FGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG-ELEPDSGEVS---IPKGLR----IG-YLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 156 LEAMMVS-------------ANLKLSEKQEVKKEL------------------VNEILTALGLLECSYTRTIS-LSGGQR 203
Cdd:COG0488 79 LDTVLDGdaelraleaeleeLEAKLAEPDEDLERLaelqeefealggweaearAEEILSGLGFPEEDLDRPVSeLSGGWR 158
|
170 180
....*....|....*....|....*.
gi 2024481026 204 KRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
54-286 |
1.47e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.28 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 54 SAVNIEFIDLSYSVregswwrkrGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGR--PR 131
Cdd:PRK13536 38 STVAIDLAGVSKSY---------GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD-AGKITVLGVpvPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 132 DLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKkELVNEILTALGLLECSYTRTISLSGGQRKRLAIALE 211
Cdd:PRK13536 108 RARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIE-AVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024481026 212 LVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKGVVTNLI 286
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHfmEEAERL---CDRLCVLEAGRKIAEGRPHALI 260
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
76-257 |
1.98e-19 |
|
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: 86.64 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 76 RGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRP----RDLRTfrKMSCYIMQDDMLLP 151
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP-DSGEVRWNGTPlaeqRDEPH--ENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 152 HLTVLEammvsaNLK-LSEKQEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 230
Cdd:TIGR01189 87 ELSALE------NLHfWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*...
gi 2024481026 231 ASCFQVVSLMRS-LAQGGRTIICTiHQP 257
Cdd:TIGR01189 161 AGVALLAGLLRAhLARGGIVLLTT-HQD 187
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
93-280 |
3.03e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.37 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRPRD-----LRTFRKMSCYIMQD-DMLLPHLTVLEAMMVSA-NL 165
Cdd:PRK13636 33 EVTAILGGNGAGKSTLFQNLNGILKP-SSGRILFDGKPIDysrkgLMKLRESVGMVFQDpDNQLFSASVYQDVSFGAvNL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 166 KLSEKqEVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQ 245
Cdd:PRK13636 112 KLPED-EVRKR-VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQK 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 2024481026 246 G-GRTIICTIHQ-PSAKLFemFDKLYILSQGQCIFKG 280
Cdd:PRK13636 190 ElGLTIIIATHDiDIVPLY--CDNVFVMKEGRVILQG 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
57-245 |
5.93e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.53 E-value: 5.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 57 NIEFIDLSYSVREGSWWRKRGYKTLLKCLSgkFCQR--ELIGIMGPSGAGKST----LMNILAGYRETGMKGQILVNGRP 130
Cdd:PRK15134 277 DVEQLQVAFPIRKGILKRTVDHNVVVKNIS--FTLRpgETLGLVGESGSGKSTtglaLLRLINSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 131 RDLRTFRKMSCYIMQD--DMLLPHLTVLEamMVSANLKLSEKQ---EVKKELVNEILTALGLLECSYTRTIS-LSGGQRK 204
Cdd:PRK15134 355 RQLLPVRHRIQVVFQDpnSSLNPRLNVLQ--IIEEGLRVHQPTlsaAQREQQVIAVMEEVGLDPETRHRYPAeFSGGQRQ 432
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024481026 205 RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQ 245
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQ 473
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
62-280 |
6.76e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 86.71 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 62 DLSYSvregswwrkRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYReTGMKGQILVNGRPRDLRTFRKMSC 141
Cdd:COG4559 6 NLSVR---------LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGEL-TPSSGEVRLNGRPLAAWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 142 Y--IM-QDDMLLPHLTVLE--AMMVSANlklSEKQEVKKELVNEILTALGLL---ECSYTrtiSLSGG--QRKRLAIAL- 210
Cdd:COG4559 76 RraVLpQHSSLAFPFTVEEvvALGRAPH---GSSAAQDRQIVREALALVGLAhlaGRSYQ---TLSGGeqQRVQLARVLa 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 211 ---ELVNNPP-VMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSakLFEMF-DKLYILSQGQCIFKG 280
Cdd:COG4559 150 qlwEPVDGGPrWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLN--LAAQYaDRILLLHQGRLVAQG 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
93-275 |
6.93e-19 |
|
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: 86.24 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRPRDLRTFRKMSC-YIMQDDMLLPHLTVLEAmmVSANLKLSEKQ 171
Cdd:cd03296 29 ELVALLGPSGSGKTTLLRLIAGL-ERPDSGTILFGGEDATDVPVQERNVgFVFQHYALFRHMTVFDN--VAFGLRVKPRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 172 EV-----KKELVNEILTALGL--LECSYTRtiSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLA 244
Cdd:cd03296 106 ERppeaeIRAKVHELLKLVQLdwLADRYPA--QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLH 183
|
170 180 190
....*....|....*....|....*....|...
gi 2024481026 245 Q--GGRTIICTIHQPSAklFEMFDKLYILSQGQ 275
Cdd:cd03296 184 DelHVTTVFVTHDQEEA--LEVADRVVVMNKGR 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
93-280 |
7.01e-19 |
|
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: 86.39 E-value: 7.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYReTGMKGQILVNGRPR---DLRTFRKMSCYIMQDDMLLpHLTVLE-------AM--- 159
Cdd:cd03252 29 EVVGIVGRSGSGKSTLTKLIQRFY-VPENGRVLVDGHDLalaDPAWLRRQVGVVLQENVLF-NRSIRDnialadpGMsme 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 160 MVSANLKLSEKQEVKKELVNEILTALGllecsyTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 239
Cdd:cd03252 107 RVIEAAKLAGAHDFISELPEGYDTIVG------EQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024481026 240 MRSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 280
Cdd:cd03252 181 MHDICA-GRTVIIIAHRLST--VKNADRIIVMEKGRIVEQG 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
93-257 |
7.42e-19 |
|
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: 90.11 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRP---RDLRTFRKMSCYIMQDdmllPHL---TVLEammvsaNLK 166
Cdd:TIGR02868 362 ERVAILGPSGSGKSTLLATLAGLLDP-LQGEVTLDGVPvssLDQDEVRRRVSVCAQD----AHLfdtTVRE------NLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 167 LSeKQEVKKELVNEILTALGL------LECSY-----TRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 235
Cdd:TIGR02868 431 LA-RPDATDEELWAALERVGLadwlraLPDGLdtvlgEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE 509
|
170 180
....*....|....*....|..
gi 2024481026 236 VVSLMRSlAQGGRTIICTIHQP 257
Cdd:TIGR02868 510 LLEDLLA-ALSGRTVVLITHHL 530
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
55-245 |
9.81e-19 |
|
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: 87.42 E-value: 9.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 55 AVNiefiDLSYSVREGswwrkrgyktllkclsgkfcqrELIGIMGPSGAGKSTL----MNILAGYRETGmkGQILVNGR- 129
Cdd:COG0444 20 AVD----GVSFDVRRG----------------------ETLGLVGESGSGKSTLaraiLGLLPPPGITS--GEILFDGEd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 130 -----PRDLRTFR--KMScYIMQDDM--LLPHLTVLEAMM--VSANLKLSEKQevKKELVNEILTALGLLEcsYTRTIS- 197
Cdd:COG0444 72 llklsEKELRKIRgrEIQ-MIFQDPMtsLNPVMTVGDQIAepLRIHGGLSKAE--ARERAIELLERVGLPD--PERRLDr 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 198 ----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD---SAscfQVVSLMRSLAQ 245
Cdd:COG0444 147 ypheLSGGMRQRVMIARALALEPKLLIADEPTTALDvtiQA---QILNLLKDLQR 198
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
58-282 |
1.08e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.78 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVRegswwrkrGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYReTGMKGQILVNGRP---RDLR 134
Cdd:PRK13652 4 IETRDLCYSYS--------GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL-KPTSGSVLIRGEPitkENIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 135 TFRKMSCYIMQ--DDMLLPHLTVLEAMMVSANLKLSEkqEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALEL 212
Cdd:PRK13652 75 EVRKFVGLVFQnpDDQIFSPTVEQDIAFGPINLGLDE--ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024481026 213 VNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKGVV 282
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTV 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
74-286 |
1.15e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.17 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 74 RKR-GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGR--PRDLRTFRKMSCYIMQDDMLL 150
Cdd:PRK13537 14 EKRyGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL-THPDAGSISLCGEpvPSRARHARQRVGVVPQFDNLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 151 PHLTVLEAMMVSAN-LKLSEKQevKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:PRK13537 93 PDFTVRENLLVFGRyFGLSAAA--ARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024481026 230 SASCFQVVSLMRSLAQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKGVVTNLI 286
Cdd:PRK13537 171 PQARHLMWERLRSLLARGKTILLTTHfmEEAERL---CDRLCVIEEGRKIAEGAPHALI 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
62-277 |
1.23e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.98 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 62 DLSYSvregswwrkRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGR------PRDLRT 135
Cdd:PRK13548 7 NLSVR---------LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-SGEVRLNGRpladwsPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 136 FRKMscyimqddmlLPH-------LTVLE--AMMVSAnlkLSEKQEVKKELVNEILTALGLLECSYTRTISLSGG--QRK 204
Cdd:PRK13548 77 RRAV----------LPQhsslsfpFTVEEvvAMGRAP---HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGeqQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024481026 205 RLAIAL----ELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLA-QGGRTIICTIHqpSAKLFEMF-DKLYILSQGQCI 277
Cdd:PRK13548 144 QLARVLaqlwEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLH--DLNLAARYaDRIVLLHQGRLV 220
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
81-280 |
1.31e-18 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 90.19 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 81 LLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYReTGMKGQILVNGR------PRDLRtfRKMSCyIMQDDMLL---- 150
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLY-TPQHGQVLVDGVdlaiadPAWLR--RQMGV-VLQENVLFsrsi 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 151 --------PHLTVLEammVSANLKLSEKQEVKKELVNEILTALGllecsyTRTISLSGGQRKRLAIALELVNNPPVMFFD 222
Cdd:TIGR01846 548 rdnialcnPGAPFEH---VIHAAKLAGAHDFISELPQGYNTEVG------EKGANLSGGQRQRIAIARALVGNPRILIFD 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024481026 223 EPTSGLDSASCFQVVSLMRSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 280
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREICR-GRTVIIIAHRLST--VRACDRIIVLEKGQIAESG 673
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
55-280 |
1.35e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 86.70 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 55 AVNiefiDLSYSVREGswwrkrgyktllkclsgkfcqrELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRPRDL 133
Cdd:COG4152 16 AVD----DVSFTVPKG----------------------EIFGLLGPNGAGKTTTIRIILGiLAPDS--GEVLWDGEPLDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 134 RTFRKMScYimqddM-----LLPHLTVLEAMMVSANLKLSEKQEVKKELvNEILTALGLLECSYTRTISLSGGQRKRLAI 208
Cdd:COG4152 68 EDRRRIG-Y-----LpeergLYPKMKVGEQLVYLARLKGLSKAEAKRRA-DEWLERLGLGDRANKKVEELSKGNQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024481026 209 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQ-PSAKlfEMFDKLYILSQGQCIFKG 280
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQmELVE--ELCDRIVIINKGRKVLSG 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
77-284 |
1.84e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.35 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 77 GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG----YRETGMKGQILVNGR---PRDLRTFRKMSCYIMQDDML 149
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARVSGEVYLDGQdifKMDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 150 LPHLTVLEAmmVSANLKLSEKQEVKKEL---VNEILTALGLLECSYTR----TISLSGGQRKRLAIALELVNNPPVMFFD 222
Cdd:PRK14247 94 IPNLSIFEN--VALGLKLNRLVKSKKELqerVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024481026 223 EPTSGLDSASCFQVVSLMRSLAQgGRTIICTIHQPsAKLFEMFDKLYILSQGQCIFKG----VVTN 284
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKK-DMTIVLVTHFP-QQAARISDYVAFLYKGQIVEWGptreVFTN 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
93-275 |
2.18e-18 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 87.09 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGR-------PRDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANL 165
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGL-TRPDEGEIVLNGRtlfdsrkGIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 166 KLSEKQEVKKELVNEILTALGLLEcsyTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQ 245
Cdd:TIGR02142 103 ARPSERRISFERVIELLGIGHLLG---RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHA 179
|
170 180 190
....*....|....*....|....*....|
gi 2024481026 246 GGRTIICTIHQPSAKLFEMFDKLYILSQGQ 275
Cdd:TIGR02142 180 EFGIPILYVSHSLQEVLRLADRVVVLEDGR 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
91-230 |
2.25e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 85.30 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 91 QRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP-------RDLrtfrkmscyIMQDDMLLPHLTVLEAmmVSA 163
Cdd:COG4525 32 SGEFVVALGASGCGKTTLLNLIAGF-LAPSSGEITLDGVPvtgpgadRGV---------VFQKDALLPWLNVLDN--VAF 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024481026 164 NLKLS--EKQEvKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 230
Cdd:COG4525 100 GLRLRgvPKAE-RRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
93-229 |
2.72e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.92 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGR-----P---RDLRTfrkmscyIMQDDMLLPHLTVLEAmmVSAN 164
Cdd:PRK09452 41 EFLTLLGPSGCGKTTVLRLIAGF-ETPDSGRIMLDGQdithvPaenRHVNT-------VFQSYALFPHMTVFEN--VAFG 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024481026 165 LKLSE--KQEVKkELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:PRK09452 111 LRMQKtpAAEIT-PRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
64-245 |
4.02e-18 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 87.82 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 64 SYSVREGSWWRKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTL-MNILagyRETGMKGQILVNGRP------RDLRTF 136
Cdd:COG4172 284 WFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL---RLIPSEGEIRFDGQDldglsrRALRPL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 137 RKMSCYIMQDDM--LLPHLTVL----EAMMVSAnLKLSEKQevKKELVNEILTALGLLECSYTRTIS-LSGGQRKRLAIA 209
Cdd:COG4172 361 RRRMQVVFQDPFgsLSPRMTVGqiiaEGLRVHG-PGLSAAE--RRARVAEALEEVGLDPAARHRYPHeFSGGQRQRIAIA 437
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024481026 210 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQ 245
Cdd:COG4172 438 RALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQR 473
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
52-229 |
5.02e-18 |
|
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: 84.62 E-value: 5.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 52 KRSAVNIEFIDLSYSVREGswwrkrgyktllkclsgkfcqrELIGIMGPSGAGKSTLMNILAGYRE-TGmkGQILVNGRP 130
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREG----------------------EIFVIMGLSGSGKSTLLRCINRLIEpTS--GKVLIDGQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 131 ------RDLRTFR--KMScYIMQDDMLLPHLTVLEAmmVSANLKLS-EKQEVKKELVNEILTALGLLECSYTRTISLSGG 201
Cdd:cd03294 88 iaamsrKELRELRrkKIS-MVFQSFALLPHRTVLEN--VAFGLEVQgVPRAEREERAAEALELVGLEGWEHKYPDELSGG 164
|
170 180
....*....|....*....|....*...
gi 2024481026 202 QRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:cd03294 165 MQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
93-277 |
5.09e-18 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 81.71 E-value: 5.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRPRDLRTFRkmscyimqddmllphltvlEAMmvsanlklsekq 171
Cdd:cd03216 27 EVHALLGENGAGKSTLMKILSGlYKPDS--GEILVDGKEVSFASPR-------------------DAR------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 172 evkkelvneiltALGLlecsytRTIS-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTI 250
Cdd:cd03216 74 ------------RAGI------AMVYqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAV 135
|
170 180 190
....*....|....*....|....*....|
gi 2024481026 251 ICTIHqpsaKLFEMF---DKLYILSQGQCI 277
Cdd:cd03216 136 IFISH----RLDEVFeiaDRVTVLRDGRVV 161
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
92-232 |
5.77e-18 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 85.92 E-value: 5.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 92 RELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP---RDLRTF-----RKMScYIMQDDMLLPHLTVLEammvsa 163
Cdd:COG4148 25 RGVTALFGPSGSGKTTLLRAIAGL-ERPDSGRIRLGGEVlqdSARGIFlpphrRRIG-YVFQEARLFPHLSVRG------ 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 164 NLKLSEKQEVK---KELVNEILTALG---LLEcsyTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 232
Cdd:COG4148 97 NLLYGRKRAPRaerRISFDEVVELLGighLLD---RRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
79-257 |
6.63e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.94 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 79 KTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRET-----GMKGQILVNGRPR---DLRTFRKMSCYIMQDDMLL 150
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskiKVDGKVLYFGKDIfqiDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 151 PHLTVLEAmmVSANLK---LSEKQEVKKeLVNEILTALGLLECSYTRTIS----LSGGQRKRLAIALELVNNPPVMFFDE 223
Cdd:PRK14246 103 PHLSIYDN--IAYPLKshgIKEKREIKK-IVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190
....*....|....*....|....*....|....
gi 2024481026 224 PTSGLDSASCFQVVSLMRSLaQGGRTIICTIHQP 257
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNP 212
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
95-280 |
1.06e-17 |
|
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: 82.66 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 95 IGIMGPSGAGKSTLMNILAGYRETgMKGQILVNG---RPRDLRTFRKMSCYIMQDdMLLPHLTVLEAMMVsANLKLSEKQ 171
Cdd:cd03253 30 VAIVGPSGSGKSTILRLLFRFYDV-SSGSILIDGqdiREVTLDSLRRAIGVVPQD-TVLFNDTIGYNIRY-GRPDATDEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 172 EVKKELVNEILTALGLLECSYT-----RTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQg 246
Cdd:cd03253 107 VIEAAKAAQIHDKIMRFPDGYDtivgeRGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK- 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024481026 247 GRTIICTIHQPS----AklfemfDKLYILSQGQCIFKG 280
Cdd:cd03253 186 GRTTIVIAHRLStivnA------DKIIVLKDGRIVERG 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
93-257 |
1.11e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.52 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP---------RDLRTfrKMSCYIMQDDMLLPHLTVLEAMMVSA 163
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGL-DDGSSGEVSLVGQPlhqmdeearAKLRA--KHVGFVFQSFMLIPTLNALENVELPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 164 NLKlSEKQEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL 243
Cdd:PRK10584 114 LLR-GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSL 192
|
170
....*....|....*
gi 2024481026 244 AQG-GRTIICTIHQP 257
Cdd:PRK10584 193 NREhGTTLILVTHDL 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
49-280 |
1.22e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.82 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 49 HLPKRSAVNIEFIDLSYSVREGswwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG---YRetgmkGQIL 125
Cdd:PRK11174 341 ELASNDPVTIEAEDLEILSPDG--------KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpYQ-----GSLK 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 126 VNG---RPRDLRTFRKMSCYIMQDDmLLPHLTVLEAMMVsANLKLSE---KQEVKKELVNEILTAL--GLlecSYT---R 194
Cdd:PRK11174 408 INGielRELDPESWRKHLSWVGQNP-QLPHGTLRDNVLL-GNPDASDeqlQQALENAWVSEFLPLLpqGL---DTPigdQ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 195 TISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTiHQPSAkLFEMfDKLYILSQG 274
Cdd:PRK11174 483 AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQLED-LAQW-DQIWVMQDG 559
|
....*.
gi 2024481026 275 QCIFKG 280
Cdd:PRK11174 560 QIVQQG 565
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
39-280 |
1.45e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.42 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 39 NHITEAQ---RFS--HLPKRSAVNIEFIDLSYSVREGSwwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILA 113
Cdd:PRK11160 315 NEITEQKpevTFPttSTAAADQVSLTLNNVSFTYPDQP-------QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 114 GYRETGmKGQILVNGRP-RDLR--TFRKMSCYIMQDdmllPHL---TVLEammvsaNLKLSEKQEVKKELVnEILTALGL 187
Cdd:PRK11160 388 RAWDPQ-QGEILLNGQPiADYSeaALRQAISVVSQR----VHLfsaTLRD------NLLLAAPNASDEALI-EVLQQVGL 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 188 ---LECSYT---------RTisLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQgGRTIICTIH 255
Cdd:PRK11160 456 eklLEDDKGlnawlgeggRQ--LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH 532
|
250 260
....*....|....*....|....*
gi 2024481026 256 QpsAKLFEMFDKLYILSQGQCIFKG 280
Cdd:PRK11160 533 R--LTGLEQFDRICVMDNGQIIEQG 555
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
58-280 |
1.47e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 82.38 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVR------------EGSWWRKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETGmkGQI 124
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPTS--GEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 125 LVNG-RP-RDLRTFRKMSCYIM-QDDMLLPHLTVLEAMMVSANLKLSEKQEVKKELvNEILTALGLLECSYTRTISLSGG 201
Cdd:cd03267 79 RVAGlVPwKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRL-DELSELLDLEELLDTPVRQLSLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 202 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL-AQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIF 278
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHymKDIEAL---ARRVLVIDKGRLLY 234
|
..
gi 2024481026 279 KG 280
Cdd:cd03267 235 DG 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
93-280 |
1.47e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.63 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGY--RETGmkgQILVNGR-----PRDLRTFRKMScYIMQDDMLLPHLTVLEAMMVSANL 165
Cdd:PRK10895 30 EIVGLLGPNGAGKTTTFYMVVGIvpRDAG---NIIIDDEdisllPLHARARRGIG-YLPQEASIFRRLSVYDNLMAVLQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 166 KLSEKQEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQ 245
Cdd:PRK10895 106 RDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRD 185
|
170 180 190
....*....|....*....|....*....|....*
gi 2024481026 246 GGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 280
Cdd:PRK10895 186 SGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHG 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
58-280 |
1.89e-17 |
|
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: 80.43 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSwwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRPRDL--RT 135
Cdd:cd03247 1 LSINNVSFSYPEQE-------QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKP-QQGEITLDGVPVSDleKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 136 FRKMSCYIMQDdmllPHLtvleammvsanlklsekqevkkeLVNEILTALGllecsytrtISLSGGQRKRLAIALELVNN 215
Cdd:cd03247 73 LSSLISVLNQR----PYL-----------------------FDTTLRNNLG---------RRFSGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 216 PPVMFFDEPTSGLDSASCFQVVSLMRSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 280
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
82-274 |
2.21e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 81.74 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 82 LKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRPRDLRTFRKMscYIMQDDMLLPHLTVLE--AM 159
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL-AQPTSGGVILEGKQITEPGPDRM--VVFQNYSLLPWLTVREniAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 160 MVSANLKLSEKQEvKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS- 238
Cdd:TIGR01184 78 AVDRVLPDLSKSE-RRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEe 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024481026 239 LMRSLAQGGRTIICTIHQPSAKLFeMFDKLYILSQG 274
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALL-LSDRVVMLTNG 191
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
93-346 |
2.28e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.73 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNG----RPRDLRTFRKMSCYIMQD-DMLLPHLTVLEAMMVSA-NLK 166
Cdd:PRK13644 29 EYIGIIGKNGSGKSTLALHLNGLLRP-QKGKVLVSGidtgDFSKLQGIRKLVGIVFQNpETQFVGRTVEEDLAFGPeNLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 167 LSeKQEVKKeLVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG 246
Cdd:PRK13644 108 LP-PIEIRK-RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 247 GRTIICTIHqpSAKLFEMFDKLYILSQGQCIFKGVVTNLI--PYLKGLGLHCPTyhnpadfIIEVASgeygdlnpvlfRA 324
Cdd:PRK13644 186 GKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEPENVLsdVSLQTLGLTPPS-------LIELAE-----------NL 245
|
250 260
....*....|....*....|...
gi 2024481026 325 VQNGMCTMAEKKSSPDK-ADSSC 346
Cdd:PRK13644 246 KMHGVVIPWENTSSPSSfAEEIC 268
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
89-280 |
2.92e-17 |
|
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: 86.61 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 89 FCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGR--PRDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK 166
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGLLPP-TSGTVLVGGKdiETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 167 LSEKQEVKKELvNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG 246
Cdd:TIGR01257 1032 GRSWEEAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
|
170 180 190
....*....|....*....|....*....|....
gi 2024481026 247 GRTIICTIHQPSAKLfeMFDKLYILSQGQCIFKG 280
Cdd:TIGR01257 1111 RTIIMSTHHMDEADL--LGDRIAIISQGRLYCSG 1142
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
93-229 |
4.04e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.73 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGR-----PRDLRTFRKMscyiMQDDMLLPHLTVleammvSANLKL 167
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGF-EQPTAGQIMLDGVdlshvPPYQRPINMM----FQSYALFPHMTV------EQNIAF 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024481026 168 SEKQE--VKKEL---VNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:PRK11607 115 GLKQDklPKAEIasrVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
96-251 |
4.82e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.31 E-value: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 96 GIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGRPRDLRTFRK-MSCYI-M--QDDMLLPHLTVLE----AMMVSANLK 166
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGlYQPD--SGEILIDGKPVRIRSPRDaIALGIgMvhQHFMLVPNLTVAEnivlGLEPTKGGR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 167 LSEKQEVKKelVNEILTALGL---LEcsytRTI-SLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSASCFQVvsl 239
Cdd:COG3845 113 LDRKAARAR--IRELSERYGLdvdPD----AKVeDLSVGEQQRVEILKALYRGARILILDEPTAVLtpqEADELFEI--- 183
|
170
....*....|..
gi 2024481026 240 MRSLAQGGRTII 251
Cdd:COG3845 184 LRRLAAEGKSII 195
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
58-280 |
9.19e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.94 E-value: 9.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSwwrkrgykTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYReTGMKGQILVNGR---PRDLR 134
Cdd:PRK13647 5 IEVEDLHFRYKDGT--------KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-LPQRGRVKVMGRevnAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 135 TFRKMSCYIMQD-DMLLPHLTVLEAMMVSA-NLKLSeKQEVKkELVNEILTALGLLECSYTRTISLSGGQRKRLAIALEL 212
Cdd:PRK13647 76 WVRSKVGLVFQDpDDQVFSSTVWDDVAFGPvNMGLD-KDEVE-RRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024481026 213 VNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 280
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEG 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
79-255 |
1.11e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.60 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 79 KTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILaGYRETGMKGQILVNGRPR---DLRTFRKMSCYIMQDdmlLPH--- 152
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQPLeswSSKAFARKVAYLPQQ---LPAaeg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 153 LTVLEAMMVSA---NLKLSEKQEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:PRK10575 100 MTVRELVAIGRypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180
....*....|....*....|....*..
gi 2024481026 230 SASCFQVVSLMRSLAQG-GRTIICTIH 255
Cdd:PRK10575 180 IAHQVDVLALVHRLSQErGLTVIAVLH 206
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
93-284 |
1.16e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.77 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTL---MNILagyrETGMKGQILVNGR------PRDLRTFRKmscyimQDDMLLPHLTVLEAMMVSA 163
Cdd:PRK11153 32 EIFGVIGASGAGKSTLircINLL----ERPTSGRVLVDGQdltalsEKELRKARR------QIGMIFQHFNLLSSRTVFD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 164 N----LKLS--EKQEVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 237
Cdd:PRK11153 102 NvalpLELAgtPKAEIKAR-VTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSIL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024481026 238 SLMRSL-AQGGRTIICTIHqpsaklfEM------FDKLYILSQGQCIFKGVVTN 284
Cdd:PRK11153 181 ELLKDInRELGLTIVLITH-------EMdvvkriCDRVAVIDAGRLVEQGTVSE 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
57-288 |
1.50e-16 |
|
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: 83.64 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 57 NIEFIDLSYSVREGSwwrkrgykTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRPR---DL 133
Cdd:TIGR01193 473 DIVINDVSYSYGYGS--------NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR-SGEILLNGFSLkdiDR 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 134 RTFRKMSCYIMQDDMLLPHlTVLEAMMVSANLKLSEkQEVKKEL-VNEILTALGLLECSYTRTIS-----LSGGQRKRLA 207
Cdd:TIGR01193 544 HTLRQFINYLPQEPYIFSG-SILENLLLGAKENVSQ-DEIWAACeIAEIKDDIENMPLGYQTELSeegssISGGQKQRIA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 208 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQggRTIICTIHQPSakLFEMFDKLYILSQGQCIFKGVVTNLIP 287
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLS--VAKQSDKIIVLDHGKIIEQGSHDELLD 697
|
.
gi 2024481026 288 Y 288
Cdd:TIGR01193 698 R 698
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
93-257 |
1.71e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRPRdlrtfrkmSCYIMQ---DDMLLPhLTVLEAMMVSANLKLSE 169
Cdd:NF040873 19 SLTAVVGPNGSGKSTLLKVLAGVLRP-TSGTVRRAGGAR--------VAYVPQrseVPDSLP-LTVRDLVAMGRWARRGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 170 KQEVKKE---LVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG 246
Cdd:NF040873 89 WRRLTRDdraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHAR 168
|
170
....*....|.
gi 2024481026 247 GRTIICTIHQP 257
Cdd:NF040873 169 GATVVVVTHDL 179
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
52-280 |
1.77e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 79.30 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 52 KRSAVNiefiDLSYSVREGswwrkrgyktllkclsgkfcqrELIGIMGPSGAGKSTLMNILagyreTGM----KGQILVN 127
Cdd:COG1137 15 KRTVVK----DVSLEVNQG----------------------EIVGLLGPNGAGKTTTFYMI-----VGLvkpdSGRIFLD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 128 GR-----PRDLRT-------------FRKMScyiMQDDMLLphltVLEAmmvsanLKLSEKQevKKELVNEILTALGLLE 189
Cdd:COG1137 64 GEdithlPMHKRArlgigylpqeasiFRKLT---VEDNILA----VLEL------RKLSKKE--REERLEELLEEFGITH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 190 CSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSAKLfEMFDKLY 269
Cdd:COG1137 129 LRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETL-GICDRAY 207
|
250
....*....|.
gi 2024481026 270 ILSQGQCIFKG 280
Cdd:COG1137 208 IISEGKVLAEG 218
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
93-229 |
2.07e-16 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 83.08 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP---RDLRTFRKMSCYIMQDDMLLPHlTVLEAMMVSANLKLSE 169
Cdd:TIGR03797 480 EFVAIVGPSGSGKSTLLRLLLGF-ETPESGSVFYDGQDlagLDVQAVRRQLGVVLQNGRLMSG-SIFENIAGGAPLTLDE 557
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024481026 170 KQEVKKE--LVNEILT-ALGLlecsYTrTIS-----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:TIGR03797 558 AWEAARMagLAEDIRAmPMGM----HT-VISegggtLSGGQRQRLLIARALVRKPRILLFDEATSALD 620
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
93-275 |
3.59e-16 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 82.01 E-value: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNG---RPRDLRTFRKMSCYIMQDDMLLPHlTV----------LEAM 159
Cdd:TIGR01842 345 EALAIIGPSGSGKSTLARLIVGIWPP-TSGSVRLDGadlKQWDRETFGKHIGYLPQDVELFPG-TVaeniarfgenADPE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 160 MVSANLKLSEKQEVKKELVNEILTALGllecsyTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 239
Cdd:TIGR01842 423 KIIEAAKLAGVHELILRLPDGYDTVIG------PGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANA 496
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024481026 240 MRSLAQGGRTIICTIHQPSakLFEMFDKLYILSQGQ 275
Cdd:TIGR01842 497 IKALKARGITVVVITHRPS--LLGCVDKILVLQDGR 530
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
79-285 |
3.91e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.98 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 79 KTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNIL-------AGYRETGmkgQILVNGRP----RDLRTFRKMSCYIMQDD 147
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRYSG---DVLLGGRSifnyRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 148 MLLPhLTVLEAMMVSANL-KLSEKQEVKKeLVNEILTALGLLECSYTR----TISLSGGQRKRLAIALELVNNPPVMFFD 222
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAhKLVPRKEFRG-VAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024481026 223 EPTSGLDSASCFQVVSLMRSLAQggRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNL 285
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
93-255 |
3.97e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.99 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNG------RPRDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK 166
Cdd:PRK10908 29 EMAFLTGHSGAGKSTLLKLICGI-ERPSAGKIWFSGhditrlKNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 167 LSEKQEVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG 246
Cdd:PRK10908 108 GASGDDIRRR-VSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV 186
|
....*....
gi 2024481026 247 GRTIICTIH 255
Cdd:PRK10908 187 GVTVLMATH 195
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
93-280 |
5.65e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 77.71 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP-RDLRTFRKMS---CYIMQDDMLLPHLTVLEammvsaNLKL- 167
Cdd:COG0410 30 EIVALLGRNGAGKTTLLKAISGL-LPPRSGSIRFDGEDiTGLPPHRIARlgiGYVPEGRRIFPSLTVEE------NLLLg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 168 ----SEKQEVKK--ELVNEILTALGllECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGL-----DsascfQV 236
Cdd:COG0410 103 ayarRDRAEVRAdlERVYELFPRLK--ERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLaplivE-----EI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2024481026 237 VSLMRSLAQGGRTIICtIHQPSAKLFEMFDKLYILSQGQCIFKG 280
Cdd:COG0410 176 FEIIRRLNREGVTILL-VEQNARFALEIADRAYVLERGRIVLEG 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
93-274 |
6.06e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.20 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRPRDLRTFRKmsCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQE 172
Cdd:PRK11248 28 ELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPVEGPGAER--GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 173 vKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG-GRTII 251
Cdd:PRK11248 105 -RLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVL 183
|
170 180
....*....|....*....|...
gi 2024481026 252 CTIHQPSAKLFeMFDKLYILSQG 274
Cdd:PRK11248 184 LITHDIEEAVF-MATELVLLSPG 205
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
82-280 |
7.69e-16 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 77.19 E-value: 7.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 82 LKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNG---RPRDLRTFRKMSCYIMQDdmllPHL---TV 155
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-TSGEILLDGvdiRDLNLRWLRSQIGLVSQE----PVLfdgTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 156 LEAMMVSAN-LKLSEKQEVKKE---------LVNEILTALGllecsyTRTISLSGGQRKRLAIALELVNNPPVMFFDEPT 225
Cdd:cd03249 94 AENIRYGKPdATDEEVEEAAKKanihdfimsLPDGYDTLVG------ERGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024481026 226 SGLDSASCFQVVS-LMRslAQGGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 280
Cdd:cd03249 168 SALDAESEKLVQEaLDR--AMKGRTTIVIAHRLST--IRNADLIAVLQNGQVVEQG 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
93-251 |
8.24e-16 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 77.09 E-value: 8.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMN-ILAGYRETGmkGQILVNGR----------PRD---LRtfRKMSCYIMQDDMLLPHLTVLEA 158
Cdd:COG4778 38 ECVALTGPSGAGKSTLLKcIYGNYLPDS--GSILVRHDggwvdlaqasPREilaLR--RRTIGYVSQFLRVIPRVSALDV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 159 MMVSAnLKLSEKQEVKKELVNEILTALGLLEcsytRTISL-----SGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 233
Cdd:COG4778 114 VAEPL-LERGVDREEARARARELLARLNLPE----RLWDLppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANR 188
|
170
....*....|....*...
gi 2024481026 234 FQVVSLMRSLAQGGRTII 251
Cdd:COG4778 189 AVVVELIEEAKARGTAII 206
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
93-255 |
1.19e-15 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 76.43 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRPRdlRTFRKMSCYIMQDDML---LPhLTVLEAMMVSANLKLSE 169
Cdd:TIGR03771 7 ELLGLLGPNGAGKTTLLRAILGLIPPA-KGTVKVAGASP--GKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGRTGHIGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 170 KQEVKKE---LVNEILTALGLLECSyTRTI-SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQ 245
Cdd:TIGR03771 83 LRRPCVAdfaAVRDALRRVGLTELA-DRPVgELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELAG 161
|
170
....*....|
gi 2024481026 246 GGRTIICTIH 255
Cdd:TIGR03771 162 AGTAILMTTH 171
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
76-257 |
1.38e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.61 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 76 RGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG--YRETGmkgQILVNGRP-RDLRT-FRKMSCYIMQDDMLLP 151
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlaRPDAG---EVLWQGEPiRRQRDeYHQDLLYLGHQPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 152 HLTVLEammvsaNLKLSEK--QEVKKELVNEILTALGL-----LECSYtrtisLSGGQRKRLAIALELVNNPPVMFFDEP 224
Cdd:PRK13538 88 ELTALE------NLRFYQRlhGPGDDEALWEALAQVGLagfedVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|...
gi 2024481026 225 TSGLDSASCFQVVSLMRSLAQGGRTIICTIHQP 257
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
52-280 |
1.54e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 77.34 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 52 KRSAVNIEFIDLSYSVREGSwwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNG-- 128
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSE-------NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGlLKPQ--SGEIKIDGit 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 129 -RPRDLRTFRKMSCYIMQD-DMLLPHLTV-------LEAMMVSanlklsekQEVKKELVNEILTALGLLECSYTRTISLS 199
Cdd:PRK13632 73 iSKENLKEIRKKIGIIFQNpDNQFIGATVeddiafgLENKKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 200 GGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLA-QGGRTIICTIHQPSAKLfeMFDKLYILSQGQCIF 278
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRkTRKKTLISITHDMDEAI--LADKVIVFSEGKLIA 222
|
..
gi 2024481026 279 KG 280
Cdd:PRK13632 223 QG 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
62-275 |
1.67e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 76.64 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 62 DLSYSVREgswwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG---YRETGmkGQILVNGrpRDL----- 133
Cdd:COG0396 5 NLHVSVEG---------KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkYEVTS--GSILLDG--EDIlelsp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 134 --RtFRK---MScyiMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKK--ELVNEILTALGLLEcSY-TRTI--SLSGGQR 203
Cdd:COG0396 72 deR-ARAgifLA---FQYPVEIPGVSVSNFLRTALNARRGEELSAREflKLLKEKMKELGLDE-DFlDRYVneGFSGGEK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 204 KRLAIALELVNNPPVMFFDEPTSGLDSAScFQVVS-LMRSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQ 275
Cdd:COG0396 147 KRNEILQMLLLEPKLAILDETDSGLDIDA-LRIVAeGVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDGR 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
58-304 |
2.00e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.08 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSWWRKRG-YKTLLKCLSGKFcqrelIGIMGPSGAGKSTLMNILAGYRE----TGMKGQILVNG--RP 130
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRAlFDIDLEVKKGSY-----TALIGHTGSGKSTLLQHLNGLLQptegKVTVGDIVVSStsKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 131 RDLRTFRKMSCYIMQ--DDMLLPHLTVLEAMMVSANLKLSeKQEVKKeLVNEILTALGLLECSYTRT-ISLSGGQRKRLA 207
Cdd:PRK13643 77 KEIKPVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIP-KEKAEK-IAAEKLEMVGLADEFWEKSpFELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 208 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKGVVTNL-- 285
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKGHIISCGTPSDVfq 233
|
250 260
....*....|....*....|
gi 2024481026 286 -IPYLKGLGLHCPTYHNPAD 304
Cdd:PRK13643 234 eVDFLKAHELGVPKATHFAD 253
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
62-245 |
4.91e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.49 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 62 DLSYSVREGSWWRKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP------RDLRT 135
Cdd:PRK10419 8 GLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESPSQGNVSWRGEPlaklnrAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 136 FRKMSCYIMQDDM--LLPHLTV----LEAMMVSANLKLSEKQEVKKELVNEILTALGLLEcsyTRTISLSGGQRKRLAIA 209
Cdd:PRK10419 87 FRRDIQMVFQDSIsaVNPRKTVreiiREPLRHLLSLDKAERLARASEMLRAVDLDDSVLD---KRPPQLSGGQLQRVCLA 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024481026 210 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQ 245
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQ 199
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
85-280 |
5.03e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 85 LSGKFCQRELIGIMGPSGAGKSTLMNILAGYreTGMKGQILVNGRPrdLRTFR-----KMSCYIMQDDMLLPHLTVLE-- 157
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL--LPGSGSIQFAGQP--LEAWSaaelaRHRAYLSQQQTPPFAMPVFQyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 158 AMMVSANLKLSEKQEVkkelVNEILTALGLLEcSYTRTIS-LSGG--QRKRLAIALELV---NNP--PVMFFDEPTSGLD 229
Cdd:PRK03695 91 TLHQPDKTRTEAVASA----LNEVAEALGLDD-KLGRSVNqLSGGewQRVRLAAVVLQVwpdINPagQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024481026 230 SAscfQVV---SLMRSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 280
Cdd:PRK03695 166 VA---QQAaldRLLSELCQQGIAVVMSSHDLNHTL-RHADRVWLLKQGKLLASG 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
93-255 |
8.99e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.80 E-value: 8.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRP---RDLRTFRKMSCYIMQDDML--------------LPHLTv 155
Cdd:PRK09536 30 SLVGLVGPNGAGKTTLLRAINGTLTPT-AGTVLVAGDDveaLSARAASRRVASVPQDTSLsfefdvrqvvemgrTPHRS- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 156 leammvsanlKLSEKQEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 235
Cdd:PRK09536 108 ----------RFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVR 177
|
170 180
....*....|....*....|
gi 2024481026 236 VVSLMRSLAQGGRTIICTIH 255
Cdd:PRK09536 178 TLELVRRLVDDGKTAVAAIH 197
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
58-280 |
9.72e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.17 E-value: 9.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSWWRKRG-YKTLLKCLSGKFcqrelIGIMGPSGAGKSTLMNILAGYReTGMKGQILVNG-------R 129
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRAlFDVNLTIEDGSY-----TAFIGHTGSGKSTIMQLLNGLH-VPTQGSVRVDDtlitstsK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 130 PRDLRTFRKMSCYIMQ-DDMLLPHLTVLEAMMVSA-NLKLSEKQEVKkeLVNEILTALGLLECSYTRT-ISLSGGQRKRL 206
Cdd:PRK13649 77 NKDIKQIRKKVGLVFQfPESQLFEETVLKDVAFGPqNFGVSQEEAEA--LAREKLALVGISESLFEKNpFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024481026 207 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 280
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD-DVANYADFVYVLEKGKLVLSG 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
96-275 |
1.00e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.26 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 96 GIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRPRDLRTFRKM----SCYIMQDDMLLPHLTVLEAMMVS---ANLKL 167
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGnYQPDA--GSILIDGQEMRFASTTAAlaagVAIIYQELHLVPEMTVAENLYLGqlpHKGGI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 168 SEKQEVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGG 247
Cdd:PRK11288 112 VNRRLLNYE-AREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEG 190
|
170 180
....*....|....*....|....*...
gi 2024481026 248 RTIICTIHQpSAKLFEMFDKLYILSQGQ 275
Cdd:PRK11288 191 RVILYVSHR-MEEIFALCDAITVFKDGR 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
58-275 |
1.02e-14 |
|
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: 73.66 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSvregswWRKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRP---RDL 133
Cdd:cd03248 12 VKFQNVTFA------YPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfYQPQG--GQVLLDGKPisqYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 134 RTFRKMSCYIMQDDMLLPH---------LTVLEAMMVSANLKLSEKQEVKKELVNEILTALGllecsyTRTISLSGGQRK 204
Cdd:cd03248 84 KYLHSKVSLVGQEPVLFARslqdniaygLQSCSFECVKEAAQKAHAHSFISELASGYDTEVG------EKGSQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024481026 205 RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQgGRTIICTIHQPSakLFEMFDKLYILSQGQ 275
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE-RRTVLVIAHRLS--TVERADQILVLDGGR 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
48-285 |
1.57e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.07 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 48 SHLPKRSAVNIEFIDLSYSvregswWRKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILV 126
Cdd:TIGR00958 469 TLAPLNLEGLIEFQDVSFS------YPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlYQPTG--GQVLL 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 127 NGRP---RDLRTFRKMSCYIMQDDML---------LPHLTVLEAMMVSANLKLSEKQEVKKELVNEILTALGllecsyTR 194
Cdd:TIGR00958 541 DGVPlvqYDHHYLHRQVALVGQEPVLfsgsvreniAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVG------EK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 195 TISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDsASCFQVVSLMRSlaQGGRTIICTIHQPSakLFEMFDKLYILSQG 274
Cdd:TIGR00958 615 GSQLSGGQKQRIAIARALVRKPRVLILDEATSALD-AECEQLLQESRS--RASRTVLLIAHRLS--TVERADQILVLKKG 689
|
250
....*....|.
gi 2024481026 275 QCIFKGVVTNL 285
Cdd:TIGR00958 690 SVVEMGTHKQL 700
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
91-230 |
2.15e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.14 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 91 QRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNG--------RPRDLrtfrkmsCYIMQDDMLLPHLTVLEAmmVS 162
Cdd:PRK11432 31 QGTMVTLLGPSGCGKTTVLRLVAGL-EKPTEGQIFIDGedvthrsiQQRDI-------CMVFQSYALFPHMSLGEN--VG 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024481026 163 ANLKLS--EKQEVKKElVNEILTALGL--LECSYTRTISlsGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 230
Cdd:PRK11432 101 YGLKMLgvPKEERKQR-VKEALELVDLagFEDRYVDQIS--GGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
62-251 |
2.91e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 71.31 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 62 DLSYSVREGswwrkrgyktllkclsgkfcqrELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRPRDLRTFRKMS- 140
Cdd:cd03215 18 DVSFEVRAG----------------------EIVGIAGLVGNGQTELAEALFGLRPP-ASGEITLDGKPVTRRSPRDAIr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 141 ---CYIMQD---DMLLPHLTVLEammvsanlklsekqevkkelvNEILTALgllecsytrtisLSGGQRKRLAIALELVN 214
Cdd:cd03215 75 agiAYVPEDrkrEGLVLDLSVAE---------------------NIALSSL------------LSGGNQQKVVLARWLAR 121
|
170 180 190
....*....|....*....|....*....|....*..
gi 2024481026 215 NPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTII 251
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVL 158
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-274 |
2.92e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.77 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 13 IALEDTVCH-AGPPDAPLLTTHLKKVE-NHITeaqrFSHLPKRSAVNiefiDLSYSVREGswwrkrgyktllkclsgkfc 90
Cdd:PRK13657 310 FEVEDAVPDvRDPPGAIDLGRVKGAVEfDDVS----FSYDNSRQGVE----DVSFEAKPG-------------------- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 91 qrELIGIMGPSGAGKSTLMNILA-GYRETGmkGQILVNG---RPRDLRTFRKMSCYIMQDDMLL------------PHLT 154
Cdd:PRK13657 362 --QTVAIVGPTGAGKSTLINLLQrVFDPQS--GRILIDGtdiRTVTRASLRRNIAVVFQDAGLFnrsiednirvgrPDAT 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 155 ---VLEAMMVSANLKLSEKQEVKKElvneilTALGllecsyTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 231
Cdd:PRK13657 438 deeMRAAAERAQAHDFIERKPDGYD------TVVG------ERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2024481026 232 SCFQVVSLMRSLAQgGRTIICTIHQPS----AKLFEMFDKLYILSQG 274
Cdd:PRK13657 506 TEAKVKAALDELMK-GRTTFIIAHRLStvrnADRILVFDNGRVVESG 551
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
9-275 |
3.84e-14 |
|
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: 75.25 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 9 ACVSI--------ALEDTVC------HAGPPDAPLLT-------------THLKKVENHIT--EAQRFSHL-------PK 52
Cdd:TIGR02633 193 ACVYIshklnevkAVCDTICvirdgqHVATKDMSTMSeddiitmmvgreiTSLYPHEPHEIgdVILEARNLtcwdvinPH 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 53 RSAVNiefiDLSYSVREGswwrkrgyktllkclsgkfcqrELIGIMGPSGAGKSTLMNILAGYRETGMKGQILVNGRPRD 132
Cdd:TIGR02633 273 RKRVD----DVSFSLRRG----------------------EILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVD 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 133 LRT----FRKMSCYIMQD---DMLLPHLTVLEAMMVSANLKLSEKQEV--KKEL--VNEILTALGLLECSYTRTI-SLSG 200
Cdd:TIGR02633 327 IRNpaqaIRAGIAMVPEDrkrHGIVPILGVGKNITLSVLKSFCFKMRIdaAAELqiIGSAIQRLKVKTASPFLPIgRLSG 406
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 201 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIIcTIHQPSAKLFEMFDKLYILSQGQ 275
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAII-VVSSELAEVLGLSDRVLVIGEGK 480
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
93-229 |
4.77e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 74.11 E-value: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGR------PRDlrtfR--KMscyIMQDDMLLPHLTVLEAMmvSAN 164
Cdd:PRK11650 31 EFIVLVGPSGCGKSTLLRMVAGL-ERITSGEIWIGGRvvnelePAD----RdiAM---VFQNYALYPHMSVRENM--AYG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024481026 165 LKLS--EKQEVKK--ELVNEILTALGLLEcsyTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:PRK11650 101 LKIRgmPKAEIEErvAEAARILELEPLLD---RKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
93-280 |
5.27e-14 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 71.91 E-value: 5.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG---YRETGmkGQILVNGR-----PRDLRTfRKMSCYIMQDDMLLPHLTVLEAMMVSAN 164
Cdd:TIGR01978 27 EIHAIMGPNGSGKSTLSKTIAGhpsYEVTS--GTILFKGQdllelEPDERA-RAGLFLAFQYPEEIPGVSNLEFLRSALN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 165 LKLSEKQEVK------KELVNEILTALGLLECSYTRTIS--LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 236
Cdd:TIGR01978 104 ARRSARGEEPldlldfEKLLKEKLALLDMDEEFLNRSVNegFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024481026 237 VSLMRSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQCIFKG 280
Cdd:TIGR01978 184 AEGINRLREPDRSFLIITHYQ--RLLNYIkpDYVHVLLDGRIVKSG 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
97-280 |
5.97e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.35 E-value: 5.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 97 IMGPSGAGKSTLMN-----------------ILAGYRETGMKGQILVNGRP-RDLRTFRKMSCYIMQ-DDMLLPHLTVLE 157
Cdd:PRK13631 57 IIGNSGSGKSTLVThfnglikskygtiqvgdIYIGDKKNNHELITNPYSKKiKNFKELRRRVSMVFQfPEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 158 AMMVSAnLKLSEKQEVKKELVNEILTALGLLECSYTRT-ISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 236
Cdd:PRK13631 137 DIMFGP-VALGVKKSEAKKLAKFYLNKMGLDDSYLERSpFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2024481026 237 VSLMRSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKG 280
Cdd:PRK13631 216 MQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTG 258
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
85-275 |
6.26e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.82 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 85 LSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGR---PRD-LRTFRKMSCYIMQ---DDMLLPHLTVLE 157
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGV-DKRAGGEIRLNGKdisPRSpLDAVKKGMAYITEsrrDNGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 158 AMMVSANLKLS----------EKQEVKkelVNEILTALGLLEC-SYTRTIS-LSGGQRKRLAIALELVNNPPVMFFDEPT 225
Cdd:PRK09700 361 NMAISRSLKDGgykgamglfhEVDEQR---TAENQRELLALKChSVNQNITeLSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2024481026 226 SGLDSASCFQVVSLMRSLAQGGRTIICTihqpSAKLFEMF---DKLYILSQGQ 275
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDGKVILMV----SSELPEIItvcDRIAVFCEGR 486
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
92-299 |
6.42e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.77 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 92 RELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNG-----RPRDLRTFRKMSCYIMQddmlLPHLTVLEAMMVS---- 162
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKP-TSGKIIIDGvditdKKVKLSDIRKKVGLVFQ----YPEYQLFEETIEKdiaf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 163 --ANLKLSEkQEVKKElVNEILTALGLLECSYT--RTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 238
Cdd:PRK13637 108 gpINLGLSE-EEIENR-VKRAMNIVGLDYEDYKdkSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILN 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024481026 239 LMRSLAQG-GRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKGV---VTNLIPYLKGLGLHCP--TY 299
Cdd:PRK13637 186 KIKELHKEyNMTIILVSHsmEDVAKL---ADRIIVMNKGKCELQGTpreVFKEVETLESIGLAVPqvTY 251
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
97-255 |
1.05e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 71.27 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 97 IMGPSGAGKSTLMNILAgyRETGM-KGQILVNGRprDLRTF------RKMScyIM-QDDMLLPHLTVLEamMVS------ 162
Cdd:COG4604 32 LIGPNGAGKSTLLSMIS--RLLPPdSGEVLVDGL--DVATTpsrelaKRLA--ILrQENHINSRLTVRE--LVAfgrfpy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 163 ANLKLSEKQEvkkELVNEILTALGLLECSYtRTI-SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMR 241
Cdd:COG4604 104 SKGRLTAEDR---EIIDEAIAYLDLEDLAD-RYLdELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLR 179
|
170
....*....|....*
gi 2024481026 242 SLAQG-GRTIICTIH 255
Cdd:COG4604 180 RLADElGKTVVIVLH 194
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
58-255 |
1.17e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.78 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSWWRKRGYKTL-LKCLSGKFcqrelIGIMGPSGAGKSTLM---NIL----------AGYretgmkgQ 123
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNIsFELEEGSF-----VALVGHTGSGKSTLMqhfNALlkpssgtitiAGY-------H 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 124 ILVNGRPRDLRTFRKMSCYIMQ-DDMLLPHLTVLEAMMVSA-NLKLSEKQevKKELVNEILTALGLLECSYTRT-ISLSG 200
Cdd:PRK13641 71 ITPETGNKNLKKLRKKVSLVFQfPEAQLFENTVLKDVEFGPkNFGFSEDE--AKEKALKWLKKVGLSEDLISKSpFELSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 201 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIH 255
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
93-285 |
1.43e-13 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 70.63 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGyRETGMKGQILVNGRP-RDLRTFRKMS---CYIMQDDMLLPHLTVLEAMMVSANLKLS 168
Cdd:TIGR03410 27 EVTCVLGRNGVGKTTLLKTLMG-LLPVKSGSIRLDGEDiTKLPPHERARagiAYVPQGREIFPRLTVEENLLTGLAALPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 169 EKQEVKKELVnEILTALglLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGL------DSAscfQVVSLMRs 242
Cdd:TIGR03410 106 RSRKIPDEIY-ELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIqpsiikDIG---RVIRRLR- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2024481026 243 lAQGGRTIIcTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNL 285
Cdd:TIGR03410 179 -AEGGMAIL-LVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
64-243 |
1.63e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.05 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 64 SYSVREGSWWRKRGYKTLlKCLSG---KFCQRELIGIMGPSGAGKSTLMNILAGYRE-TGMK----GQILVNGRPRDLRT 135
Cdd:PRK15079 17 HFDIKDGKQWFWQPPKTL-KAVDGvtlRLYEGETLGVVGESGCGKSTFARAIIGLVKaTDGEvawlGKDLLGMKDDEWRA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 136 FRKMSCYIMQDDM--LLPHLTVLEamMVSANL-----KLSeKQEVKKElVNEILTALGLLECSYTR-TISLSGGQRKRLA 207
Cdd:PRK15079 96 VRSDIQMIFQDPLasLNPRMTIGE--IIAEPLrtyhpKLS-RQEVKDR-VKAMMLKVGLLPNLINRyPHEFSGGQCQRIG 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024481026 208 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL 243
Cdd:PRK15079 172 IARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
93-286 |
1.67e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.04 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILagyreTGM----KGQILVNGR-P-RDLRTFRKMSCYIM-QDDMLLPHLTVLEammvSANL 165
Cdd:COG4586 49 EIVGFIGPNGAGKSTTIKML-----TGIlvptSGEVRVLGYvPfKRRKEFARRIGVVFgQRSQLWWDLPAID----SFRL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 166 -----KLSEKQ--EVKKELVnEILTALGLLEcSYTRTISLsgGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 238
Cdd:COG4586 120 lkaiyRIPDAEykKRLDELV-ELLDLGELLD-TPVRQLSL--GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIRE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 239 LMRSL-AQGGRTIICTIHqpsaklfEMFD------KLYILSQGQCIFKGVVTNLI 286
Cdd:COG4586 196 FLKEYnRERGTTILLTSH-------DMDDiealcdRVIVIDHGRIIYDGSLEELK 243
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
93-229 |
1.97e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.89 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGrpRDLrTFR---KMSCYI---MQDDML--LPHLTVLEAMMVSA 163
Cdd:COG1101 33 DFVTVIGSNGAGKSTLLNAIAGsLPPDS--GSILIDG--KDV-TKLpeyKRAKYIgrvFQDPMMgtAPSMTIEENLALAY 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024481026 164 N------LKLSEKQEvKKELVNEILTALGL-LECS-YTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:COG1101 108 RrgkrrgLRRGLTKK-RRELFRELLATLGLgLENRlDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
74-275 |
2.00e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.48 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 74 RKR-GYKTLLKCL-----SGKFcqrelIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRPrdLRTFRKMSCYIMQDD 147
Cdd:PRK11247 19 SKRyGERTVLNQLdlhipAGQF-----VAVVGRSGCGKSTLLRLLAGL-ETPSAGELLAGTAP--LAEAREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 148 MLLPHLTVLEAmmVSANLKLSEKQEVKkelvnEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSG 227
Cdd:PRK11247 91 RLLPWKKVIDN--VGLGLKGQWRDAAL-----QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024481026 228 LDSASCFQVVSLMRSL-AQGGRTIICTIHQPSAKLfEMFDKLYILSQGQ 275
Cdd:PRK11247 164 LDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAV-AMADRVLLIEEGK 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
77-258 |
4.57e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.49 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 77 GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMN----ILAGYRETGMKGQILVNGR-----PRDLRTFRKMSCYIMQDD 147
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEARVEGEVRLFGRniyspDVDPIEVRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 148 MLLPHLTVLEAmmVSANLKLSEKQEVKKELVNEILTAL---GLLECSYTR----TISLSGGQRKRLAIALELVNNPPVMF 220
Cdd:PRK14267 95 NPFPHLTIYDN--VAIGVKLNGLVKSKKELDERVEWALkkaALWDEVKDRlndyPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024481026 221 FDEPTSGLDSASCFQVVSLMRSLAQgGRTIICTIHQPS 258
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPA 209
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
91-229 |
8.29e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.86 E-value: 8.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 91 QRELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRPRD------------LRTFrkmscyimQDDMLLPHLTVLE 157
Cdd:PRK11300 30 EQEIVSLIGPNGAGKTTVFNCLTGfYKPTG--GTILLRGQHIEglpghqiarmgvVRTF--------QHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 158 AMMVSANLKL----------------SEKQEVkkELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFF 221
Cdd:PRK11300 100 NLLVAQHQQLktglfsgllktpafrrAESEAL--DRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
....*...
gi 2024481026 222 DEPTSGLD 229
Cdd:PRK11300 178 DEPAAGLN 185
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
93-280 |
1.02e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.45 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNG---------RPRDLRtfRKMSCYIMQDDMLLPHLTVLEAM---M 160
Cdd:PRK10070 55 EIFVIMGLSGSGKSTMVRLLNRLIEP-TRGQVLIDGvdiakisdaELREVR--RKKIAMVFQSFALMPHMTVLDNTafgM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 161 VSANLKLSEKQEvkKELvnEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV-SL 239
Cdd:PRK10070 132 ELAGINAEERRE--KAL--DALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdEL 207
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024481026 240 MRSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 280
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVG 247
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
97-255 |
1.29e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 97 IMGPSGAGKSTLMNILAGYRETGmKGQILVNGRPRDLRTFRKMSCYIMQD---DMLLPHLTVLEAMMVSAN----LKLSE 169
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGFVRLA-SGKISILGQPTRQALQKNLVAYVPQSeevDWSFPVLVEDVVMMGRYGhmgwLRRAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 170 KQEvkKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRT 249
Cdd:PRK15056 117 KRD--RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKT 194
|
....*.
gi 2024481026 250 IICTIH 255
Cdd:PRK15056 195 MLVSTH 200
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
58-280 |
1.55e-12 |
|
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: 66.78 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREgswwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG---YRETgmKGQILVNGR----- 129
Cdd:cd03217 1 LEIKDLHVSVGG---------KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkYEVT--EGEILFKGEditdl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 130 PRDLRTfrKMSCYIM-QDDMLLPHLTVLEAMmvsanlklsekqevkkELVNEiltalgllecsytrtiSLSGGQRKRLAI 208
Cdd:cd03217 70 PPEERA--RLGIFLAfQYPPEIPGVKNADFL----------------RYVNE----------------GFSGGEKKRNEI 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024481026 209 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQpsAKLFEMF--DKLYILSQGQCIFKG 280
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY--QRLLDYIkpDRVHVLYDGRIVKSG 187
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
58-285 |
1.56e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 68.65 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSWWRKRGyktlLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRE--TGM--KGQILVNGRPRD- 132
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQA----IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKptTGTvtVDDITITHKTKDk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 133 -LRTFRKMSCYIMQ--DDMLLPHLTVLEAMMVSANLKLSEKQevKKELVNEILTALGllecsYTRTI------SLSGGQR 203
Cdd:PRK13646 79 yIRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDE--VKNYAHRLLMDLG-----FSRDVmsqspfQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 204 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL-AQGGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKGVV 282
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMN-EVARYADEVIVMKEGSIVSQTSP 230
|
...
gi 2024481026 283 TNL 285
Cdd:PRK13646 231 KEL 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
58-229 |
1.88e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.09 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVregswwrkrGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGyRETGMKGQI-----LVNGrprd 132
Cdd:COG0488 316 LELEGLSKSY---------GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-ELEPDSGTVklgetVKIG---- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 133 lrtfrkmscYIMQD-DMLLPHLTVLEAMmvsanlklsekQEVKKELvnEILTALGLLEC-------SYTRTISLSGGQRK 204
Cdd:COG0488 382 ---------YFDQHqEELDPDKTVLDEL-----------RDGAPGG--TEQEVRGYLGRflfsgddAFKPVGVLSGGEKA 439
|
170 180
....*....|....*....|....*
gi 2024481026 205 RLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLD 464
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
57-275 |
2.07e-12 |
|
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: 66.75 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 57 NIEFIDLSYSVREGSwwrkrgyKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRP------ 130
Cdd:cd03244 2 DIEFKNVSLRYRPNL-------PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-SSGSILIDGVDiskigl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 131 RDLRtfRKMSCyIMQDDMLL---------PHLTVLEAMMVSAnLKlsekqEVK-KELVNEILTALGLLECSytRTISLSG 200
Cdd:cd03244 74 HDLR--SRISI-IPQDPVLFsgtirsnldPFGEYSDEELWQA-LE-----RVGlKEFVESLPGGLDTVVEE--GGENLSV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 201 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSlAQGGRTIIC------TIHQpsaklfemFDKLYILSQG 274
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTiahrldTIID--------SDRILVLDKG 213
|
.
gi 2024481026 275 Q 275
Cdd:cd03244 214 R 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
88-251 |
2.96e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 66.98 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 88 KFCQRELIGIMGPSGAGKSTL------MNILagYRETGMKGQILVNGR--------PRDLRT-----FRK-----MSCYi 143
Cdd:COG1117 33 DIPENKVTALIGPSGCGKSTLlrclnrMNDL--IPGARVEGEILLDGEdiydpdvdVVELRRrvgmvFQKpnpfpKSIY- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 144 mqDDmllphltvleammVSANLKLSE--KQEVKKELVNEILTALGL-------LECSYTrtiSLSGGQRKRLAIALELVN 214
Cdd:COG1117 110 --DN-------------VAYGLRLHGikSKSELDEIVEESLRKAALwdevkdrLKKSAL---GLSGGQQQRLCIARALAV 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 2024481026 215 NPPVMFFDEPTSGLDSASCFQVVSLMRSLAQgGRTII 251
Cdd:COG1117 172 EPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIV 207
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
58-297 |
3.00e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.47 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSWWRkrgyktlLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRP---RDLR 134
Cdd:PRK13648 8 IVFKNVSFQYQSDASFT-------LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI-EKVKSGEIFYNNQAitdDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 135 TFRKMSCYIMQDDmllphltvlEAMMVSANLKLS-----EKQEVK----KELVNEILTALGLLECSYTRTISLSGGQRKR 205
Cdd:PRK13648 80 KLRKHIGIVFQNP---------DNQFVGSIVKYDvafglENHAVPydemHRRVSEALKQVDMLERADYEPNALSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 206 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGR-TIICTIHQPSAKLFEmfDKLYILSQGQCIFKGVVTN 284
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEA--DHVIVMNKGTVYKEGTPTE 228
|
250
....*....|....*.
gi 2024481026 285 LIPYLKGL---GLHCP 297
Cdd:PRK13648 229 IFDHAEELtriGLDLP 244
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
91-279 |
3.72e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 91 QRELIGIMGPSGAGKSTLMNILAGY-RETgmKGQILVNGRP-RDLRTFRkmscyIMQDDM-LLPH-LTVLEAMMVSANLK 166
Cdd:PRK11614 30 QGEIVTLIGANGAGKTTLLGTLCGDpRAT--SGRIVFDGKDiTDWQTAK-----IMREAVaIVPEgRRVFSRMTVEENLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 167 L----SEKQEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRS 242
Cdd:PRK11614 103 MggffAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQ 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 2024481026 243 LAQGGRTIIcTIHQPSAKLFEMFDKLYILSQGQCIFK 279
Cdd:PRK11614 183 LREQGMTIF-LVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
82-255 |
4.21e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.42 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 82 LKCLSGKFCQRELIGIMGPSGAGKSTL---MNIL--------------------AGYRETGMKGQILVNGRPRDLRT--- 135
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALllpdtgtiewifkdeknkkkTKEKEKVLEKLVIQKTRFKKIKKike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 136 FRKMSCYIMQ-DDMLLPHLTVLEAMMVSANLKLSEKQEVKKeLVNEILTALGLLECSYTRT-ISLSGGQRKRLAIALELV 213
Cdd:PRK13651 103 IRRRVGVVFQfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKK-RAAKYIELVGLDESYLQRSpFELSGGQKRRVALAGILA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2024481026 214 NNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIH 255
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
93-275 |
4.28e-12 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 69.01 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRprDLRTFRKMSC-----YIMQDDMLLPHlTVLE--AMMVSAN 164
Cdd:COG4618 359 EVLGVIGPSGSGKSTLARLLVGvWPPTA--GSVRLDGA--DLSQWDREELgrhigYLPQDVELFDG-TIAEniARFGDAD 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 165 lklSEKqeVKK--------ELvneIL-------TALGllecsyTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:COG4618 434 ---PEK--VVAaaklagvhEM---ILrlpdgydTRIG------EGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024481026 230 SASCFQVVSLMRSLAQGGRTIICTIHQPSAkLFEMfDKLYILSQGQ 275
Cdd:COG4618 500 DEGEAALAAAIRALKARGATVVVITHRPSL-LAAV-DKLLVLRDGR 543
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
91-255 |
4.49e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 68.68 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 91 QRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILV--------------NGRPRDLRtfrkmscYI---MQDDMLLPHL 153
Cdd:TIGR03269 309 EGEIFGIVGTSGAGKTTLSKIIAGVLEP-TSGEVNVrvgdewvdmtkpgpDGRGRAKR-------YIgilHQEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 154 TVLEAMMVSANLKLSEKQEVKKELVneILTALGLLEcSYTRTI------SLSGGQRKRLAIALELVNNPPVMFFDEPTSG 227
Cdd:TIGR03269 381 TVLDNLTEAIGLELPDELARMKAVI--TLKMVGFDE-EKAEEIldkypdELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180
....*....|....*....|....*....
gi 2024481026 228 LDSASCFQVV-SLMRSLAQGGRTIICTIH 255
Cdd:TIGR03269 458 MDPITKVDVThSILKAREEMEQTFIIVSH 486
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
93-251 |
5.77e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRPRDLRTFRKMS----CYIMQD---DMLLPHLTVLEAMMVsAN 164
Cdd:COG1129 279 EILGIAGLVGAGRTELARALFGaDPADS--GEIRLDGKPVRIRSPRDAIragiAYVPEDrkgEGLVLDLSIRENITL-AS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 165 LK-------LSEKQEvkKELVNEILTALGL----LEcsyTRTISLSGG-QRKrLAIALELVNNPPVMFFDEPTSGLDSAS 232
Cdd:COG1129 356 LDrlsrgglLDRRRE--RALAEEYIKRLRIktpsPE---QPVGNLSGGnQQK-VVLAKWLATDPKVLILDEPTRGIDVGA 429
|
170
....*....|....*....
gi 2024481026 233 CFQVVSLMRSLAQGGRTII 251
Cdd:COG1129 430 KAEIYRLIRELAAEGKAVI 448
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
77-253 |
6.57e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.95 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 77 GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTL------MNILAgyRETGMKGQILVNGR----PR-DLRTFRKMSCYIMQ 145
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsinrMNDLN--PEVTITGSIVYNGHniysPRtDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 146 DDMLLPhLTVLEAMMVSANLKLSEKQEVKKELVNEILTALGLLECSYTR----TISLSGGQRKRLAIALELVNNPPVMFF 221
Cdd:PRK14239 94 QPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190
....*....|....*....|....*....|..
gi 2024481026 222 DEPTSGLDSASCFQVVSLMRSLAQGGRTIICT 253
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDYTMLLVT 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
93-285 |
9.67e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 9.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRPRDlRTFRKMSC-----YIMQDDMLLPHLTVLEAMMVSanlKL 167
Cdd:PRK09700 32 EIHALLGENGAGKSTLMKVLSGIHEP-TKGTITINNINYN-KLDHKLAAqlgigIIYQELSVIDELTVLENLYIG---RH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 168 SEKQEVKKELVN---------EILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 238
Cdd:PRK09700 107 LTKKVCGVNIIDwremrvraaMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2024481026 239 LMRSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKGVVTNL 285
Cdd:PRK09700 187 IMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-275 |
1.18e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 9 ACVSI--------ALEDTVC------HAGPPDAPLLT-------------THLKKVENH-----ITEAQRFSHL----PK 52
Cdd:PRK13549 195 ACIYIshklnevkAISDTICvirdgrHIGTRPAAGMTeddiitmmvgrelTALYPREPHtigevILEVRNLTAWdpvnPH 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 53 RSAVNiefiDLSYSVREGswwrkrgyktllkclsgkfcqrELIGIMGPSGAGKSTLMNILAGYRETGMKGQILVNGRPRD 132
Cdd:PRK13549 275 IKRVD----DVSFSLRRG----------------------EILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 133 LRTFRKMS----CYIMQD---DMLLPHLTVLEAMMVSANLKLSEKQEVKKEL----VNEILTALGLLECSYTRTI-SLSG 200
Cdd:PRK13549 329 IRNPQQAIaqgiAMVPEDrkrDGIVPVMGVGKNITLAALDRFTGGSRIDDAAelktILESIQRLKVKTASPELAIaRLSG 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024481026 201 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTihqpSAKLFE---MFDKLYILSQGQ 275
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI----SSELPEvlgLSDRVLVMHEGK 482
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
93-255 |
1.43e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 65.08 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG--------YRETGMKGQILVNGRPRDLRTFRKMscyIMQDDM----------LLPHLT 154
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDEFRGSELQNYFTK---LLEGDVkvivkpqyvdLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 155 vleAMMVSANLKLSEKQEVKKELVnEILTALGLLEcsytRTIS-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 233
Cdd:cd03236 104 ---KGKVGELLKKKDERGKLDELV-DQLELRHVLD----RNIDqLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180
....*....|....*....|..
gi 2024481026 234 FQVVSLMRSLAQGGRTIICTIH 255
Cdd:cd03236 176 LNAARLIRELAEDDNYVLVVEH 197
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
52-297 |
1.71e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.21 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 52 KRSAVNiefiDLSYSVREGSWwrkrgyktllkclsgkfcqrelIGIMGPSGAGKSTLMNILAGY--RETGMKGQILVNGR 129
Cdd:PRK13640 19 KKPALN----DISFSIPRGSW----------------------TALIGHNGSGKSTISKLINGLllPDDNPNSKITVDGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 130 PRDLRTF---RKMSCYIMQD-DMLLPHLTVLEAMMVSANLKLSEKQEVKKeLVNEILTALGLLECSYTRTISLSGGQRKR 205
Cdd:PRK13640 73 TLTAKTVwdiREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIK-IVRDVLADVGMLDYIDSEPANLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 206 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLA-QGGRTIICTIHQPSAKlfEMFDKLYILSQGQCIFKGVVTN 284
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA--NMADQVLVLDDGKLLAQGSPVE 229
|
250
....*....|....*.
gi 2024481026 285 LIP---YLKGLGLHCP 297
Cdd:PRK13640 230 IFSkveMLKEIGLDIP 245
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
79-304 |
1.90e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.06 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 79 KTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAgyRETGMKGQILVNGRPR-----------DLRTFRKMSCYIMQDD 147
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN--RMNELESEVRVEGRVEffnqniyerrvNLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 148 MLLPhLTVLEAMMVSANL----------KLSEKQEVKKELVNEILTALgllecsYTRTISLSGGQRKRLAIALELVNNPP 217
Cdd:PRK14258 98 NLFP-MSVYDNVAYGVKIvgwrpkleidDIVESALKDADLWDEIKHKI------HKSALDLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 218 VMFFDEPTSGLDSASCFQVVSLMRSLA-QGGRTIICTIHQpsaklfemFDKLYILSQGQCIFKGvVTNLIPYLKGLGLHC 296
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHN--------LHQVSRLSDFTAFFKG-NENRIGQLVEFGLTK 241
|
....*...
gi 2024481026 297 PTYHNPAD 304
Cdd:PRK14258 242 KIFNSPHD 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
93-277 |
2.00e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG-YRETGMKGQILVNGRP------RDlrTFRKMSCYIMQDDMLLPHLTVLEAMMVSANL 165
Cdd:PRK13549 32 EIVSLCGENGAGKSTLMKVLSGvYPHGTYEGEIIFEGEElqasniRD--TERAGIAIIHQELALVKELSVLENIFLGNEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 166 klsekqeVKKELVN---------EILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 236
Cdd:PRK13549 110 -------TPGGIMDydamylraqKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2024481026 237 VSLMRSLAQGGRTIICTIHqpsaKLFEMF---DKLYILSQGQCI 277
Cdd:PRK13549 183 LDIIRDLKAHGIACIYISH----KLNEVKaisDTICVIRDGRHI 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
58-280 |
2.38e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.81 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSWWRKRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRPRDLRTFR 137
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-SGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 138 KMSC---YIMQD--DMLLPHLTVLEAMMVSANLKLSEKQEVKKELVNEILTALGLL-ECSYTRTISLSGGQRKRLAIALE 211
Cdd:PRK15112 84 YRSQrirMIFQDpsTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024481026 212 LVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL--AQGGRTIICTIHQPSAKlfEMFDKLYILSQGQCIFKG 280
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMK--HISDQVLVMHQGEVVERG 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
93-277 |
2.71e-11 |
|
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: 66.39 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG-YRETGMKGQILVNGRP---RDLR-TFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKL 167
Cdd:TIGR02633 28 ECVGLCGENGAGKSTLMKILSGvYPHGTWDGEIYWSGSPlkaSNIRdTERAGIVIIHQELTLVPELSVAENIFLGNEITL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 168 SEKQEVKKELV---NEILTALGLLECSYTRTIS-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL 243
Cdd:TIGR02633 108 PGGRMAYNAMYlraKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 2024481026 244 AQGGRTIICTIHqpsaKLFE---MFDKLYILSQGQCI 277
Cdd:TIGR02633 188 KAHGVACVYISH----KLNEvkaVCDTICVIRDGQHV 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
75-280 |
2.83e-11 |
|
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: 63.71 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 75 KRGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGRPR---DLRTFrkmscyimqddmLL 150
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPPD--SGTVTVRGRVSsllGLGGG------------FN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 151 PHLTVLE-AMMVSANLKLSEKQevKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:cd03220 97 PELTGREnIYLNGRLLGLSRKE--IDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2024481026 230 SAscFQ--VVSLMRSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 280
Cdd:cd03220 175 AA--FQekCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
97-229 |
2.84e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.28 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 97 IMGPSGAGKSTLMNILAGYrETGMKGQILVNGR---PRDLRTF-----RKMScYIMQDDMLLPHLTVleammvSANLKLS 168
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGL-TRPQKGRIVLNGRvlfDAEKGIClppekRRIG-YVFQDARLFPHYKV------RGNLRYG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024481026 169 EKqEVKKELVNEILTALGLlECSYTR-TISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:PRK11144 101 MA-KSMVAQFDKIVALLGI-EPLLDRyPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
95-286 |
2.86e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.58 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 95 IGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRprDLRTFRKMS----CYIMQDDMLLPHLTVLEAMMVSANLKLSEK 170
Cdd:PRK11176 372 VALVGRSGSGKSTIANLLTRFYDI-DEGEILLDGH--DLRDYTLASlrnqVALVSQNVHLFNDTIANNIAYARTEQYSRE 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 171 QEVK-----------KELVNEILTALGllecsyTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 239
Cdd:PRK11176 449 QIEEaarmayamdfiNKMDNGLDTVIG------ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAA 522
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2024481026 240 MRSLaQGGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKGVVTNLI 286
Cdd:PRK11176 523 LDEL-QKNRTSLVIAHRLST--IEKADEILVVEDGEIVERGTHAELL 566
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
93-255 |
3.42e-11 |
|
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: 66.96 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGyRETGMKGQILVNGRP--RDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEK 170
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTG-DTTVTSGDATVAGKSilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 171 QEVKKeLVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTI 250
Cdd:TIGR01257 2045 EEIEK-VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAV 2123
|
....*
gi 2024481026 251 ICTIH 255
Cdd:TIGR01257 2124 VLTSH 2128
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
95-251 |
3.82e-11 |
|
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: 65.96 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 95 IGIMGPSGAGKSTLMNILAGyretgmkgQILVN-GRPRD-------LRTFRKMscyIMQDdmllpHLTVLeammVSANLK 166
Cdd:COG1245 102 TGILGPNGIGKSTALKILSG--------ELKPNlGDYDEepswdevLKRFRGT---ELQD-----YFKKL----ANGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 167 LSEK-QEVK----------KEL---------VNEILTALGLlECSYTRTIS-LSGGQRKRLAIALELVNNPPVMFFDEPT 225
Cdd:COG1245 162 VAHKpQYVDlipkvfkgtvRELlekvdergkLDELAEKLGL-ENILDRDISeLSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180
....*....|....*....|....*.
gi 2024481026 226 SGLDSASCFQVVSLMRSLAQGGRTII 251
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEEGKYVL 266
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
58-233 |
5.11e-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: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVregswwrkrGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGyRETGMKGQILVNGRPRdlrtfr 137
Cdd:cd03221 1 IELENLSKTY---------GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-ELEPDEGIVTWGSTVK------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 138 kmSCYIMQddmllphltvleammvsanlklsekqevkkelvneiltalgllecsytrtisLSGGQRKRLAIALELVNNPP 217
Cdd:cd03221 65 --IGYFEQ----------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170
....*....|....*.
gi 2024481026 218 VMFFDEPTSGLDSASC 233
Cdd:cd03221 91 LLLLDEPTNHLDLESI 106
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
93-275 |
7.74e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.99 E-value: 7.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGRP---RDLRTFRKMSCYIMQDDMLLPHLTVleammvsanlklS 168
Cdd:PRK10522 350 ELLFLIGGNGSGKSTLAMLLTGlYQPQ--SGEILLDGKPvtaEQPEDYRKLFSAVFTDFHLFDQLLG------------P 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 169 EKQEVKKELVNEILTALGL-----LECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSglDSASCFQVV---SLM 240
Cdd:PRK10522 416 EGKPANPALVEKWLERLKMahkleLEDGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAA--DQDPHFRREfyqVLL 493
|
170 180 190
....*....|....*....|....*....|....*
gi 2024481026 241 RSLAQGGRTIICTIHQPSakLFEMFDKLYILSQGQ 275
Cdd:PRK10522 494 PLLQEMGKTIFAISHDDH--YFIHADRLLEMRNGQ 526
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
93-243 |
9.20e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.64 E-value: 9.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGyRETGMKGQILVNGRPRDLRTFRKMS------------CYIMQD--DMLlphltvleA 158
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSA-RLAPDAGEVHYRMRDGQLRDLYALSeaerrrllrtewGFVHQHprDGL--------R 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 159 MMVSANLKLSEK-----QEVKKELVNEILTALGLLECSYTRTISL----SGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:PRK11701 104 MQVSAGGNIGERlmavgARHYGDIRATAGDWLERVEIDAARIDDLpttfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
170
....*....|....
gi 2024481026 230 SASCFQVVSLMRSL 243
Cdd:PRK11701 184 VSVQARLLDLLRGL 197
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
58-275 |
1.22e-10 |
|
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: 61.33 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSvregswWRKRGYKT--LLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGyrETG-MKGQILVNGRprdlr 134
Cdd:cd03250 1 ISVEDASFT------WDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEkLSGSVSVPGS----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 135 tfrkMScYIMQddmllphltvlEAMMVSANLKlsEK----QEVKKELVNEILTALGLL---------------EcsytRT 195
Cdd:cd03250 68 ----IA-YVSQ-----------EPWIQNGTIR--ENilfgKPFDEERYEKVIKACALEpdleilpdgdlteigE----KG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 196 ISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS---ASCFQvvSLMRSLAQGGRTIICTIHQPSakLFEMFDKLYILS 272
Cdd:cd03250 126 INLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAhvgRHIFE--NCILGLLLNNKTRILVTHQLQ--LLPHADQIVVLD 201
|
...
gi 2024481026 273 QGQ 275
Cdd:cd03250 202 NGR 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
82-256 |
1.44e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 82 LKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGRPRDLRT---FRKMSCYIM-QDDMLLPHLTVLE 157
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGI-VPPDSGTLEIGGNPCARLTpakAHQLGIYLVpQEPLLFPNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 158 AMMvsanLKLSEKQEVKKELvNEILTALGlleCSYTRTI---SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 234
Cdd:PRK15439 106 NIL----FGLPKRQASMQKM-KQLLAALG---CQLDLDSsagSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETE 177
|
170 180
....*....|....*....|..
gi 2024481026 235 QVVSLMRSLAQGGRTIICTIHQ 256
Cdd:PRK15439 178 RLFSRIRELLAQGVGIVFISHK 199
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
54-254 |
1.56e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.82 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 54 SAVNiefiDLSYSVREGswwrkrgyktllkclsgkfcqrELIGIMGPSGAGKS----TLMNILAGYRETG----MKGQIL 125
Cdd:PRK09473 30 TAVN----DLNFSLRAG----------------------ETLGIVGESGSGKSqtafALMGLLAANGRIGgsatFNGREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 126 VNGRPRDLRTFR--KMScYIMQDDM--LLPHLTVLEAMMVSANL-KLSEKQEVKKELVnEILTALGLLECSYTRTI---S 197
Cdd:PRK09473 84 LNLPEKELNKLRaeQIS-MIFQDPMtsLNPYMRVGEQLMEVLMLhKGMSKAEAFEESV-RMLDAVKMPEARKRMKMyphE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024481026 198 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTI 254
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMI 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
82-275 |
2.02e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 60.89 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 82 LKCLSGKFCQRELIGIMGPSGAGKSTLmnILAGYRET-GMKGQILVNGRP------RDLRtfRKMSCyIMQDDMLLphlt 154
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLeAEEGKIEIDGIDistiplEDLR--SSLTI-IPQDPTLF---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 155 vleAMMVSANLKLSEKQEVKkelvnEILTALGLLECSytrtISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 234
Cdd:cd03369 95 ---SGTIRSNLDPFDEYSDE-----EIYGALRVSEGG----LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024481026 235 QVVSLMRSLAQGGrTIICTIHQPSAKLfeMFDKLYILSQGQ 275
Cdd:cd03369 163 LIQKTIREEFTNS-TILTIAHRLRTII--DYDKILVMDAGE 200
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
53-245 |
2.19e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.29 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 53 RSAVNIEFIDL--SYSVREGSWWRKRgyktLLKCLSG-KFC-QR-ELIGIMGPSGAGKSTLMNILAgYRETGMKGQILVN 127
Cdd:PRK11308 1 SQQPLLQAIDLkkHYPVKRGLFKPER----LVKALDGvSFTlERgKTLAVVGESGCGKSTLARLLT-MIETPTGGELYYQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 128 GR------PRDLRTFRKMSCYIMQDDM--LLPHLTV---LEAMMVsANLKLSEKQevKKELVNEILTALGLLECSYTRTI 196
Cdd:PRK11308 76 GQdllkadPEAQKLLRQKIQIVFQNPYgsLNPRKKVgqiLEEPLL-INTSLSAAE--RREKALAMMAKVGLRPEHYDRYP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024481026 197 SL-SGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQ 245
Cdd:PRK11308 153 HMfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
160-300 |
2.32e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.45 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 160 MVSANLKLSEKQevKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 239
Cdd:NF000106 109 MIGR*LDLSRKD--ARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024481026 240 MRSLAQGGRTIICTIhQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYH 300
Cdd:NF000106 187 VRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAH 246
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
79-255 |
2.50e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.42 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 79 KTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYrETGMKGQIlvngRPRDLRTFRkmscYIMQDDMLLPHLTVLEA 158
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKDFNGEA----RPQPGIKVG----YLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 159 MM---------------VSANL--------KLSEKQEVKKELV---------NEILTALGLLECSY--TRTISLSGGQRK 204
Cdd:TIGR03719 89 VEegvaeikdaldrfneISAKYaepdadfdKLAAEQAELQEIIdaadawdldSQLEIAMDALRCPPwdADVTKLSGGERR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024481026 205 RLAIALELVNNPPVMFFDEPTSGLDSAScfqVVSLMRSLAQGGRTIICTIH 255
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPGTVVAVTH 216
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
93-229 |
2.98e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.63 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRPRDLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQE 172
Cdd:PRK13543 38 EALLVQGDNGAGKTTLLRVLAGLLHVE-SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQ 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024481026 173 VKkelvNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:PRK13543 117 MP----GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
93-306 |
2.99e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.41 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYrETGMKGQILVNGR------PRDlrtfRKMScYIMQDDMLLPHLTVLEAmmVSANLK 166
Cdd:PRK10851 29 QMVALLGPSGSGKTTLLRIIAGL-EHQTSGHIRFHGTdvsrlhARD----RKVG-FVFQHYALFRHMTVFDN--IAFGLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 167 LSEKQE-----VKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMR 241
Cdd:PRK10851 101 VLPRRErpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 242 SLAQGGR--TIICTIHQPSAklFEMFDKLYILSQGqCI--------------------FKGVVTNLIPYLKGLGLHCPTY 299
Cdd:PRK10851 181 QLHEELKftSVFVTHDQEEA--MEVADRVVVMSQG-NIeqagtpdqvwrepatrfvleFMGEVNRLQGTIRGGQFHVGAH 257
|
....*..
gi 2024481026 300 HNPADFI 306
Cdd:PRK10851 258 RWPLGYT 264
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
97-276 |
3.38e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 59.09 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 97 IMGPSGAGKSTLMNILAGYRETGmKGQIlvnGRPRDLRTFrkmscYIMQddmllphltvlEAMMVSANLKlsekqevkke 176
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWG-SGRI---GMPEGEDLL-----FLPQ-----------RPYLPLGTLR---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 177 lvnEILtalgllecSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLaqgGRTIICTIHQ 256
Cdd:cd03223 82 ---EQL--------IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHR 147
|
170 180
....*....|....*....|.
gi 2024481026 257 PS-AKLFEMfdKLYILSQGQC 276
Cdd:cd03223 148 PSlWKFHDR--VLDLDGEGGW 166
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
58-230 |
3.56e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.81 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 58 IEFIDLSYSVREGSWwrkrgyktLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRPRDL---R 134
Cdd:PRK10790 341 IDIDNVSFAYRDDNL--------VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL-TEGEIRLDGRPLSSlshS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 135 TFRKMSCYIMQDDMLLphltvleAMMVSANLKLSekQEVKKELVNEILTALGLLEcsYTRTIS-------------LSGG 201
Cdd:PRK10790 412 VLRQGVAMVQQDPVVL-------ADTFLANVTLG--RDISEEQVWQALETVQLAE--LARSLPdglytplgeqgnnLSVG 480
|
170 180
....*....|....*....|....*....
gi 2024481026 202 QRKRLAIALELVNNPPVMFFDEPTSGLDS 230
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDS 509
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
93-223 |
3.76e-10 |
|
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: 62.89 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRP---RDLRTFRKMSCYIMQDDMLLPHLtvleammvsanlkLS 168
Cdd:COG4615 359 ELVFIVGGNGSGKSTLAKLLTGlYRPES--GEILLDGQPvtaDNREAYRQLFSAVFSDFHLFDRL-------------LG 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 169 EKQEVKKELVNEILTALGLLE-CSYTR----TISLSGGQRKRLAIALELVNNPPVMFFDE 223
Cdd:COG4615 424 LDGEADPARARELLERLELDHkVSVEDgrfsTTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
78-275 |
4.63e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 62.52 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 78 YKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETGmKGQILvngRPRDLRTfrkmscyimqddMLLPHltvlE 157
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG-SGRIA---RPAGARV------------LFLPQ----R 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 158 AMMVSANLK--LS---EKQEVKKELVNEILTALGL--------LECSYTRTisLSGGQRKRLAIALELVNNPPVMFFDEP 224
Cdd:COG4178 435 PYLPLGTLReaLLypaTAEAFSDAELREALEAVGLghlaerldEEADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024481026 225 TSGLDSASCFQVVSLMRSLAQGGrTIICTIHQPSakLFEMFDKLYILSQGQ 275
Cdd:COG4178 513 TSALDEENEAALYQLLREELPGT-TVISVGHRST--LAAFHDRVLELTGDG 560
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
93-275 |
5.16e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGY--REtgmKGQILVNGRPRDLRT----FRKMSCYIMQD---DMLLPHLTVLEAMMVSA 163
Cdd:PRK10762 279 EILGVSGLMGAGRTELMKVLYGAlpRT---SGYVTLDGHEVVTRSpqdgLANGIVYISEDrkrDGLVLGMSVKENMSLTA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 164 NLKLSE-----KQEVKKELVNEILTALGLLECSYTRTIS-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 237
Cdd:PRK10762 356 LRYFSRaggslKHADEQQAVSDFIRLFNIKTPSMEQAIGlLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIY 435
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024481026 238 SLMRSLAQGGRTIICTihqpSAKLFE---MFDKLYILSQGQ 275
Cdd:PRK10762 436 QLINQFKAEGLSIILV----SSEMPEvlgMSDRILVMHEGR 472
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
93-229 |
7.03e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 7.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGyrETGM-KGQI-----LVNGR-----PRD-------------------LRTFRKMSCY 142
Cdd:PRK11147 30 ERVCLVGRNGAGKSTLMKILNG--EVLLdDGRIiyeqdLIVARlqqdpPRNvegtvydfvaegieeqaeyLKRYHDISHL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 143 IMQD--DMLLPHLTVLEAMMVSANLKLSEKQevkkelVNEILTALGLleCSYTRTISLSGGQRKRLAIALELVNNPPVMF 220
Cdd:PRK11147 108 VETDpsEKNLNELAKLQEQLDHHNLWQLENR------INEVLAQLGL--DPDAALSSLSGGWLRKAALGRALVSNPDVLL 179
|
....*....
gi 2024481026 221 FDEPTSGLD 229
Cdd:PRK11147 180 LDEPTNHLD 188
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
95-246 |
7.19e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 95 IGIMGPSGAGKSTLMNILAG---------------------YRETGMKG--QILVNGrprDLRTFRKMScYImqdDmLLP 151
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGelipnlgdyeeepswdevlkrFRGTELQNyfKKLYNG---EIKVVHKPQ-YV---D-LIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 152 HL---TVLEAmmvsanLKLSEKQEVKKELVNEiltaLGLlECSYTRTIS-LSGGQRKRLAIALELVNNPPVMFFDEPTSG 227
Cdd:PRK13409 174 KVfkgKVREL------LKKVDERGKLDEVVER----LGL-ENILDRDISeLSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170
....*....|....*....
gi 2024481026 228 LDSASCFQVVSLMRSLAQG 246
Cdd:PRK13409 243 LDIRQRLNVARLIRELAEG 261
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
93-243 |
8.02e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 8.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGR------PRDLRTFRKMSCYIMQDDM--LLPHLTVLEAMMVSAN 164
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVES-QGGEIIFNGQridtlsPGKLQALRRDIQFIFQDPYasLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 165 LKLSEKQEVKKELVNEILTALGLL-ECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL 243
Cdd:PRK10261 430 VHGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
93-280 |
8.13e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.71 E-value: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGRprdlrtfrkMSCyimqddmLL-------PHLTVLE-AMMVSA 163
Cdd:COG1134 53 ESVGIIGRNGAGKSTLLKLIAGiLEPT--SGRVEVNGR---------VSA-------LLelgagfhPELTGREnIYLNGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 164 NLKLSeKQEVkKELVNEIL--TALGllecsytRTI-----SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAscFQ- 235
Cdd:COG1134 115 LLGLS-RKEI-DEKFDEIVefAELG-------DFIdqpvkTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA--FQk 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024481026 236 -VVSLMRSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 280
Cdd:COG1134 184 kCLARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMDG 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
76-285 |
9.13e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.78 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 76 RGYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNG-------RPRdLRTFRKMSCYIMQDDM 148
Cdd:PRK11831 17 RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-HGEILFDGenipamsRSR-LYTVRKRMSMLFQSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 149 LLPHLTVLE--AMMVSANLKLSEkqEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTS 226
Cdd:PRK11831 95 LFTDMNVFDnvAYPLREHTQLPA--PLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 227 GLDSASCFQVVSLMRSLAQG-GRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKGVVTNL 285
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSAlGVTCVVVSHD-VPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
97-256 |
9.21e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.03 E-value: 9.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 97 IMGPSGAGKSTLMNILAGY-RETgmKGQI------LVNG-RPRDLRTFRKMSCYIMQddmlLPHLTVLEAMMVS------ 162
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLlQPT--SGTVtigervITAGkKNKKLKPLRKKVGIVFQ----FPEHQLFEETVEKdicfgp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 163 ANLKLSEKQevKKELVNEILTALGLLECSYTRT-ISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMR 241
Cdd:PRK13634 112 MNFGVSEED--AKQKAREMIELVGLPEELLARSpFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFY 189
|
170
....*....|....*.
gi 2024481026 242 SLAQ-GGRTIICTIHQ 256
Cdd:PRK13634 190 KLHKeKGLTTVLVTHS 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
93-292 |
1.13e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.41 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKS----TLMNILAGYRETGMKGQILVNGRPRDLRTFRKMSCYIMQD----DM----------LLPHLT 154
Cdd:PRK10261 43 ETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHvrgaDMamifqepmtsLNPVFT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 155 VLEAMMVSANLKLSEKQEvkkELVNEILTALGLLECSYTRTI------SLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 228
Cdd:PRK10261 123 VGEQIAESIRLHQGASRE---EAMVEAKRMLDQVRIPEAQTIlsryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTAL 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024481026 229 DSASCFQVVSLMRSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLI-----PYLKGL 292
Cdd:PRK10261 200 DVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFhapqhPYTRAL 268
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
91-261 |
1.23e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.00 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 91 QRELIGIMGPSGAGKSTLMNILAGYRETGMKGQILVNGrprdlrtfrkmscyimqddmllphltvleammvsanlklsek 170
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 171 qevkkELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS------CFQVVSLMRSLA 244
Cdd:smart00382 39 -----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllLEELRLLLLLKS 113
|
170
....*....|....*..
gi 2024481026 245 QGGRTIICTIHQPSAKL 261
Cdd:smart00382 114 EKNLTVILTTNDEKDLG 130
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
79-297 |
1.41e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.33 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 79 KTLLKCLSGKFCQRELIGIMGPSGAGKSTL---MNILAgyreTGMKGQILVNG----RPRDLRTFRKMSCYIMQ--DDML 149
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL----IPSEGKVYVDGldtsDEENLWDIRNKAGMVFQnpDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 150 LPhlTVLEAMMVSANLKLSEKQEVKKELVNEILTALGLLEcsYTRTIS--LSGGQRKRLAIALELVNNPPVMFFDEPTSG 227
Cdd:PRK13633 99 VA--TIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYE--YRRHAPhlLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024481026 228 LDSASCFQVVSLMRSL-AQGGRTIICTIH--QPSAKLfemfDKLYILSQGQCIFKGVVTNL---IPYLKGLGLHCP 297
Cdd:PRK13633 175 LDPSGRREVVNTIKELnKKYGITIILITHymEEAVEA----DRIIVMDSGKVVMEGTPKEIfkeVEMMKKIGLDVP 246
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
79-257 |
2.20e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.05 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 79 KTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGyRETGMKGQilvngrprdlrtfrkmSCYIMQDDMLLPHLTVLEA 158
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-ALKGTPVA----------------GCVDVPDNQFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 159 mmvsanlkLSEKQEVKkeLVNEILTALGLLEC-SYTRTIS-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 236
Cdd:COG2401 106 --------IGRKGDFK--DAVELLNAVGLSDAvLWLRRFKeLSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180
....*....|....*....|..
gi 2024481026 237 VSLMRSLAQ-GGRTIICTIHQP 257
Cdd:COG2401 176 ARNLQKLARrAGITLVVATHHY 197
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
95-251 |
3.62e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 59.83 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 95 IGIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRprDLRTfrkmscyIMQDDM-----LLPHLTVL------------ 156
Cdd:COG5265 387 VAIVGPSGAGKSTLARLLFRfYDVTS--GRILIDGQ--DIRD-------VTQASLraaigIVPQDTVLfndtiayniayg 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 157 ---------EAMMVSANL-----KLSEKQEVkkeLVNEiltalgllecsytRTISLSGGQRKRLAIALELVNNPPVMFFD 222
Cdd:COG5265 456 rpdaseeevEAAARAAQIhdfieSLPDGYDT---RVGE-------------RGLKLSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180
....*....|....*....|....*....
gi 2024481026 223 EPTSGLDSASCFQVVSLMRSLAQGGRTII 251
Cdd:COG5265 520 EATSALDSRTERAIQAALREVARGRTTLV 548
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
79-280 |
4.58e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.05 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 79 KTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAG---YRETgmKGQILVN----------GRPrdlrTFRKMSC---- 141
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqYEPT--SGRIIYHvalcekcgyvERP----SKVGEPCpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 142 ---------YIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKKELVNE-----------ILTALGLLE---CSYTRT--- 195
Cdd:TIGR03269 87 gtlepeevdFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEAleeigyegkeaVGRAVDLIEmvqLSHRIThia 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 196 ISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQG 274
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEV-IEDLSDKAIWLENG 245
|
....*.
gi 2024481026 275 QCIFKG 280
Cdd:TIGR03269 246 EIKEEG 251
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
88-280 |
5.27e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 57.71 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 88 KFCQRELIGIMGPSGAGKSTLMNILAGY--RETGmkgQILVNG--------RPRDLRTFRKMSCYIMQDDMLLPHLTVLE 157
Cdd:PRK13645 33 TFKKNKVTCVIGTTGSGKSTMIQLTNGLiiSETG---QTIVGDyaipanlkKIKEVKRLRKEIGLVFQFPEYQLFQETIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 158 AMMVSANLKLSE-KQEVKKElVNEILTALGLLECSYTRT-ISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 235
Cdd:PRK13645 110 KDIAFGPVNLGEnKQEAYKK-VPELLKLVQLPEDYVKRSpFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEED 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024481026 236 VVSLMRSLAQG-GRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 280
Cdd:PRK13645 189 FINLFERLNKEyKKRIIMVTHNMD-QVLRIADEVIVMHEGKVISIG 233
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
96-285 |
1.02e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 96 GIMGPSGAGKSTLMNILAG-YRETGmkGQILVNGRPrdlRTFR--KMS-----CYIMQDDMLLPHLTVLEammvsaNLKL 167
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGiYTRDA--GSILYLGKE---VTFNgpKSSqeagiGIIHQELNLIPQLTIAE------NIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 168 SekqevkKELVNEI---------------LTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---D 229
Cdd:PRK10762 103 G------REFVNRFgridwkkmyaeadklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtdtE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024481026 230 SASCFQVVslmRSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKGVVTNL 285
Cdd:PRK10762 177 TESLFRVI---RELKSQGRGIVYISHR-LKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
93-283 |
1.04e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.57 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRE-TGMKGQILVNGR-----PRDLRTfrKMSCYI-MQDDMLLPHLTVLEAMMVSANL 165
Cdd:CHL00131 34 EIHAIMGPNGSGKSTLSKVIAGHPAyKILEGDILFKGEsildlEPEERA--HLGIFLaFQYPIEIPGVSNADFLRLAYNS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 166 KLSEKQEVKK------ELVNEILTALGLLECSYTRTIS--LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 237
Cdd:CHL00131 112 KRKFQGLPELdpleflEIINEKLKLVGMDPSFLSRNVNegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2024481026 238 SLMRSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQCIFKGVVT 283
Cdd:CHL00131 192 EGINKLMTSENSIILITHYQ--RLLDYIkpDYVHVMQNGKIIKTGDAE 237
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
93-245 |
1.99e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.86 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKS----TLMNIL-AGYRETGmkGQILVNGRPRDLRTFR-KMSCYIMQD--DMLLPHLTVleAMMVSAN 164
Cdd:PRK10418 30 RVLALVGGSGSGKSltcaAALGILpAGVRQTA--GRVLLDGKPVAPCALRgRKIATIMQNprSAFNPLHTM--HTHARET 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 165 LKLSEKQEVKKELVnEILTALGLLECSytRTISL-----SGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 239
Cdd:PRK10418 106 CLALGKPADDATLT-AALEAVGLENAA--RVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDL 182
|
....*.
gi 2024481026 240 MRSLAQ 245
Cdd:PRK10418 183 LESIVQ 188
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
427-640 |
2.84e-08 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 54.44 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 427 MLFLMFAALMPTILTFPQEMSV-FLREHLNYWYSLKAYYLAKTMADVPFQVICPIAYCSIVYWMTGQPPEATRFLLFSAL 505
Cdd:COG0842 11 AMSLLFTALMLTALSIAREREQgTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLLLLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 506 ATATALVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYVSYVRYGFEGVILTIYAmered 585
Cdd:COG0842 91 LLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRALFLG----- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 586 lecledfcpfqkpikilqelDVEEAKLYLDFLILGIFFIILRLLAYLVLRYKVKS 640
Cdd:COG0842 166 --------------------GAGLADVWPSLLVLLAFAVVLLALALRLFRRRLRG 200
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
94-256 |
2.91e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 94 LIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGR--PRDLRTFRKMSCYIMQDDMLLPHLTVLEAMMV-----SANL 165
Cdd:PRK13540 29 LLHLKGSNGAGKTTLLKLIAGlLNPE--KGEILFERQsiKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYdihfsPGAV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 166 KLSEKQEVKKeLVNEILTALGLLecsytrtislSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQ 245
Cdd:PRK13540 107 GITELCRLFS-LEHLIDYPCGLL----------SSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRA 175
|
170
....*....|.
gi 2024481026 246 GGRTIICTIHQ 256
Cdd:PRK13540 176 KGGAVLLTSHQ 186
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
93-280 |
3.41e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.64 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRPrdlrtfrkmsCYIMQDDMLLPHLTVLEAM------MVSANLK 166
Cdd:PRK10789 342 QMLGICGPTGSGKSTLLSLIQRHFDVS-EGDIRFHDIP----------LTKLQLDSWRSRLAVVSQTpflfsdTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 167 L------SEKQEVKKELVN---EIL-------TALGllecsyTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 230
Cdd:PRK10789 411 LgrpdatQQEIEHVARLASvhdDILrlpqgydTEVG------ERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024481026 231 ASCFQVVSLMRSLAQgGRTIICTIHQPSAkLFEMfDKLYILSQGQCIFKG 280
Cdd:PRK10789 485 RTEHQILHNLRQWGE-GRTVIISAHRLSA-LTEA-SEILVMQHGHIAQRG 531
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
77-255 |
4.37e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.99 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 77 GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYReTGMKGQILVNGRPRDLRTFRKMSCYI--MQDDMLLPHLT 154
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-TPAHGHVWLDGEHIQHYASKEVARRIglLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 155 VLEAMMVSANLK----LSEKQEVKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 230
Cdd:PRK10253 97 TVQELVARGRYPhqplFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180
....*....|....*....|....*.
gi 2024481026 231 ASCFQVVSLMRSL-AQGGRTIICTIH 255
Cdd:PRK10253 177 SHQIDLLELLSELnREKGYTLAAVLH 202
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
82-230 |
5.88e-08 |
|
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: 54.34 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 82 LKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGyRETGMKGQILVngrprDLRTFRKMSCYIMQD-DMllphlTVLEAMM 160
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAG-VLKPDEGDIEI-----ELDTVSYKPQYIKADyEG-----TVRDLLS 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 161 VSANLKLSEKQevkkeLVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 230
Cdd:cd03237 84 SITKDFYTHPY-----FKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
62-255 |
7.02e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 54.25 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 62 DLSYSVREGSWwrkrgyktllkclsgkfcqrelIGIMGPSGAGKSTLMNILAG-YRETgmKGQILVNGRPRDLRT---FR 137
Cdd:PRK13635 25 DVSFSVYEGEW----------------------VAIVGHNGSGKSTLAKLLNGlLLPE--AGTITVGGMVLSEETvwdVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 138 KMSCYIMQD-DMLLPHLTV-------LEammvsaNLKLSEKQEVKKelVNEILTALGLLECSYTRTISLSGGQRKRLAIA 209
Cdd:PRK13635 81 RQVGMVFQNpDNQFVGATVqddvafgLE------NIGVPREEMVER--VDQALRQVGMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2024481026 210 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL-AQGGRTIICTIH 255
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITH 199
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
196-271 |
9.45e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.98 E-value: 9.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 196 ISLSGGQRKRLAIALEL----VNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPsaKLFEMFDKLYIL 271
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLIHI 153
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
93-251 |
1.52e-07 |
|
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: 54.41 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGyRETGMKGQIlvngrPRDLRTFRKMScYIMQD-DMllphlTVLEAMMVSANLKLSEKQ 171
Cdd:COG1245 367 EVLGIVGPNGIGKTTFAKILAG-VLKPDEGEV-----DEDLKISYKPQ-YISPDyDG-----TVEEFLRSANTDDFGSSY 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 172 evkkeLVNEILTALGL---LECSYTrtiSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG-G 247
Cdd:COG1245 435 -----YKTEIIKPLGLeklLDKNVK---DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrG 506
|
....
gi 2024481026 248 RTII 251
Cdd:COG1245 507 KTAM 510
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
93-245 |
1.76e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 54.31 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKS-TLMNI--LAGYRETGMKGQILVNGR------PRDLRTFR--KMSCyIMQDDM--LLPHLTV---- 155
Cdd:COG4172 37 ETLALVGESGSGKSvTALSIlrLLPDPAAHPSGSILFDGQdllglsERELRRIRgnRIAM-IFQEPMtsLNPLHTIgkqi 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 156 LEAMMVSANLKlseKQEVKKELVnEILTALGLLECSytRTIS-----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD- 229
Cdd:COG4172 116 AEVLRLHRGLS---GAAARARAL-ELLERVGIPDPE--RRLDayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDv 189
|
170
....*....|....*...
gi 2024481026 230 --SAscfQVVSLMRSLAQ 245
Cdd:COG4172 190 tvQA---QILDLLKDLQR 204
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
97-229 |
2.81e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.64 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 97 IMGPSGAGKSTLMNILAGYRETgMKGQILVNGRPRDL---RTFRKMSCYIMQDDMLLPHlTVLEammvsaNLKLS---EK 170
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISP-TSGTLLFEGEDISTlkpEIYRQQVSYCAQTPTLFGD-TVYD------NLIFPwqiRN 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 171 QEVKKELVNEILTALGLLECSYTRTIS-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:PRK10247 110 QQPDPAIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
93-229 |
2.87e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILagyreTGM----KGQILVNGRP---RDLRTFRK---MScyimQDDMLLPHLTVLEAMMVS 162
Cdd:NF033858 293 EIFGFLGSNGCGKSTTMKML-----TGLlpasEGEAWLFGQPvdaGDIATRRRvgyMS----QAFSLYGELTVRQNLELH 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024481026 163 ANL-KLSEKQevKKELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:NF033858 364 ARLfHLPAAE--IAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
196-264 |
3.58e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.09 E-value: 3.58e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024481026 196 ISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQgGRTIICTIH--QPSAKLFEM 264
Cdd:PRK14243 150 LSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHnmQQAARVSDM 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
91-275 |
4.31e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.04 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 91 QRELIGIMGPSGAGKSTLMNILAGYRETGmKGQILVNGRPR------DLRtfRKMSCYIMQDDMLLPHLTVLEAMMVSAN 164
Cdd:PRK13650 32 QGEWLSIIGHNGSGKSTTVRLIDGLLEAE-SGQIIIDGDLLteenvwDIR--HKIGMVFQNPDNQFVGATVEDDVAFGLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 165 LKLSEKQEVKkELVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLA 244
Cdd:PRK13650 109 NKGIPHEEMK-ERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIR 187
|
170 180 190
....*....|....*....|....*....|....
gi 2024481026 245 QG-GRTIICTIHQpsakLFE--MFDKLYILSQGQ 275
Cdd:PRK13650 188 DDyQMTVISITHD----LDEvaLSDRVLVMKNGQ 217
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
91-292 |
6.30e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.67 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 91 QRELIGIMGPSGAGKS----TLMNiLAGYRETGMKGQILVNGRprDLRTF-----RKMS----CYIMQDDM--LLPHLTV 155
Cdd:PRK11022 32 QGEVVGIVGESGSGKSvsslAIMG-LIDYPGRVMAEKLEFNGQ--DLQRIsekerRNLVgaevAMIFQDPMtsLNPCYTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 156 LEAMMVSANLKLSEKQEVKKELVNEILTALGLLECSYTRTI---SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 232
Cdd:PRK11022 109 GFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 233 CFQVVSLMRSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLI-----PYLKGL 292
Cdd:PRK11022 189 QAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFraprhPYTQAL 253
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
87-248 |
8.60e-07 |
|
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: 49.49 E-value: 8.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 87 GKFCQRELIGIMGPSGAGKSTLMNILAGYREtgmkgqilvngrPRDlrtfrkmscyimqDDMLLPHLTVLeammvsanlk 166
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGQLI------------PNG-------------DNDEWDGITPV---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 167 lsekqeVKKElvneiltalgllecsytrTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQG 246
Cdd:cd03222 65 ------YKPQ------------------YIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
..
gi 2024481026 247 GR 248
Cdd:cd03222 121 GK 122
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
82-243 |
9.03e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.86 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 82 LKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRE-----TGMKGQILVNGRPRDLRtfRKMSCYIMQDDMLLPHLTVL 156
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEefegkVKIDGELLTAENVWNLR--RKIGMVFQNPDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 157 EAMMVSANLKLSEKQEVKKElVNEILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 236
Cdd:PRK13642 101 DDVAFGMENQGIPREEMIKR-VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
....*..
gi 2024481026 237 VSLMRSL 243
Cdd:PRK13642 180 MRVIHEI 186
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
91-229 |
9.26e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 91 QRELIGIMGPSGAGKSTLMNILAGyRETGMKGQILVngrprDLRTFRKMScYIMQDdmllPHLTVlEAMMVSANLKLSEK 170
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAG-VLKPDEGEVDP-----ELKISYKPQ-YIKPD----YDGTV-EDLLRSITDDLGSS 431
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024481026 171 QevkkeLVNEILTALGL---LECSYTrtiSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:PRK13409 432 Y-----YKSEIIKPLQLerlLDKNVK---DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
95-255 |
1.60e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 95 IGIMGPSGAGKSTLMNILAG---------YRETGMK-GqilvngrprdlrtfrkmscYIMQDDMLLPHLTVLEAMMVSan 164
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGvdkefegeaRPAPGIKvG-------------------YLPQEPQLDPEKTVRENVEEG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 165 lkLSEKQEVKKELvNEILTALGLLECSYTRTI---------------------------------------SLSGGQRKR 205
Cdd:PRK11819 95 --VAEVKAALDRF-NEIYAAYAEPDADFDALAaeqgelqeiidaadawdldsqleiamdalrcppwdakvtKLSGGERRR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024481026 206 LAIALELVNNPPVMFFDEPTSGLDSAScfqVVSLMRSLAQGGRTIICTIH 255
Cdd:PRK11819 172 VALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDYPGTVVAVTH 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
77-246 |
2.27e-06 |
|
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: 50.70 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 77 GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGyRETGMKGQILVnGRPRDLrtfrkmsCYIMQD-DMLLPHLTV 155
Cdd:TIGR03719 333 GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG-QEQPDSGTIEI-GETVKL-------AYVDQSrDALDPNKTV 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 156 LEA-------MMV------------SANLKLSEKQevKKelVNEiltalgllecsytrtisLSGGQRKRLAIALELVNNP 216
Cdd:TIGR03719 404 WEEisggldiIKLgkreipsrayvgRFNFKGSDQQ--KK--VGQ-----------------LSGGERNRVHLAKTLKSGG 462
|
170 180 190
....*....|....*....|....*....|
gi 2024481026 217 PVMFFDEPTSGLDsascfqvVSLMRSLAQG 246
Cdd:TIGR03719 463 NVLLLDEPTNDLD-------VETLRALEEA 485
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
77-229 |
2.43e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.34 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 77 GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETGmKGQILvngRPRDLRTfrkmsCYIMQD---DMLLPhL 153
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD-EGVIK---RNGKLRI-----GYVPQKlylDTTLP-L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 154 TVLEAMMVSANlklsekqeVKKElvnEILTALG------LLECSYTRtisLSGGQRKRLAIALELVNNPPVMFFDEPTSG 227
Cdd:PRK09544 85 TVNRFLRLRPG--------TKKE---DILPALKrvqaghLIDAPMQK---LSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
..
gi 2024481026 228 LD 229
Cdd:PRK09544 151 VD 152
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
97-277 |
2.65e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 97 IMGPSGAGKSTLMNILAGYRETG-MKGQILVNGRPRDLRTFR----KMSCYIMQDDMLLPHLTVLEammvsaNLKLSEKQ 171
Cdd:NF040905 32 LCGENGAGKSTLMKVLSGVYPHGsYEGEILFDGEVCRFKDIRdseaLGIVIIHQELALIPYLSIAE------NIFLGNER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 172 eVKKELVN---------EILTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSAscfQVVSL 239
Cdd:NF040905 106 -AKRGVIDwnetnrrarELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneeDSA---ALLDL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2024481026 240 MRSL-AQGGRTIIctIhqpSAKLFEMF---DKLYILSQGQCI 277
Cdd:NF040905 182 LLELkAQGITSII--I---SHKLNEIRrvaDSITVLRDGRTI 218
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
197-275 |
2.73e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 2.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024481026 197 SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIIcTIHQPSAKLFEMFDKLYILSQGQ 275
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII-IISSEMPELLGITDRILVMSNGL 468
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
93-275 |
2.84e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTL-MNILAGYRETGMKGQILVNGRPRDLRTF--------------RKMSCYIMQDDML----LPHL 153
Cdd:NF040905 287 EIVGIAGLMGAGRTELaMSVFGRSYGRNISGTVFKDGKEVDVSTVsdaidaglayvtedRKGYGLNLIDDIKrnitLANL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 154 TvleamMVSANLKLSEKQEVKkeLVNEILTALGLLECS-YTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 232
Cdd:NF040905 367 G-----KVSRRGVIDENEEIK--VAEEYRKKMNIKTPSvFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGA 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024481026 233 CFQVVSLMRSLAQGGRTIIcTIhqpSAKLFE---MFDKLYILSQGQ 275
Cdd:NF040905 440 KYEIYTIINELAAEGKGVI-VI---SSELPEllgMCDRIYVMNEGR 481
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
60-275 |
7.25e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 60 FIDLSYSVREGswwrkrgyktllkclsgkfcqrELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRprdlrTFRKM 139
Cdd:PRK15439 279 FRNISLEVRAG----------------------EILGLAGVVGAGRTELAETLYGLRPA-RGGRIMLNGK-----EINAL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 140 SCYIMQDDML--LP-----HLTVLEAMM---VSA------NLKLSEKQEvkKELVNEILTALGLlECSY----TRTisLS 199
Cdd:PRK15439 331 STAQRLARGLvyLPedrqsSGLYLDAPLawnVCAlthnrrGFWIKPARE--NAVLERYRRALNI-KFNHaeqaART--LS 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024481026 200 GGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTihqpSAKLFE---MFDKLYILSQGQ 275
Cdd:PRK15439 406 GGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFI----SSDLEEieqMADRVLVMHQGE 480
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
78-232 |
9.60e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 9.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 78 YKTL-LKCLSGKfcqreLIGIMGPSGAGKSTLMNILAGY------------------------------RETGMK----- 121
Cdd:PTZ00265 1184 YKDLtFSCDSKK-----TTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgdeeQNVGMKnvnef 1258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 122 ------------------GQILVNGR---PRDLRTFRKMSCYIMQDDMLLpHLTVLEAMM----------VSANLKLSEK 170
Cdd:PTZ00265 1259 sltkeggsgedstvfknsGKILLDGVdicDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKfgkedatredVKRACKFAAI 1337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024481026 171 QEVKKELVNEILTALGllecSYTRtiSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 232
Cdd:PTZ00265 1338 DEFIESLPNKYDTNVG----PYGK--SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
93-245 |
1.02e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKS----TLMNILAGYRETGMKGQILVNGRP------RDLRTFR--KMScYIMQDdmllPhltvleamM 160
Cdd:PRK15134 36 ETLALVGESGSGKSvtalSILRLLPSPPVVYPSGDIRFHGESllhaseQTLRGVRgnKIA-MIFQE----P--------M 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 161 VSAN-LKLSEKQ--EV--------KKELVNEILTAL---GLLECSytRTIS-----LSGGQRKRLAIALELVNNPPVMFF 221
Cdd:PRK15134 103 VSLNpLHTLEKQlyEVlslhrgmrREAARGEILNCLdrvGIRQAA--KRLTdyphqLSGGERQRVMIAMALLTRPELLIA 180
|
170 180
....*....|....*....|....
gi 2024481026 222 DEPTSGLDSASCFQVVSLMRSLAQ 245
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQ 204
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
93-256 |
1.05e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 46.94 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 93 ELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRPRDLRTF-------RKMSCYIMQDDMLLpHLTVLEAMMVSANL 165
Cdd:cd03290 28 QLTMIVGQVGCGKSSLLLAILGEMQT-LEGKVHWSNKNESEPSFeatrsrnRYSVAYAAQKPWLL-NATVEENITFGSPF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 166 KlseKQEVKK-----ELVNEI-LTALGLLECSYTRTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD---SASCFQv 236
Cdd:cd03290 106 N---KQRYKAvtdacSLQPDIdLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDihlSDHLMQ- 181
|
170 180
....*....|....*....|
gi 2024481026 237 VSLMRSLAQGGRTIICTIHQ 256
Cdd:cd03290 182 EGILKFLQDDKRTLVLVTHK 201
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
197-258 |
2.66e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.01 E-value: 2.66e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024481026 197 SLSGGQRKRLAIALEL-VNNPPVMF-FDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPS 258
Cdd:cd03238 87 TLSGGELQRVKLASELfSEPPGTLFiLDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
46-258 |
3.56e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.81 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 46 RFSHLPKRSAVNIEFIDlsySVREGSWWRKRG-YKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETGmKGQI 124
Cdd:PRK13545 6 KFEHVTKKYKMYNKPFD---KLKDLFFRSKDGeYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPN-KGTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 125 LVNGRprdlrtfrkmSCYIMQDDMLLPHLTVLEAMMVSAnLKLSEKQEVKKELVNEILTALGLLECSYTRTISLSGGQRK 204
Cdd:PRK13545 82 DIKGS----------AALIAISSGLNGQLTGIENIELKG-LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024481026 205 RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPS 258
Cdd:PRK13545 151 RLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLS 204
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
97-229 |
5.18e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 97 IMGPSGAGKSTLMNILAGYRETGMKGQILVNGRPR-------DLRtfRKMScYIMQDdmllPHLTvleaMMVSANLK--- 166
Cdd:PRK10938 291 IVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGRRRgsgetiwDIK--KHIG-YVSSS----LHLD----YRVSTSVRnvi 359
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024481026 167 -------------LSEKQEVkkeLVNEILTALGLLECSYTRTI-SLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 229
Cdd:PRK10938 360 lsgffdsigiyqaVSDRQQK---LAQQWLDILGIDKRTADAPFhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-258 |
6.69e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 131 RDLRTFRKMSCYIMQDDMLlPHLTVLEAMMVSANLKLSEKQEV----KKELVNEILTAL-----GLLECSYTRtisLSGG 201
Cdd:PTZ00265 508 KNKRNSCRAKCAGDLNDMS-NTTDSNELIEMRKNYQTIKDSEVvdvsKKVLIHDFVSALpdkyeTLVGSNASK---LSGG 583
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024481026 202 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSL-AQGGRTIICTIHQPS 258
Cdd:PTZ00265 584 QKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLS 641
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
180-255 |
9.51e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 180 EILTALGLLECSYTRTI-SLSGGQRKRLAIALELVN---NPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIH 255
Cdd:PRK00635 791 HALCSLGLDYLPLGRPLsSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
194-274 |
1.05e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.74 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 194 RTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV-SLMRSLAQGGRTIICT--IHqpsakLFEMFDKLYI 270
Cdd:PLN03232 737 RGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdSCMKDELKGKTRVLVTnqLH-----FLPLMDRIIL 811
|
....
gi 2024481026 271 LSQG 274
Cdd:PLN03232 812 VSEG 815
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
255-312 |
1.67e-04 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 44.51 E-value: 1.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024481026 255 HQPSAKLFEMFDKLYILSQGQCI-FKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASG 312
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTvYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEG 59
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
95-275 |
2.10e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 95 IGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRPRdLRTFRKMSCyimqDDMLLPHLTVLEAMMVSANLKlseKQEVK 174
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQP-SSGTVFRSAKVR-MAVFSQHHV----DGLDLSSNPLLYMMRCFPGVP---EQKLR 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 175 KELVNEILTALGLLECSYTrtisLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAScfqVVSLMRSLA--QGGrtiIC 252
Cdd:PLN03073 609 AHLGSFGVTGNLALQPMYT----LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVlfQGG---VL 678
|
170 180
....*....|....*....|...
gi 2024481026 253 TIHQPSAKLFEMFDKLYILSQGQ 275
Cdd:PLN03073 679 MVSHDEHLISGSVDELWVVSEGK 701
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
198-302 |
2.81e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.64 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 198 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCI 277
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90 100 110
....*....|....*....|....*....|
gi 2024481026 278 FKGVVTNLI-----PYLKGLGLHCPTYHNP 302
Cdd:PRK15093 239 ETAPSKELVttphhPYTQALIRAIPDFGSA 268
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
197-269 |
4.75e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.82 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 197 SLSGGQRK------RLAIALELVNNPPVMFFDEPTSGLDSASC-FQVVSLMRS-LAQGGRTIICTIHQPsaKLFEMFDKL 268
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIeESLAEIIEErKSQKNFQLIVITHDE--ELVDAADHI 192
|
.
gi 2024481026 269 Y 269
Cdd:cd03240 193 Y 193
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
92-244 |
6.25e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.53 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 92 RELIGIMGPSGAGKSTLMN-ILAG-YRETGMKGQIlvngrPRDLRTFRKMSCYI---------------MQDDML----- 149
Cdd:COG0419 23 DGLNLIVGPNGAGKSTILEaIRYAlYGKARSRSKL-----RSDLINVGSEEASVelefehggkryrierRQGEFAeflea 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 150 -----------LPHLTVLEAMMVSANlKLSEKQEVKKELVNEILTA----LGLLEcSYTRTISLSGGQRKRLAIAlELVN 214
Cdd:COG0419 98 kpserkealkrLLGLEIYEELKERLK-ELEEALESALEELAELQKLkqeiLAQLS-GLDPIETLSGGERLRLALA-DLLS 174
|
170 180 190
....*....|....*....|....*....|
gi 2024481026 215 nppvMFFDepTSGLDSASCFQVVSLMRSLA 244
Cdd:COG0419 175 ----LILD--FGSLDEERLERLLDALEELA 198
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
67-149 |
6.57e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 67 VREGSWWRKR-GYKTLLKCLSGKFCQRELIGIMGPSGAGKSTLMNILAGYRETgMKGQILVNGRP---RDLRTFRKMSCY 142
Cdd:PTZ00243 1310 VFEGVQMRYReGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEV-CGGEIRVNGREigaYGLRELRRQFSM 1388
|
....*..
gi 2024481026 143 IMQDDML 149
Cdd:PTZ00243 1389 IPQDPVL 1395
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
197-258 |
1.02e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 1.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024481026 197 SLSGGQRK---RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIHQPS 258
Cdd:pfam13304 236 ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
194-251 |
1.56e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 1.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024481026 194 RTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTII 251
Cdd:PRK10938 132 RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLV 189
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
197-255 |
1.61e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 1.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024481026 197 SLSGGQRKRLAIALEL---VNNPPVMFFDEPTSGLDSASCFQVVSLMRSLAQGGRTIICTIH 255
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
79-292 |
2.01e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 40.28 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 79 KTLLKCLSGKFCQRELIGIMGPSGAGKSTLMniLAGYRETGM-KGQILVNG---RPRDLRTFRKMSCYIMQDDMLLPHLT 154
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIfDGKIVIDGidiSKLPLHTLRSRLSIILQDPILFSGSI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 155 V--LEAMMVSANLKLSEKQEVKkELVNEILTALGLLECSYTRT-ISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 231
Cdd:cd03288 112 RfnLDPECKCTDDRLWEALEIA-QLKNMVKSLPGGLDAVVTEGgENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024481026 232 S--CFQVVsLMRSLAQggRTIICTIHQPSAKLFEmfDKLYILSQGQCIFKGVVTNLIPYLKGL 292
Cdd:cd03288 191 TenILQKV-VMTAFAD--RTVVTIAHRVSTILDA--DLVLVLSRGILVECDTPENLLAQEDGV 248
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
80-136 |
3.94e-03 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 39.47 E-value: 3.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024481026 80 TLLKCLSGkfcQRelIGIMGPSGAGKSTLMNILAGYRETGMKGQILVNGRPRDLRTF 136
Cdd:cd01136 60 GLLTCGEG---QR--IGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGREVREF 111
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
77-119 |
4.08e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 4.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2024481026 77 GYKTLLKCLSGKfcqreLIGIMGPSGAGKSTLMNILAG--YRETG 119
Cdd:cd01854 75 GLDELRELLKGK-----TSVLVGQSGVGKSTLLNALLPelVLATG 114
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
94-113 |
5.87e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 38.25 E-value: 5.87e-03
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
94-113 |
7.99e-03 |
|
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.
Pssm-ID: 238977 [Multi-domain] Cd Length: 69 Bit Score: 35.39 E-value: 7.99e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
171-287 |
8.11e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024481026 171 QEVKKELVNE--ILTALGLLECSYTRTI-SLSGGQRKRLAIA----LELVNnppVMF-FDEPTSGLDSASCFQVVSLMRS 242
Cdd:PRK00635 447 EEVLQGLKSRlsILIDLGLPYLTPERALaTLSGGEQERTALAkhlgAELIG---ITYiLDEPSIGLHPQDTHKLINVIKK 523
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2024481026 243 LAQGGRTIICTIHQpsAKLFEMFDKLYILSQGQCIFKG-VVTNLIP 287
Cdd:PRK00635 524 LRDQGNTVLLVEHD--EQMISLADRIIDIGPGAGIFGGeVLFNGSP 567
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
194-236 |
8.78e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.34 E-value: 8.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2024481026 194 RTISLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 236
Cdd:PLN03130 737 RGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV 779
|
|
| |
