|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
44-646 |
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: 627.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 44 ITEAQRFSHLPKRSAVDIEfVELSYSVREGPCWRKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGM 123
Cdd:TIGR00955 1 LTYSWRNSDVFGRVAQDGS-WKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 124 KGQ--ILVNGKPRELRTFRKMSCYIMQEDILLPHLTVLEAMMISANLKLNEK--QEVKKELVTEILTALGLLSCSHTRTA 199
Cdd:TIGR00955 80 KGSgsVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRvtKKEKRERVDEVLQALGLRKCANTRIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 200 L------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYI 273
Cdd:TIGR00955 160 VpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 274 LSQGQCIFKGMVTNLIPYLKGLGLHCPTYHNPADFIIEVASGEYGDLNPLlfRAVQNGLCAMAEKNSGPEKNEVPT---- 349
Cdd:TIGR00955 240 MAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGSENES--RERIEKICDSFAVSDIGRDMLVNTnlws 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 350 -LCPPCPLEVDTIESHTFATSTLTQFCILFKRSFLSVLRDMVLTHLRFISHAVIGVLIGLLYLQTGNDANKVLNNTGCLF 428
Cdd:TIGR00955 318 gKAGGLVKDSENMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 429 FSILFLMFAAMMPTVLTFPLEMAVFLREHLNYWYSLKIYFLAKTMADVPFQVICPAVYCSIMYWMTSQPAETSRFLLFLA 508
Cdd:TIGR00955 398 LFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 509 LGASTALAAQSLGMLIGAASSSLQVATFLGPVTAIPVLLFSGFFVSFKAIPSYLQWSSYLSYVRYGFEGVILTIYGmGRE 588
Cdd:TIGR00955 478 LVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWS-DVD 556
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157427812 589 DLSCL----TEHCPFQKpENILRAMDVEDGKLYVDFLALGIFFLLLRLLAYLVLRYRIKSKR 646
Cdd:TIGR00955 557 NIECTsantTGPCPSSG-EVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
58-283 |
2.10e-92 |
|
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: 283.67 E-value: 2.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 58 AVDIEFVELSYSVREgpcWRKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKS-GMKGQILVNGKPREL 136
Cdd:cd03213 1 GVTLSFRNLTVTVKS---SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlGVSGEVLINGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 137 RTFRKMSCYIMQEDILLPHLTVLEAMMISANLKlnekqevkkelvteiltalGLlscshtrtallSGGQRKRLAIALELV 216
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------GL-----------SGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157427812 217 NNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
82-593 |
8.30e-81 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 268.67 E-value: 8.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 82 KTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAG-YRKSGMKGQILVNGKPRELRTFRKMScYIMQEDILLPHLTVLE 160
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFTGTILANNRKPTKQILKRTG-FVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 161 AMMISANLKLNEK--QEVKKELVTEILTALGLLSCSHTRTAL-----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:PLN03211 160 TLVFCSLLRLPKSltKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 234 ASSFQVASLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGMVTNLIPYLKGLGLHCPTYHNPADFIIEVA 313
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 314 SGE------------------YGDLNPLLfrAVQNGLCAMAEKNSGPEKNEVPTLCPPCPLEVDTIESHTFatstLTQFC 375
Cdd:PLN03211 320 NGVcqtdgvserekpnvkqslVASYNTLL--APKVKAAIEMSHFPQANARFVGSASTKEHRSSDRISISTW----FNQFS 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 376 ILFKRSfLSVLRDMVLTHLRFISHAVIGVLIGLLYLQTgnDANKVLNNTGCLFFSILFLMFAAMMPTVLTFPLEMAVFLR 455
Cdd:PLN03211 394 ILLQRS-LKERKHESFNTLRVFQVIAAALLAGLMWWHS--DFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVK 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 456 EHLNYWYSLKIYFLAKTMADVPFQVICPAVYCSIMYWMTSQPAETSRFLLFLALGASTALAAQSLGMLIGAASSSLQVAT 535
Cdd:PLN03211 471 ERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKAS 550
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 157427812 536 FLGPVTAIPVLLFSGFFVSfkAIPSYLQWSSYLSYVRYGFEGVILTIYGMGREDLSCL 593
Cdd:PLN03211 551 TIVTVTMLAFVLTGGFYVH--KLPSCMAWIKYISTTFYSYRLLINVQYGEGKRISSLL 606
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
78-584 |
4.61e-66 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 236.16 E-value: 4.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 78 KRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGM--KGQILVNGKPRElRTFRKMSCYIMQEDILLPH 155
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitGGDRLVNGRPLD-SSFQRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 156 LTVLEAMMISANLKLNEK--QEVKKELVTEILTALGLLSCSHTRTAL----LSGGQRKRLAIALELVNNPP-VMFFDEPT 228
Cdd:TIGR00956 851 STVRESLRFSAYLRQPKSvsKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKlLLFLDEPT 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 229 SGLDSASSFQVASLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQG-QCIFKGMV----TNLIPYLKGLGLH-CPTY 302
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGDLgensHTIINYFEKHGAPkCPED 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 303 HNPADFIIEVASGEYGD----------LNPLLFRAVQNGLCAMAEKNSG-PEKNEVPTLcppcplevdtiesHTFATSTL 371
Cdd:TIGR00956 1011 ANPAEWMLEVIGAAPGAhanqdyhevwRNSSEYQAVKNELDRLEAELSKaEDDNDPDAL-------------SKYAASLW 1077
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 372 TQFCILFKRSFLSVLRDMVLTHLRFISHAVIGVLIGLLYLQTGNDANKVLNNTGCLFFSILFL--MFAAMMPTVLTfpLE 449
Cdd:TIGR00956 1078 YQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGTSLQGLQNQMFAVFMATVLFnpLIQQYLPPFVA--QR 1155
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 450 MAVFLREHLNYWYSLKIYFLAKTMADVPFQVICPAVYCSIMYWM-------TSQPAETSRFLLFLALGASTALAAQSLGM 522
Cdd:TIGR00956 1156 DLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPvgfywnaSKTGQVHERGVLFWLLSTMFFLYFSTLGQ 1235
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157427812 523 LIGAASSSLQVATFLGPVTAIPVLLFSGFFVSFKAIPSYLQWSSYLSYVRYGFEGVILTIYG 584
Cdd:TIGR00956 1236 MVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLA 1297
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
77-283 |
2.14e-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: 204.04 E-value: 2.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 77 RKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAG-YRKSGMK-GQILVNGKPRELRTFRKMSCYIMQEDILLP 154
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGTTsGQILFNGQPRKPDQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 155 HLTVLEAMMISANLKLNEKQ---EVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 231
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSsdaIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 157427812 232 DSASSFQVASLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
84-584 |
1.38e-58 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 213.94 E-value: 1.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 84 LLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGyRKSG--MKGQILVNGKPRELRTFRKMSCYIMQEDILLPHLTVLEA 161
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG-RKTGgyIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 162 MMISANLKLneKQEVKKE----LVTEILTALGLLSCSHTRTAL-----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PLN03140 974 LIYSAFLRL--PKEVSKEekmmFVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 233 SASSFQVASLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQ-GQCIFKGMV----TNLIPYLKGL-GL-HCPTYHNP 305
Cdd:PLN03140 1052 ARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLgrnsHKIIEYFEAIpGVpKIKEKYNP 1131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 306 ADFIIEVASGEyGDLNPLLFRAVQNGLCAMAEKNsgpeKNEVPTLCPPCPLEVDTIESHTFATSTLTQFCILFKRSFLSV 385
Cdd:PLN03140 1132 ATWMLEVSSLA-AEVKLGIDFAEHYKSSSLYQRN----KALVKELSTPPPGASDLYFATQYSQSTWGQFKSCLWKQWWTY 1206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 386 LRDMVLTHLRFISHAVIGVLIGLLYLQTG---NDANKVLNNTGCLFFSILFLMFAAMMPTVLTFPLEMAVFLREHLNYWY 462
Cdd:PLN03140 1207 WRSPDYNLVRFFFTLAAALMVGTIFWKVGtkrSNANDLTMVIGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAAGMY 1286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 463 SLKIYFLAKTMADVPFQVICPAVYCSIMYWMTSQPAETSRFLLFLALGASTALAAQSLGMLIGAASSSLQVATFLGPVTA 542
Cdd:PLN03140 1287 SALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFY 1366
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 157427812 543 IPVLLFSGFFVSFKAIPSYLQWSSYLSYVRYGFEGVILTIYG 584
Cdd:PLN03140 1367 GLFNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQYG 1408
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
61-283 |
3.51e-55 |
|
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: 186.29 E-value: 3.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 61 IEFVELSYSVREgpcwrKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSG-MKGQILVNGKPRElRTF 139
Cdd:cd03232 4 LTWKNLNYTVPV-----KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvITGEILINGRPLD-KNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 140 RKMSCYIMQEDILLPHLTVLEAMMISANLKlnekqevkkelvteiltalGLlscshtrtallSGGQRKRLAIALELVNNP 219
Cdd:cd03232 78 QRSTGYVEQQDVHSPNLTVREALRFSALLR-------------------GL-----------SVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157427812 220 PVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQ-GQCIFKG 283
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
377-579 |
2.74e-52 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 178.62 E-value: 2.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 377 LFKRSFLSVLRDMVLTHLRFISHAVIGVLIGLLYLQTGNDANkVLNNTGCLFFSILFLMFAAMMPTVLTFPLEMAVFLRE 456
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQG-GLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 457 HLNYWYSLKIYFLAKTMADVPFQVICPAVYCSIMYWMTSQPAETSRFLLFLALGASTALAAQSLGMLIGAASSSLQVATF 536
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 157427812 537 LGPVTAIPVLLFSGFFVSFKAIPSYLQWSSYLSYVRYGFEGVI 579
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALR 202
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
77-579 |
3.38e-50 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 188.78 E-value: 3.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 77 RKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLA----GYRKsGMKGQILVNGKPRE--LRTFRKMSCYIMQED 150
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHI-GVEGVITYDGITPEeiKKHYRGDVVYNAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 151 ILLPHLTVLEAMMISANLK-------LNEKQEVKKELVTEILTALGLlscSHTRTAL--------LSGGQRKRLAIALEL 215
Cdd:TIGR00956 148 VHFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKHIADVYMATYGL---SHTRNTKvgndfvrgVSGGERKRVSIAEAS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 216 VNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ-GGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGMVTNLIPYLKG 294
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEK 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 295 LGLHCPTYHNPADFIIEVAS-------GEYGDLNPL-------LFRAVQNGLCAMAEKNSGPEKNEVPTlcppcplEVDT 360
Cdd:TIGR00956 305 MGFKCPDRQTTADFLTSLTSpaerqikPGYEKKVPRtpqefetYWRNSPEYAQLMKEIDEYLDRCSESD-------TKEA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 361 I-ESH-------TFATSTLT-----QFCILFKRSFLSVLRDMVLTHLRFISHAVIGVLIGLLYLQTGNDANKVLNNTGCL 427
Cdd:TIGR00956 378 YrESHvakqskrTRPSSPYTvsfsmQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGAL 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 428 FFSILFLMFAAMMPTVLTFplEMAVFLREHLNY-WYSLKIYFLAKTMADVPFQVICPAVYCSIMYWMTSQPAETSRFLLF 506
Cdd:TIGR00956 458 FFAILFNAFSSLLEIASMY--EARPIVEKHRKYaLYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFY 535
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157427812 507 LALGASTALAAQSLGMLIGAASSSLQVATFLGPVTAIPVLLFSGFFVSFKAIPSYLQWSSYLSYVRYGFEGVI 579
Cdd:TIGR00956 536 LLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLM 608
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
96-289 |
2.10e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.61 E-value: 2.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP--RELRTFRKMSCYIMQEDILLPHLTVLEAMMISANLKLNEK 173
Cdd:COG1131 27 EIFGLLGPNGAGKTTTIRMLLGLLRPT-SGEVRVLGEDvaRDPAEVRRRIGYVPQEPALYPDLTVRENLRFFARLYGLPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 174 QEVKkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTI 253
Cdd:COG1131 106 KEAR-ERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTV 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 157427812 254 ICTIHQPSAkLFEMFDKLYILSQGQCIFKGMVTNLI 289
Cdd:COG1131 185 LLSTHYLEE-AERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
96-278 |
4.55e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 151.73 E-value: 4.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRK-SGmkGQILVNGKP------RELRTFRKMSC-YIMQEDILLPHLTVLE----AMM 163
Cdd:COG1136 35 EFVAIVGPSGSGKSTLLNILGGLDRpTS--GEVLIDGQDisslseRELARLRRRHIgFVFQFFNLLPELTALEnvalPLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 164 ISanlklNEKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLM 243
Cdd:COG1136 113 LA-----GVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELL 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 157427812 244 KSLA-QGGRTIICTIHqpSAKLFEMFDKLYILSQGQ 278
Cdd:COG1136 188 RELNrELGTTIVMVTH--DPELAARADRVIRLRDGR 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
96-278 |
5.67e-41 |
|
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: 148.41 E-value: 5.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP------RELRTFR--KMScYIMQEDILLPHLTVLEAMMISAN 167
Cdd:cd03255 31 EFVAIVGPSGSGKSTLLNILGGLDRPT-SGEVRVDGTDisklseKELAAFRrrHIG-FVFQSFNLLPDLTALENVELPLL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 LKLNEKQEvKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLA 247
Cdd:cd03255 109 LAGVPKKE-RRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELN 187
|
170 180 190
....*....|....*....|....*....|..
gi 157427812 248 -QGGRTIICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:cd03255 188 kEAGTTIVVVTHDPE--LAEYADRIIELRDGK 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
62-278 |
8.36e-41 |
|
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: 147.61 E-value: 8.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 62 EFVELSYSvregpcwRKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKP---RELRT 138
Cdd:cd03225 1 ELKNLSFS-------YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-TSGEVLVDGKDltkLSLKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 139 FRKMSCYIMQ--EDILLpHLTVLEAMMISA-NLKLNEKQEVKKelVTEILTALGLLSCSHTRTALLSGGQRKRLAIALEL 215
Cdd:cd03225 73 LRRKVGLVFQnpDDQFF-GPTVEEEVAFGLeNLGLPEEEIEER--VEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157427812 216 VNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQPSaKLFEMFDKLYILSQGQ 278
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
61-283 |
1.41e-40 |
|
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: 147.86 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 61 IEFVELSYSVREGpcwrkrgyKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKsGMKGQILVNGKP---RELR 137
Cdd:COG1122 1 IELENLSFSYPGG--------TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLK-PTSGEVLVDGKDitkKNLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 138 TFRKMSCYIMQ--ED-ILLPhlTVLEAMMIS-ANLKLnEKQEVKkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIAL 213
Cdd:COG1122 72 ELRRKVGLVFQnpDDqLFAP--TVEEDVAFGpENLGL-PREEIR-ERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 214 ELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADG 216
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
96-283 |
3.76e-37 |
|
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: 138.84 E-value: 3.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP--RELRTFRKMSCYIMQEDILLPHLTVLEAMMISANLKLNEK 173
Cdd:COG4555 28 EITGLLGPNGAGKTTLLRMLAGLLKPD-SGSILIDGEDvrKEPREARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 174 QEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTI 253
Cdd:COG4555 107 EELKKR-IEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTV 185
|
170 180 190
....*....|....*....|....*....|..
gi 157427812 254 ICTIHQPS--AKLfemFDKLYILSQGQCIFKG 283
Cdd:COG4555 186 LFSSHIMQevEAL---CDRVVILHKGKVVAQG 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
78-280 |
5.03e-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: 137.64 E-value: 5.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 78 KRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGKP--RELRTFRKMSCYIMQEDILLP 154
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGeLRPTS--GTAYINGYSirTDRKAARQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 155 HLTVLEAMMISANLK-LNEKQEvkKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:cd03263 89 ELTVREHLRFYARLKgLPKSEI--KEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 157427812 234 ASSFQVASLMKSLaQGGRTIICTIHqpSAKLFEMF-DKLYILSQGQ--CI 280
Cdd:cd03263 167 ASRRAIWDLILEV-RKGRSIILTTH--SMDEAEALcDRIAIMSDGKlrCI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
61-293 |
7.75e-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: 137.63 E-value: 7.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 61 IEFVELSYSvregpcwrkRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAG-YRKSgmKGQILVNGKPR----- 134
Cdd:cd03261 1 IELRGLTKS---------FGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGlLRPD--SGEVLIDGEDIsglse 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 135 -ELRTFRKMSCYIMQEDILLPHLTVLE--AMMISANLKLNEkqEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAI 211
Cdd:cd03261 70 aELYRLRRRMGMLFQSGALFDSLTVFEnvAFPLREHTRLSE--EEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 212 ALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL--AQGGRTIICTiHQPSAkLFEMFDKLYILSQGQCIFKGMVTNLI 289
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVT-HDLDT-AFAIADRIAVLYDGKIVAEGTPEELR 225
|
....*...
gi 157427812 290 ----PYLK 293
Cdd:cd03261 226 asddPLVR 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
96-283 |
1.28e-35 |
|
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: 134.23 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYrKSGMKGQILVNG------KPRELRTFRKMSCYIMQEDILLPHLTVLEAMM------ 163
Cdd:cd03256 28 EFVALIGPSGAGKSTLLRCLNGL-VEPTSGSVLIDGtdinklKGKALRQLRRQIGMIFQQFNLIERLSVLENVLsgrlgr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 164 ---ISANLKLNEKQEvkKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVA 240
Cdd:cd03256 107 rstWRSLFGLFPKEE--KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 157427812 241 SLMKSLAQG-GRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG 283
Cdd:cd03256 185 DLLKRINREeGITVIVSLHQVDlAREY--ADRIVGLKDGRIVFDG 227
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
78-578 |
1.34e-35 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 144.22 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 78 KRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGMK--GQILVNGkpRELRTF--RKMSCYIMQEDILL 153
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKvsGEITYNG--YRLNEFvpRKTSAYISQNDVHV 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 154 PHLTVLEAMMISAN--------------------------------LKLNEKQEVKKELVTE-ILTALGLLSCSHTRTAL 200
Cdd:PLN03140 252 GVMTVKETLDFSARcqgvgtrydllselarrekdagifpeaevdlfMKATAMEGVKSSLITDyTLKILGLDICKDTIVGD 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 201 -----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGR-TIICTIHQPSAKLFEMFDKLYIL 274
Cdd:PLN03140 332 emirgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEaTVLMSLLQPAPETFDLFDDIILL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 275 SQGQCIFKGMVTNLIPYLKGLGLHCPTYHNPADFIIEVASGE-----YGDLN-PLLFRAVQNGLCAMAEKNSGPE-KNEV 347
Cdd:PLN03140 412 SEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKdqeqyWADRNkPYRYISVSEFAERFKSFHVGMQlENEL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 348 ptlcppcPLEVDTIESH-------TFATSTLTQFCILFKRSFLSVLRDMVLTHLRFISHAVIGVLIGLLYLQ----TGND 416
Cdd:PLN03140 492 -------SVPFDKSQSHkaalvfsKYSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRtemhTRNE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 417 ANKVLnNTGCLFFSILFLMF---AAMMPTVLTFPlemaVFLRE-----HLNYWYSLKIYFLAktmadVPFQVICPAVYCS 488
Cdd:PLN03140 565 EDGAL-YIGALLFSMIINMFngfAELALMIQRLP----VFYKQrdllfHPPWTFTLPTFLLG-----IPISIIESVVWVV 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 489 IMYWMTSQPAETSRFLLFLALGASTALAAQSLGMLIGAASSSLQVATFLGPVTAIPVLLFSGFFVSFKAIPSYLQWSSYL 568
Cdd:PLN03140 635 ITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWV 714
|
570
....*....|
gi 157427812 569 SYVRYGFEGV 578
Cdd:PLN03140 715 SPLSYGFNAL 724
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
77-283 |
2.13e-34 |
|
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: 129.69 E-value: 2.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 77 RKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKS--GMKGQILVNGKP--RELRTFRKMSCYIMQEDIL 152
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvSVEGDIHYNGIPykEFAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 153 LPHLTVLEAMMISANLKLNEKqeVKKelvteiltalgllscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:cd03233 95 FPTLTVRETLDFALRCKGNEF--VRG----------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 157427812 233 SASSFQVASLMKSLAQG-GRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03233 151 SSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
96-278 |
5.72e-34 |
|
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: 127.51 E-value: 5.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP--RELRTFRKMSCYIMQEDILLPHLTVLEammisaNLKLnek 173
Cdd:cd03230 27 EIYGLLGPNGAGKTTLIKIILGLLKPD-SGEIKVLGKDikKEPEEVKRRIGYLPEEPSLYENLTVRE------NLKL--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 174 qevkkelvteiltalgllscshtrtallSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTI 253
Cdd:cd03230 97 ----------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTI 148
|
170 180
....*....|....*....|....*
gi 157427812 254 ICTIHQPSAkLFEMFDKLYILSQGQ 278
Cdd:cd03230 149 LLSSHILEE-AERLCDRVAILNNGR 172
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
96-229 |
8.52e-34 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 126.22 E-value: 8.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGyRKSGMKGQILVNGKP---RELRTFRKMSCYIMQEDILLPHLTVLEAMMISANLKLNE 172
Cdd:pfam00005 12 EILALVGPNGAGKSTLLKLIAG-LLSPTEGTILLDGQDltdDERKSLRKEIGYVFQDPQLFPRLTVRENLRLGLLLKGLS 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157427812 173 KQEVKKElVTEILTALGLLSCSHTR----TALLSGGQRKRLAIALELVNNPPVMFFDEPTS 229
Cdd:pfam00005 91 KREKDAR-AEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
96-283 |
1.85e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 128.64 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGyRKSGMKGQILVNG------KPRELRTFRKMSCYIMQEDILLPHLTVLEAMMI----- 164
Cdd:COG3638 30 EFVALIGPSGAGKSTLLRCLNG-LVEPTSGEILVDGqdvtalRGRALRRLRRRIGMIFQQFNLVPRLSVLTNVLAgrlgr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 165 ----SANLKLNEKQEvkKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVA 240
Cdd:COG3638 109 tstwRSLLGLFPPED--RERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVM 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 157427812 241 SLMKSLAQ-GGRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG 283
Cdd:COG3638 187 DLLRRIAReDGITVVVNLHQVDlARRY--ADRIIGLRDGRVVFDG 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
77-278 |
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 157427812 77 RKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRkSGMKGQILVNGKPRE---LRTFRKMSCYIMQEdill 153
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLD-PPTSGEIYLDGKPLSampPPEWRRQVAYVPQE---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 154 phlTVLEAMMISANLKL---NEKQEVKKELVTEILTALGL-LSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 229
Cdd:COG4619 83 ---PALWGGTVRDNLPFpfqLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 157427812 230 GLDSASSFQVASLMKSL-AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQ 278
Cdd:COG4619 160 ALDPENTRRVEELLREYlAEEGRAVLWVSHDP-EQIERVADRVLTLEAGR 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
76-278 |
1.61e-32 |
|
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: 123.45 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 76 WRKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKP-----RELRTFRKMSCYIMQED 150
Cdd:cd03229 7 SKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEP-DSGSILIDGEDltdleDELPPLRRRIGMVFQDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 151 ILLPHLTVLEammisaNLklnekqevkkelvteiltALGLlscshtrtallSGGQRKRLAIALELVNNPPVMFFDEPTSG 230
Cdd:cd03229 86 ALFPHLTVLE------NI------------------ALGL-----------SGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157427812 231 LDSASSFQVASLMKSL-AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQ 278
Cdd:cd03229 131 LDPITRREVRALLKSLqAQLGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
79-260 |
1.79e-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: 124.51 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 79 RGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPRELR--TFRKMSCYIMQEDILLPHL 156
Cdd:COG4133 12 RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPP-SAGEVLWNGEPIRDAreDYRRRLAYLGHADGLKPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 157 TVLEAMMISANLKlneKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASS 236
Cdd:COG4133 91 TVRENLRFWAALY---GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180
....*....|....*....|....
gi 157427812 237 FQVASLMKSLAQGGRTIICTIHQP 260
Cdd:COG4133 168 ALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
97-283 |
8.22e-32 |
|
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: 122.69 E-value: 8.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 97 MIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP--RELRTFRKMSCYIMQEDILLPHLTVLEAMMISANLKLNEKQ 174
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPPS-SGTIRIDGQDvlKQPQKLRRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 175 EVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQgGRTII 254
Cdd:cd03264 106 EVKAR-VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVI 183
|
170 180
....*....|....*....|....*....
gi 157427812 255 CTIHQPSaKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03264 184 LSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
82-283 |
8.30e-32 |
|
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: 124.00 E-value: 8.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 82 KTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP------RELRtfRKMScYIMQEDILLPH 155
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-SGEVLLDGRDlaslsrRELA--RRIA-YVPQEPPAPFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 156 LTVLEAMM------ISANLKLNEKQEvkkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 229
Cdd:COG1120 90 LTVRELVAlgryphLGLFGRPSAEDR---EAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157427812 230 GLDSASSFQVASLMKSLAQG-GRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG 283
Cdd:COG1120 167 HLDLAHQLEVLELLRRLARErGRTVVMVLHDLNlAARY--ADRLVLLKDGRIVAQG 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
96-278 |
2.04e-31 |
|
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: 119.66 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP---RELRTFRKMSCYIMQedillphltvleammisanlklne 172
Cdd:cd00267 26 EIVALVGPNGSGKSTLLRAIAGLLKPT-SGEILIDGKDiakLPLEELRRRIGYVPQ------------------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 173 kqevkkelvteiltalgllscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRT 252
Cdd:cd00267 81 ----------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRT 132
|
170 180
....*....|....*....|....*..
gi 157427812 253 IICTIHQPS-AKLFemFDKLYILSQGQ 278
Cdd:cd00267 133 VIIVTHDPElAELA--ADRVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
80-279 |
2.86e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.12 E-value: 2.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 80 GYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPRELRtfRKMSCYIMQE---DILLPhL 156
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-TSGTVRLFGKPPRRA--RRRIGYVPQRaevDWDFP-I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 157 TVLEAMM------ISANLKLNEKQevkKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSG 230
Cdd:COG1121 93 TVRDVVLmgrygrRGLFRRPSRAD---REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157427812 231 LDSASSFQVASLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQC 279
Cdd:COG1121 170 VDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRGLV 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
79-258 |
6.17e-31 |
|
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: 120.05 E-value: 6.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 79 RGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPRELRTFRKMSCYIMQE-DILLPHLT 157
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE-SSGSILLNGKPIKAKERRKSIGYVMQDvDYQLFTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 158 VLEAMMISANLKLNEKQEVKkelvtEILTALGL--LSCSHTRTalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 235
Cdd:cd03226 89 VREELLLGLKELDAGNEQAE-----TVLKDLDLyaLKERHPLS--LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180
....*....|....*....|...
gi 157427812 236 SFQVASLMKSLAQGGRTIICTIH 258
Cdd:cd03226 162 MERVGELIRELAAQGKAVIVITH 184
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
96-259 |
1.65e-30 |
|
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: 119.17 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTL---MNLLAGYRKsgmkGQILVNGKP-----RELRTFRKMSCYIMQEDILLPHLTVLEAMMISAN 167
Cdd:cd03262 27 EVVVIIGPSGSGKSTLlrcINLLEEPDS----GTIIIDGLKltddkKNINELRQKVGMVFQQFNLFPHLTVLENITLAPI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 LKLNEKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLA 247
Cdd:cd03262 103 KVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLA 182
|
170
....*....|..
gi 157427812 248 QGGRTIICTIHQ 259
Cdd:cd03262 183 EEGMTMVVVTHE 194
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
96-258 |
3.05e-30 |
|
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: 118.28 E-value: 3.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGyRKSGMKGQILVNGKP------RELRTFRKMSCYIMQEDILLPHLTVLEAMMISANLK 169
Cdd:cd03292 28 EFVFLVGPSGAGKSTLLKLIYK-EELPTSGTIRVNGQDvsdlrgRAIPYLRRKIGVVFQDFRLLPDRNVYENVAFALEVT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 LNEKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQG 249
Cdd:cd03292 107 GVPPREIRKR-VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKA 185
|
....*....
gi 157427812 250 GRTIICTIH 258
Cdd:cd03292 186 GTTVVVATH 194
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
96-278 |
4.53e-30 |
|
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: 116.33 E-value: 4.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP-REL--RTFRKMSCYIMQEDILLpHLTVLEammisanlklNe 172
Cdd:cd03228 29 EKVAIVGPSGSGKSTLLKLLLRLYDPT-SGEILIDGVDlRDLdlESLRKNIAYVPQDPFLF-SGTIRE----------N- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 173 kqevkkelvteiltalgllscshtrtaLLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQgGRT 252
Cdd:cd03228 96 ---------------------------ILSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK-GKT 147
|
170 180
....*....|....*....|....*.
gi 157427812 253 IICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:cd03228 148 VIVIAHRLS--TIRDADRIIVLDDGR 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
96-283 |
4.96e-30 |
|
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: 118.31 E-value: 4.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSgmKGQILVNG------KPREL------RTFRKMScyimqediLLPHLTVLEAM 162
Cdd:cd03219 27 EIHGLIGPNGAGKTTLFNLISGfLRPT--SGSVLFDGeditglPPHEIarlgigRTFQIPR--------LFPELTVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 163 MISANLKLNE---------KQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:cd03219 97 MVAAQARTGSglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 157427812 234 ASSFQVASLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03219 177 EETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEG 225
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
96-283 |
4.97e-30 |
|
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: 118.55 E-value: 4.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNG------KPRELRTFRKMSCYIMQEDILLPHLTVLEAMMISA--- 166
Cdd:TIGR02315 29 EFVAIIGPSGAGKSTLLRCINRLVEPS-SGSILLEGtditklRGKKLRKLRRRIGMIFQHYNLIERLTVLENVLHGRlgy 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 167 ----NLKLNEKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASL 242
Cdd:TIGR02315 108 kptwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDY 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 157427812 243 MKSLAQG-GRTIICTIHQPS-AKLFEmfDKLYILSQGQCIFKG 283
Cdd:TIGR02315 188 LKRINKEdGITVIINLHQVDlAKKYA--DRIVGLKAGEIVFDG 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
78-283 |
5.95e-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: 116.38 E-value: 5.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 78 KRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPRELRTFRKMscyimqedillphlt 157
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-SGEILLDGKDLASLSPKEL--------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 158 vleAMMISanlklnekqevkkeLVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSF 237
Cdd:cd03214 72 ---ARKIA--------------YVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 157427812 238 QVASLMKSLA-QGGRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG 283
Cdd:cd03214 135 ELLELLRRLArERGKTVVMVLHDLNlAARY--ADRVILLKDGRIVAQG 180
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
96-283 |
1.25e-29 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 117.39 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSgmKGQILVNGK------PRELRTFR-KMScYIMQEDILLPHLTVLE--AMMIS 165
Cdd:COG1127 32 EILAIIGGSGSGKSVLLKLIIGlLRPD--SGEILVDGQditglsEKELYELRrRIG-MLFQGGALFDSLTVFEnvAFPLR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 166 ANLKLNEKQevKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKS 245
Cdd:COG1127 109 EHTDLSEAE--IRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157427812 246 L--AQGGRTIICTiHQ-PSAklFEMFDKLYILSQGQCIFKG 283
Cdd:COG1127 187 LrdELGLTSVVVT-HDlDSA--FAIADRVAVLADGKIIAEG 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
90-287 |
1.65e-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: 116.42 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 90 GKFCCremigIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGKPreLRTFRKMSCYIMQEDILLPHLTVLEAMMISANL 168
Cdd:cd03293 30 GEFVA-----LVGPSGCGKSTLLRIIAGlERPTS--GEVLVDGEP--VTGPGPDRGYVFQQDALLPWLTVLDNVALGLEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 169 KLNEKQEvKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQV-ASLMKSLA 247
Cdd:cd03293 101 QGVPKAE-ARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLqEELLDIWR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 157427812 248 QGGRTIICTIHQPSAKLFeMFDKLYILSQGQCIFKGMVTN 287
Cdd:cd03293 180 ETGKTVLLVTHDIDEAVF-LADRVVVLSARPGRIVAEVEV 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
96-283 |
8.73e-29 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 114.13 E-value: 8.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYrKSGMKGQILVNG------KPRElrtfRKMScYIMQEDILLPHLTVLE--AMMISAN 167
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGF-ETPQSGRVLINGvdvtaaPPAD----RPVS-MLFQENNLFAHLTVEQnvGLGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 LKLNEKQevkKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL- 246
Cdd:cd03298 99 LKLTAED---RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLh 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 157427812 247 AQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 283
Cdd:cd03298 176 AETKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
96-278 |
1.06e-28 |
|
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: 121.86 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSgmKGQILVNGK------PRELRtfRKMScYIMQEDILLpHLTVLEammisaNL 168
Cdd:COG2274 502 ERVAIVGRSGSGKSTLLKLLLGlYEPT--SGRILIDGIdlrqidPASLR--RQIG-VVLQDVFLF-SGTIRE------NI 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 169 KLNeKQEVKKELVTEILTALGLLS--CSH---------TRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSF 237
Cdd:COG2274 570 TLG-DPDATDEEIIEAARLAGLHDfiEALpmgydtvvgEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEA 648
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157427812 238 QVASLMKSLAQgGRTIICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:COG2274 649 IILENLRRLLK-GRTVIIIAHRLS--TIRLADRIIVLDKGR 686
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
96-258 |
1.12e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 113.99 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSgmKGQILVNG------KPRE---LRtfRKMScYIMQEDILLPHLTVLEammis 165
Cdd:COG2884 29 EFVFLTGPSGAGKSTLLKLLYGeERPT--SGQVLVNGqdlsrlKRREipyLR--RRIG-VVFQDFRLLPDRTVYE----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 166 aNLKL------NEKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQV 239
Cdd:COG2884 99 -NVALplrvtgKSRKEIRRR-VREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEI 176
|
170
....*....|....*....
gi 157427812 240 ASLMKSLAQGGRTIICTIH 258
Cdd:COG2884 177 MELLEEINRRGTTVLIATH 195
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
96-278 |
1.16e-28 |
|
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: 113.77 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGY-RKSGmkGQILVNGK-----PRELRTFrkmsCYIMQEDILLPHLTVLEAMMISANLK 169
Cdd:cd03259 27 EFLALLGPSGCGKTTLLRLIAGLeRPDS--GEILIDGRdvtgvPPERRNI----GMVFQDYALFPHLTVAENIAFGLKLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 LNEKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL-AQ 248
Cdd:cd03259 101 GVPKAEIRAR-VRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELqRE 179
|
170 180 190
....*....|....*....|....*....|.
gi 157427812 249 GGRTIICTIHQPS-AklFEMFDKLYILSQGQ 278
Cdd:cd03259 180 LGITTIYVTHDQEeA--LALADRIAVMNEGR 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
96-280 |
2.54e-28 |
|
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: 113.37 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKP------RELRTFRKMSCYIMQEDI--LLPHLTV----LEAMM 163
Cdd:cd03257 32 ETLGLVGESGSGKSTLARAILGLLKP-TSGSIIFDGKDllklsrRLRKIRRKEIQMVFQDPMssLNPRMTIgeqiAEPLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 164 IsanLKLNEKQEVKKELVTEILTALGLLS-CSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASL 242
Cdd:cd03257 111 I---HGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDL 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 157427812 243 MKSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCI 280
Cdd:cd03257 188 LKKLQEElGLTLLFITHDLGV-VAKIADRVAVMYAGKIV 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
96-260 |
5.63e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 112.54 E-value: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGK------PRElrtfRKMScYIMQEDILLPHLTVLE--AMMISAN 167
Cdd:COG3840 26 ERVAILGPSGAGKSTLLNLIAGFLPP-DSGRILWNGQdltalpPAE----RPVS-MLFQENNLFPHLTVAQniGLGLRPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 LKLNEKQevkKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLA 247
Cdd:COG3840 100 LKLTAEQ---RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELC 176
|
170
....*....|....
gi 157427812 248 QG-GRTIICTIHQP 260
Cdd:COG3840 177 RErGLTVLMVTHDP 190
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
53-278 |
3.27e-27 |
|
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: 116.40 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 53 LPKRSAVDIEFVELSYSVREGpcwrkrgyKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGK 132
Cdd:COG4988 329 LPAAGPPSIELEDVSFSYPGG--------RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP-YSGSILINGV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 133 P-RELR--TFRKMSCYIMQEDiLLPHLTVLEammisaNLKLNE----KQEVKKEL----VTEILTAL--GLlscsHTRT- 198
Cdd:COG4988 400 DlSDLDpaSWRRQIAWVPQNP-YLFAGTIRE------NLRLGRpdasDEELEAALeaagLDEFVAALpdGL----DTPLg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 199 ---ALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTiHQPSakLFEMFDKLYILS 275
Cdd:COG4988 469 eggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLA--LLAQADRILVLD 545
|
...
gi 157427812 276 QGQ 278
Cdd:COG4988 546 DGR 548
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
96-278 |
6.16e-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: 109.89 E-value: 6.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKsGMKGQILVNGKP---RELRTFRKMSCYIMQ--EDILLPHLTVLEAmmISANLKL 170
Cdd:COG1124 32 ESFGLVGESGSGKSTLLRALAGLER-PWSGEVTFDGRPvtrRRRKAFRRRVQMVFQdpYASLHPRHTVDRI--LAEPLRI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 171 NEKQEVKKElVTEILTALGLlscshTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMK 244
Cdd:COG1124 109 HGLPDREER-IAELLEQVGL-----PPSFLdryphqLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLK 182
|
170 180 190
....*....|....*....|....*....|....*
gi 157427812 245 SL-AQGGRTIICTIHQPSAKLFeMFDKLYILSQGQ 278
Cdd:COG1124 183 DLrEERGLTYLFVSHDLAVVAH-LCDRVAVMQNGR 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
54-232 |
8.25e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 109.79 E-value: 8.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 54 PKRSAVDIEFVELSYSVREGPcwrkrgyKTLLKCLS-----GKFCCremigIMGPSGSGKSTLMNLLAG-YRKSGmkGQI 127
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGG-------VTALDDVSltvaaGEFVA-----LVGPSGCGKSTLLRLIAGlEKPTS--GEV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 128 LVNGKPRElRTFRKMScYIMQEDILLPHLTVLEAMMISANLKLNEKQEvKKELVTEILTALGLLSCSHTRTALLSGGQRK 207
Cdd:COG1116 69 LVDGKPVT-GPGPDRG-VVFQEPALLPWLTVLDNVALGLELRGVPKAE-RRERARELLELVGLAGFEDAYPHQLSGGMRQ 145
|
170 180
....*....|....*....|....*
gi 157427812 208 RLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALD 170
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
96-283 |
1.43e-26 |
|
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: 107.69 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGK--PRELRTFRKMSCyIMQEDILLPHLTVLEAMMISANLKLNE 172
Cdd:cd03268 27 EIYGFLGPNGAGKTTTMKIILGlIKPDS--GEITFDGKsyQKNIEALRRIGA-LIEAPGFYPNLTARENLRLLARLLGIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 173 KQEVKkelvtEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRT 252
Cdd:cd03268 104 KKRID-----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGIT 178
|
170 180 190
....*....|....*....|....*....|.
gi 157427812 253 IICTIHQPSaKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03268 179 VLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
80-259 |
1.75e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 108.26 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 80 GYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLM---NLLagyrKSGMKGQILV-----NGKPRELRTFRKMSCYIMQEDI 151
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKL----EEITSGDLIVdglkvNDPKVDERLIRQEAGMVFQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 152 LLPHLTVLEAMMISANLKLNEKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 231
Cdd:PRK09493 88 LFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180
....*....|....*....|....*...
gi 157427812 232 DSASSFQVASLMKSLAQGGRTIICTIHQ 259
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
85-258 |
1.86e-26 |
|
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: 106.74 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 85 LKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKP-----RELRTFRKMSCYIMQE-DILLPHLTV 158
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRP-QSGAVLIDGEPldysrKGLLERRQRVGLVFQDpDDQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 159 LEAMMISA-NLKLNEkQEVKkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSF 237
Cdd:TIGR01166 87 DQDVAFGPlNLGLSE-AEVE-RRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|.
gi 157427812 238 QVASLMKSLAQGGRTIICTIH 258
Cdd:TIGR01166 165 QMLAILRRLRAEGMTVVISTH 185
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
96-283 |
3.75e-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: 113.32 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKP-RELR--TFRKMSCYIMQEdillPHL---TVLEammisaNLK 169
Cdd:COG4987 362 ERVAIVGPSGSGKSTLLALLLRFLDP-QSGSITLGGVDlRDLDedDLRRRIAVVPQR----PHLfdtTLRE------NLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 LnEKQEVKKELVTEILTALGL--LSCS-----HTRT----ALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQ 238
Cdd:COG4987 431 L-ARPDATDEELWAALERVGLgdWLAAlpdglDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQA 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 157427812 239 VASLMKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 283
Cdd:COG4987 510 LLADLLEALA-GRTVLLITHRLAG--LERMDRILVLEDGRIVEQG 551
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
96-254 |
3.89e-26 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 112.69 E-value: 3.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGKP------RELRTFRKMSCYIMQ--EDILLPHLTVLEAMMISA 166
Cdd:COG1123 292 ETLGLVGESGSGKSTLARLLLGlLRPTS--GSILFDGKDltklsrRSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAEPL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 167 -NLKLNEKQEVKkELVTEILTALGL-LSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMK 244
Cdd:COG1123 370 rLHGLLSRAERR-ERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLR 448
|
170
....*....|.
gi 157427812 245 SL-AQGGRTII 254
Cdd:COG1123 449 DLqRELGLTYL 459
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
96-277 |
4.81e-26 |
|
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: 106.08 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPreLRTFRKMSCYIMQ-EDIL--LPhLTVLEAMMISANLKLNE 172
Cdd:cd03235 26 EFLAIVGPNGAGKSTLLKAILGLLKP-TSGSIRVFGKP--LEKERKRIGYVPQrRSIDrdFP-ISVRDVVLMGLYGHKGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 173 KQEVKKE---LVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQG 249
Cdd:cd03235 102 FRRLSKAdkaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE 181
|
170 180
....*....|....*....|....*...
gi 157427812 250 GRTIICTIHQPSAkLFEMFDKLYILSQG 277
Cdd:cd03235 182 GMTILVVTHDLGL-VLEYFDRVLLLNRT 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
96-289 |
6.79e-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: 106.51 E-value: 6.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGK------PRELRTFRKMSCYIMQEDILLPHLTVLEAmmISANLK 169
Cdd:cd03258 32 EIFGIIGRSGAGKSTLIRCINGLERPT-SGSVLVDGTdltllsGKELRKARRRIGMIFQHFNLLSSRTVFEN--VALPLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 L-NEKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ 248
Cdd:cd03258 109 IaGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINR 188
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 157427812 249 G-GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKGMVTNLI 289
Cdd:cd03258 189 ElGLTIVLITHEMEV-VKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
96-267 |
8.29e-26 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 106.23 E-value: 8.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTL---MNLLAGYRKsgmkGQILVNG-----KPRELRTFRKMSCYIMQEDILLPHLTVLE----AMM 163
Cdd:COG1126 28 EVVVIIGPSGSGKSTLlrcINLLEEPDS----GTITVDGedltdSKKDINKLRRKVGMVFQQFNLFPHLTVLEnvtlAPI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 164 ISanLKLNeKQEVKkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLM 243
Cdd:COG1126 104 KV--KKMS-KAEAE-ERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVM 179
|
170 180
....*....|....*....|....
gi 157427812 244 KSLAQGGRTIICTIHqpsaklfEM 267
Cdd:COG1126 180 RDLAKEGMTMVVVTH-------EM 196
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
81-284 |
1.03e-25 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 105.33 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 81 YKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPR-ELRTFRKMSCYIMQEDILLPHLTVL 159
Cdd:TIGR01277 10 YEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEP-ASGSIKVNDQSHtGLAPYQRPVSMLFQENNLFAHLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 160 E--AMMISANLKLNEKQevkKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSF 237
Cdd:TIGR01277 89 QniGLGLHPGLKLNAEQ---QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 157427812 238 QVASLMKSLA-QGGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKGM 284
Cdd:TIGR01277 166 EMLALVKQLCsERQRTLLMVTHHLS-DARAIASQIAVVSQGKIKVVSD 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
96-283 |
1.43e-25 |
|
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: 104.98 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNG------KPRELRtfRKMScYIMQEdillPHL---TVLEAMMISA 166
Cdd:cd03245 31 EKVAIIGRVGSGKSTLLKLLAGLYKP-TSGSVLLDGtdirqlDPADLR--RNIG-YVPQD----VTLfygTLRDNITLGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 167 nlklnekQEVKKELVTEILTALGL--LSCSH---------TRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 235
Cdd:cd03245 103 -------PLADDERILRAAELAGVtdFVNKHpngldlqigERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 157427812 236 SFQVASLMKSLAqGGRTIICTIHQPSakLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03245 176 EERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
96-232 |
3.40e-25 |
|
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: 104.24 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP-RELRTFRKMSCYIMQEDILLPHLTVLEAMMISANLKLNEKQ 174
Cdd:cd03300 27 EFFTLLGPSGCGKTTLLRLIAGFETPT-SGEILLDGKDiTNLPPHKRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKA 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 157427812 175 EVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:cd03300 106 EIKER-VAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
96-283 |
4.42e-25 |
|
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: 103.53 E-value: 4.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGK------------PRElrtfRKMScYIMQEDILLPHLTVLEAmm 163
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPD-GGTIVLNGTvlfdsrkkinlpPQQ----RKIG-LVFQQYALFPHLNVREN-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 164 ISANLKLNEkQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLM 243
Cdd:cd03297 96 LAFGLKRKR-NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 157427812 244 KSLAQ--GGRTIICTiHQPSaKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03297 175 KQIKKnlNIPVIFVT-HDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
96-260 |
7.81e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 109.43 E-value: 7.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLL-------AG-YRKSGMKGQILVNGKPRELRtfRKMSCYIMQEDILLPHLTVLEAMMISAN 167
Cdd:PRK10535 35 EMVAIVGASGSGKSTLMNILgcldkptSGtYRVAGQDVATLDADALAQLR--REHFGFIFQRYHLLSHLTAAQNVEVPAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 LKLNEKQEvKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLA 247
Cdd:PRK10535 113 YAGLERKQ-RLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR 191
|
170
....*....|...
gi 157427812 248 QGGRTIICTIHQP 260
Cdd:PRK10535 192 DRGHTVIIVTHDP 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
96-288 |
1.03e-24 |
|
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: 102.83 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKP--RELRTFRKMSCYIMQEDILLPHLTVLEAMMISANLKlNEK 173
Cdd:cd03265 27 EIFGLLGPNGAGKTTTIKMLTTLLKP-TSGRATVAGHDvvREPREVRRRIGIVFQDLSVDDELTGWENLYIHARLY-GVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 174 QEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL-AQGGRT 252
Cdd:cd03265 105 GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMT 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 157427812 253 IICTIH-QPSAKlfEMFDKLYILSQGQCIFKGMVTNL 288
Cdd:cd03265 185 ILLTTHyMEEAE--QLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
61-283 |
1.44e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 103.62 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 61 IEFVELSYSVREGpcwrkrgyKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP-----RE 135
Cdd:PRK13639 2 LETRDLKYSYPDG--------TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPT-SGEVLIKGEPikydkKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 136 LRTFRKMSCYIMQ---EDILLPhlTVLEAMMISA-NLKLNeKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAI 211
Cdd:PRK13639 73 LLEVRKTVGIVFQnpdDQLFAP--TVEEDVAFGPlNLGLS-KEEVEKR-VKEALKAVGMEGFENKPPHHLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157427812 212 ALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQpsAKLFEMF-DKLYILSQGQCIFKG 283
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEG 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
96-234 |
1.70e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 102.35 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYrKSGMKGQILVNGKPRELRTFRKMSCYIM-QEDILLPHLTVLE--AMMISANLKLNE 172
Cdd:PRK10771 26 ERVAILGPSGAGKSTLLNLIAGF-LTPASGSLTLNGQDHTTTPPSRRPVSMLfQENNLFSHLTVAQniGLGLNPGLKLNA 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157427812 173 KQevkKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 234
Cdd:PRK10771 105 AQ---REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
96-330 |
7.16e-24 |
|
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: 105.76 E-value: 7.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGY--RKSGMKGQILVNGK-----PRELRtfRKMSCYIMQE-DILLPHLTVLEAMMISAN 167
Cdd:COG1123 33 ETVALVGESGSGKSTLALALMGLlpHGGRISGEVLLDGRdllelSEALR--GRRIGMVFQDpMTQLNPVTVGDQIAEALE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 LKLNEKQEVKkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL- 246
Cdd:COG1123 111 NLGLSRAEAR-ARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELq 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 247 AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQCIFKGMVTNL---------IPYLKGLGLHCPTYHNPADFIIEVA--SG 315
Cdd:COG1123 190 RERGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPPEEIlaapqalaaVPRLGAARGRAAPAAAAAEPLLEVRnlSK 268
|
250
....*....|....*
gi 157427812 316 EYGDLNPLLFRAVQN 330
Cdd:COG1123 269 RYPVRGKGGVRAVDD 283
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
85-259 |
1.16e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.09 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 85 LKCLSGkfccrEMIGIMGPSGSGKSTL---MNLLAGYRKsgmkGQILVNG---------KPRELRTFRKMSCYIMQEDIL 152
Cdd:COG4161 23 LECPSG-----ETLVLLGPSGAGKSSLlrvLNLLETPDS----GQLNIAGhqfdfsqkpSEKAIRLLRQKVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 153 LPHLTVLEAMmISAN---LKLNEKQEVKKelVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 229
Cdd:COG4161 94 WPHLTVMENL-IEAPckvLGLSKEQAREK--AMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190
....*....|....*....|....*....|
gi 157427812 230 GLDSASSFQVASLMKSLAQGGRTIICTIHQ 259
Cdd:COG4161 171 ALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
79-260 |
1.40e-23 |
|
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: 98.58 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 79 RGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPR-ELRTFRKMSC-YIMQEDILLPHL 156
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP-DSGEVRWNGTPLaEQRDEPHENIlYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 157 TVLEammisaNLK-LNEKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 235
Cdd:TIGR01189 89 SALE------NLHfWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|....*.
gi 157427812 236 SFQVASLMKS-LAQGGRTIICTiHQP 260
Cdd:TIGR01189 163 VALLAGLLRAhLARGGIVLLTT-HQD 187
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
96-277 |
1.67e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 100.21 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTL---MNLL----AGYRKSG---MKGQILVNGKPRELRTFRKMSCYIMQEDILLPHLTVLEAMMIS 165
Cdd:PRK11264 30 EVVAIIGPSGSGKTTLlrcINLLeqpeAGTIRVGditIDTARSLSQQKGLIRQLRQHVGFVFQNFNLFPHRTVLENIIEG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 166 ANLKLNEKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKS 245
Cdd:PRK11264 110 PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQ 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 157427812 246 LAQGGRTIICTIHQPS-----AKLFEMFDKLYILSQG 277
Cdd:PRK11264 190 LAQEKRTMVIVTHEMSfardvADRAIFMDQGRIVEQG 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
96-283 |
2.31e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.09 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLM----NLLAGYRKSGMKGQILVN-----GK-PRELRTFRKMSCYIMQEDILLPHLTVLEAMMIS 165
Cdd:PRK09984 31 EMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIELLGRtvqreGRlARDIRKSRANTGYIFQQFNLVNRLSVLENVLIG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 166 A-------NLKLNEKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQ 238
Cdd:PRK09984 111 AlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 157427812 239 VASLMKSLAQG-GRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 283
Cdd:PRK09984 191 VMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDG 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
77-283 |
3.33e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 98.12 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 77 RKR-GYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPRELRTFRKMScYIMQEDILLPH 155
Cdd:cd03269 7 TKRfGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD-SGEVLFDGKPLDIAARNRIG-YLPEERGLYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 156 LTVLEAMMISANLKLNEKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 235
Cdd:cd03269 85 MKVIDQLVYLAQLKGLKKEEARRR-IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 157427812 236 SFQVASLMKSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03269 164 VELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
96-278 |
4.26e-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: 96.52 E-value: 4.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPRE---LRTFRKMSCYIMQEDILLPHlTVLEAmmisanlklne 172
Cdd:cd03246 29 ESLAIIGPSGSGKSTLARLILGLLRPT-SGRVRLDGADISqwdPNELGDHVGYLPQDDELFSG-SIAEN----------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 173 kqevkkelvteiltalgllscshtrtaLLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRT 252
Cdd:cd03246 96 ---------------------------ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGAT 148
|
170 180
....*....|....*....|....*.
gi 157427812 253 IICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:cd03246 149 RIVIAHRPE--TLASADRILVLEDGR 172
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
79-260 |
5.47e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 97.25 E-value: 5.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 79 RGYKTLLKCLSgkFCCR--EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPRELRTFRKMSCYIMQEDILLPHL 156
Cdd:PRK13539 12 RGGRVLFSGLS--FTLAagEALVLTGPNGSGKTTLLRLIAGLLPP-AAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 157 TVLEAMMISANLKLNEKQEVkkelvTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASS 236
Cdd:PRK13539 89 TVAENLEFWAAFLGGEELDI-----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|....*
gi 157427812 237 FQVASLMKS-LAQGGRTIICTiHQP 260
Cdd:PRK13539 164 ALFAELIRAhLAQGGIVIAAT-HIP 187
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
96-261 |
6.04e-23 |
|
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: 97.89 E-value: 6.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGY-RKSGmkGQILVNGKP------RELRTFRKMSC-YIMQEDILLPHLTVLEAMMISAN 167
Cdd:COG4181 39 ESVAIVGASGSGKSTLLGLLAGLdRPTS--GTVRLAGQDlfaldeDARARLRARHVgFVFQSFQLLPTLTALENVMLPLE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 LKlNEKQevKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL- 246
Cdd:COG4181 117 LA-GRRD--ARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELn 193
|
170
....*....|....*
gi 157427812 247 AQGGRTIICTIHQPS 261
Cdd:COG4181 194 RERGTTLVLVTHDPA 208
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
100-244 |
6.77e-23 |
|
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: 97.79 E-value: 6.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGK-----PRELRTFrkmsCYIMQEDILLPHLTVLEAMMISANLKLNEKQ 174
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKPD-SGKILLNGKditnlPPEKRDI----SYVPQNYALFPHMTVYKNIAYGLKKRKVDKK 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 175 EVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMK 244
Cdd:cd03299 105 EIERK-VLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
60-283 |
9.37e-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: 97.30 E-value: 9.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 60 DIEFVELSYSVREGpcwrkrgyKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAG-YRKSgmKGQILVNGKP---RE 135
Cdd:cd03254 2 EIEFENVNFSYDEK--------KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfYDPQ--KGQILIDGIDirdIS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 136 LRTFRKMSCYIMQEDILLPHlTVLEammisaNLKLNeKQEVKKELVTEILTAL-----------GLLSCSHTRTALLSGG 204
Cdd:cd03254 72 RKSLRSMIGVVLQDTFLFSG-TIME------NIRLG-RPNATDEEVIEAAKEAgahdfimklpnGYDTVLGENGGNLSQG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157427812 205 QRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQgGRTIICTIHQPSAKLFEmfDKLYILSQGQCIFKG 283
Cdd:cd03254 144 ERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKNA--DKILVLDDGKIIEEG 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
96-256 |
2.76e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.04 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYrKSGMKGQILVNGKP---------RELRTfRKMScYIMQEDILLPHLTVLE--AM-M 163
Cdd:PRK11629 36 EMMAIVGSSGSGKSTLLHLLGGL-DTPTSGDVIFNGQPmsklssaakAELRN-QKLG-FIYQFHHLLPDFTALEnvAMpL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 164 ISANLKLNEKQEVKKELvteiLTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLM 243
Cdd:PRK11629 113 LIGKKKPAEINSRALEM----LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLL 188
|
170
....*....|....*
gi 157427812 244 KSL--AQGGRTIICT 256
Cdd:PRK11629 189 GELnrLQGTAFLVVT 203
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
79-260 |
3.51e-22 |
|
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: 94.87 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 79 RGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKP-RELRTFRKMSC-YIMQEDILLPHL 156
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP-LAGRVLLNGGPlDFQRDSIARGLlYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 157 TVLEAMMISANLKLNEKqevkkelVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASS 236
Cdd:cd03231 89 SVLENLRFWHADHSDEQ-------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|....
gi 157427812 237 FQVASLMKSLAQGGRTIICTIHQP 260
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
96-283 |
4.52e-22 |
|
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: 95.19 E-value: 4.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKP-RELRTFRKMS---CYIMQEDILLPHLTVLEAMMISANLKLN 171
Cdd:cd03224 27 EIVALLGRNGAGKTTLLKTIMGLLPP-RSGSIRFDGRDiTGLPPHERARagiGYVPEGRRIFPELTVEENLLLGAYARRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 172 EKQEVKKELVTEILTALGLLScsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLdsASSF--QVASLMKSLAQG 249
Cdd:cd03224 106 AKRKARLERVYELFPRLKERR--KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL--APKIveEIFEAIRELRDE 181
|
170 180 190
....*....|....*....|....*....|....
gi 157427812 250 GRTIIcTIHQPSAKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03224 182 GVTIL-LVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
76-278 |
6.54e-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: 94.24 E-value: 6.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 76 WRKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGK------PRElrtfRKMScYIMQE 149
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT-SGRIYIGGRdvtdlpPKD----RDIA-MVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 150 DILLPHLTVLEAMmiSANLKLN-EKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPT 228
Cdd:cd03301 81 YALYPHMTVYDNI--AFGLKLRkVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 157427812 229 SGLDSASSFQVASLMKSLAQG-GRTIICTIH-QPSAklFEMFDKLYILSQGQ 278
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRlGTTTIYVTHdQVEA--MTMADRIAVMNDGQ 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
96-289 |
7.98e-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: 94.53 E-value: 7.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNG-----KPRELRTfRKMSCYIMQEDILLPHLTVLEAMMISANLKL 170
Cdd:cd03218 27 EIVGLLGPNGAGKTTTFYMIVGLVKPD-SGKILLDGqditkLPMHKRA-RLGIGYLPQEASIFRKLTVEENILAVLEIRG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 171 NEKQEVKKELVtEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGG 250
Cdd:cd03218 105 LSKKEREEKLE-ELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRG 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 157427812 251 RTIICTIHQPSAKLfEMFDKLYILSQGQCIFKGMVTNLI 289
Cdd:cd03218 184 IGVLITDHNVRETL-SITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
46-283 |
1.27e-21 |
|
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: 99.56 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 46 EAQRFSHLPKRSAvDIEF--VELSYSVREGPCwrkrgyktlLKCLSgkFCCR--EMIGIMGPSGSGKSTLMNLLAG-YRK 120
Cdd:TIGR03375 450 EGTRFLHRPRLQG-EIEFrnVSFAYPGQETPA---------LDNVS--LTIRpgEKVAIIGRIGSGKSTLLKLLLGlYQP 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 121 SgmKGQILVNG------KPRELRtfRKMScYIMQeDILLPHLTVLEAMMISAnlklnekQEVKKELVTEILTALGLLSC- 193
Cdd:TIGR03375 518 T--EGSVLLDGvdirqiDPADLR--RNIG-YVPQ-DPRLFYGTLRDNIALGA-------PYADDEEILRAAELAGVTEFv 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 194 -SHT---------RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQvasLMKSLAQ--GGRTIICTIHQPS 261
Cdd:TIGR03375 585 rRHPdgldmqigeRGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEER---FKDRLKRwlAGKTLVLVTHRTS 661
|
250 260
....*....|....*....|..
gi 157427812 262 akLFEMFDKLYILSQGQCIFKG 283
Cdd:TIGR03375 662 --LLDLVDRIIVMDNGRIVADG 681
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
61-283 |
1.75e-21 |
|
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: 94.83 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 61 IEFVELSYSVREGPCWRKRGyktlLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNG------KPR 134
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKA----LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPT-SGTVTIDGrditakKKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 135 ELRTFRKMSCYIMQ-------EDillphlTVLEAMMIS-ANLKLNEKqEVKkELVTEILTALGL-LSCSHTRTALLSGGQ 205
Cdd:TIGR04521 76 KLKDLRKKVGLVFQfpehqlfEE------TVYKDIAFGpKNLGLSEE-EAE-ERVKEALELVGLdEEYLERSPFELSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157427812 206 RKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ-GGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 283
Cdd:TIGR04521 148 MRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSME-DVAEYADRVIVMHKGKIVLDG 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
79-258 |
2.07e-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: 93.40 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 79 RGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTL------MNLLAGYRKSGmkGQILVNGK--------PRELRTFRKMsc 144
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLlrllnrLNDLIPGAPDE--GEVLLDGKdiydldvdVLELRRRVGM-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 145 yIMQEDILLPhLTVLEAmmISANLKLNE--KQEVKKELVTEILTALGLLSCSHTRTAL--LSGGQRKRLAIALELVNNPP 220
Cdd:cd03260 86 -VFQKPNPFP-GSIYDN--VAYGLRLHGikLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALANEPE 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 157427812 221 VMFFDEPTSGLDSASSFQVASLMKSLAQgGRTIICTIH 258
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTH 198
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
96-232 |
2.17e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 95.91 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGK------PRElrtfRKMScyiM--QEDILLPHLTVLEAMMISa 166
Cdd:COG3839 30 EFLVLLGPSGCGKSTLLRMIAGlEDPTS--GEILIGGRdvtdlpPKD----RNIA---MvfQSYALYPHMTVYENIAFP- 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157427812 167 nLKLN--EKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:COG3839 100 -LKLRkvPKAEIDRR-VREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
96-232 |
2.44e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 95.94 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGK------PRElrtfRKMScYIMQEDILLPHLTVLEammisaN- 167
Cdd:COG3842 32 EFVALLGPSGCGKTTLLRMIAGfETPDS--GRILLDGRdvtglpPEK----RNVG-MVFQDYALFPHLTVAE------Nv 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 ---LKL--NEKQEVkKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:COG3842 99 afgLRMrgVPKAEI-RARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
85-259 |
2.99e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.16 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 85 LKCLSGkfccrEMIGIMGPSGSGKSTLM---NLLAGYRKsgmkGQILVNG---------KPRELRTFRKMSCYIMQEDIL 152
Cdd:PRK11124 23 LDCPQG-----ETLVLLGPSGAGKSSLLrvlNLLEMPRS----GTLNIAGnhfdfsktpSDKAIRELRRNVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 153 LPHLTVLEAMmISANLK---LNEKQEVKKELvtEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 229
Cdd:PRK11124 94 WPHLTVQQNL-IEAPCRvlgLSKDQALARAE--KLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190
....*....|....*....|....*....|
gi 157427812 230 GLDSASSFQVASLMKSLAQGGRTIICTIHQ 259
Cdd:PRK11124 171 ALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-261 |
7.00e-21 |
|
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: 96.59 E-value: 7.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 16 GAVAMAVALEDGAEPPVLtthlkkvenhiteaqrfSHLPKRSAVD--IEFVELSYsvregpcwRKRGYKTLLKCLSGKFC 93
Cdd:TIGR02857 292 AAAEALFAVLDAAPRPLA-----------------GKAPVTAAPAssLEFSGVSV--------AYPGRRPALRPVSFTVP 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 94 CREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPR---ELRTFRKMSCYIMQedilLPHLTvleAMMISANLKL 170
Cdd:TIGR02857 347 PGERVALVGPSGAGKSTLLNLLLGFVDPT-EGSIAVNGVPLadaDADSWRDQIAWVPQ----HPFLF---AGTIAENIRL 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 171 NEKqEVKKELVTEILTALGLLSCS-------HT----RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQV 239
Cdd:TIGR02857 419 ARP-DASDAEIREALERAGLDEFVaalpqglDTpigeGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
250 260
....*....|....*....|..
gi 157427812 240 ASLMKSLAQgGRTIICTIHQPS 261
Cdd:TIGR02857 498 LEALRALAQ-GRTVLLVTHRLA 518
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
78-283 |
7.47e-21 |
|
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: 92.45 E-value: 7.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 78 KRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGMKGQILVNGKPR------ELRTfrkmscYI----- 146
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRggedvwELRK------RIglvsp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 147 -MQEDILlPHLTVLEaMMISA-------NLKLNEKQEvkkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNN 218
Cdd:COG1119 86 aLQLRFP-RDETVLD-VVLSGffdsiglYREPTDEQR---ERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157427812 219 PPVMFFDEPTSGLDSASSFQVASLMKSLAQ-GGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVLVTHHVEE-IPPGITHVLLLKDGRVVAAG 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
96-278 |
1.21e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 96.00 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGKP-RE--LRTFRKMSCYIMQEDILLpHLTVLEammisaNLKLN 171
Cdd:COG1132 367 ETVALVGPSGSGKSTLVNLLLRfYDPTS--GRILIDGVDiRDltLESLRRQIGVVPQDTFLF-SGTIRE------NIRYG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 172 EK----QEV----KKELVTEILTAL--GLlscsHT----RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSF 237
Cdd:COG1132 438 RPdatdEEVeeaaKAAQAHEFIEALpdGY----DTvvgeRGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEA 513
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 157427812 238 QVASLMKSLAQgGRTIIcTI-HQPSAklFEMFDKLYILSQGQ 278
Cdd:COG1132 514 LIQEALERLMK-GRTTI-VIaHRLST--IRNADRILVLDDGR 551
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
96-288 |
1.21e-20 |
|
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: 92.84 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGY-RKSGmkGQILVNG-----KPRELR-----TFRKMSCYimqEDillphLTVLEAMMI 164
Cdd:TIGR01188 20 EVFGFLGPNGAGKTTTIRMLTTLlRPTS--GTARVAGydvvrEPRKVRrsigiVPQYASVD---ED-----LTGRENLEM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 165 SANLkLNEKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMK 244
Cdd:TIGR01188 90 MGRL-YGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 157427812 245 SLAQGGRTIICTIHQpsakLFE---MFDKLYILSQGQCIFKGMVTNL 288
Cdd:TIGR01188 169 ALKEEGVTILLTTHY----MEEadkLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
60-248 |
1.26e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.93 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 60 DIEFVELSYSVREGPCWRKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTlmNLLAGYRKSGMKGQILVNGKPRELRTF 139
Cdd:PRK15134 277 DVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKST--TGLALLRLINSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 140 RKMSCYIMQEDI--------LLPHLTVLEamMISANLKLNEKQ---EVKKELVTEILTALGLLSCSHTR-TALLSGGQRK 207
Cdd:PRK15134 355 RQLLPVRHRIQVvfqdpnssLNPRLNVLQ--IIEEGLRVHQPTlsaAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQ 432
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157427812 208 RLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ 248
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQ 473
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
99-289 |
1.52e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 93.22 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 99 GIMGPSGSGKSTL---MNLLAgyRKSGmkGQILVNGK------PRELRTFRK---MscyIMQEDILLPHLTVLEammisa 166
Cdd:COG1135 35 GIIGYSGAGKSTLircINLLE--RPTS--GSVLVDGVdltalsERELRAARRkigM---IFQHFNLLSSRTVAE------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 167 N----LKLN--EKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVA 240
Cdd:COG1135 102 NvalpLEIAgvPKAEIRKR-VAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSIL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157427812 241 SLMKSL-AQGGRTIICTIHqpsaklfEM------FDKLYILSQGQCIFKGMVTNLI 289
Cdd:COG1135 181 DLLKDInRELGLTIVLITH-------EMdvvrriCDRVAVLENGRIVEQGPVLDVF 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
57-324 |
1.67e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.36 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 57 SAVDIEFVELSYSVregpcwrkrGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGK--PR 134
Cdd:PRK13536 38 STVAIDLAGVSKSY---------GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD-AGKITVLGVpvPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 135 ELRTFRKMSCYIMQEDILLPHLTVLEAMMISANLKLNEKQEVKkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALE 214
Cdd:PRK13536 108 RARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIE-AVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 215 LVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKGMVTNLIPYL 292
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHfmEEAERL---CDRLCVLEAGRKIAEGRPHALIDEH 263
|
250 260 270
....*....|....*....|....*....|..
gi 157427812 293 KGlglhCPtyhnpadfIIEVASGEYGDLNPLL 324
Cdd:PRK13536 264 IG----CQ--------VIEIYGGDPHELSSLV 283
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
89-278 |
1.94e-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: 90.82 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 89 SGKFCCremigIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGK------PRELRtfRKMScYIMQEDILLPHLTVLEAm 162
Cdd:cd03295 26 KGEFLV-----LIGPSGSGKTTTMKMINRLIEP-TSGEIFIDGEdireqdPVELR--RKIG-YVIQQIGLFPHMTVEEN- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 163 mISANLKLNE-KQEVKKELVTEILTALGLLSCSHTR--TALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQV 239
Cdd:cd03295 96 -IALVPKLLKwPKEKIRERADELLALVGLDPAEFADryPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 157427812 240 ASLMKSLAQG-GRTIICTIHQpsakLFEMF---DKLYILSQGQ 278
Cdd:cd03295 175 QEEFKRLQQElGKTIVFVTHD----IDEAFrlaDRIAIMKNGE 213
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
100-234 |
2.49e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.85 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYRKSG--MKGQILVNGKP-RELRTFRKMSCYIMQEDILLPHLTVLE--AMMISANLKLNEKq 174
Cdd:COG4136 32 LMGPSGSGKSTLLAAIAGTLSPAfsASGEVLLNGRRlTALPAEQRRIGILFQDDLLFPHLSVGEnlAFALPPTIGRAQR- 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 175 evkKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 234
Cdd:COG4136 111 ---RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
96-258 |
4.75e-20 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 90.40 E-value: 4.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKP------RELRTFR--KMScYIMQEDILLPHLTVLEAMMISAN 167
Cdd:cd03294 51 EIFVIMGLSGSGKSTLLRCINRLIEP-TSGKVLIDGQDiaamsrKELRELRrkKIS-MVFQSFALLPHRTVLENVAFGLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 LKlNEKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVAS-LMKSL 246
Cdd:cd03294 129 VQ-GVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDeLLRLQ 207
|
170
....*....|..
gi 157427812 247 AQGGRTIICTIH 258
Cdd:cd03294 208 AELQKTIVFITH 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
77-259 |
8.13e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.64 E-value: 8.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 77 RKR-GYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGK----------------PRELRTF 139
Cdd:PRK10619 12 HKRyGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPS-EGSIVVNGQtinlvrdkdgqlkvadKNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 140 RKMSCYIMQEDILLPHLTVLEAMMISANLKLNEKQEVKKELVTEILTALGLLSCSHTRTAL-LSGGQRKRLAIALELVNN 218
Cdd:PRK10619 91 RTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAME 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157427812 219 PPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQ 259
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
96-277 |
9.82e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.24 E-value: 9.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRK--SG--MKGQILVNGKPRELRTFrKMscyIMQEDILLPHLTVLEAMmiSANLKLN 171
Cdd:PRK11000 30 EFVVFVGPSGCGKSTLLRMIAGLEDitSGdlFIGEKRMNDVPPAERGV-GM---VFQSYALYPHLSVAENM--SFGLKLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 172 --EKQEVKK--ELVTEILTALGLLScshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQ----VASLM 243
Cdd:PRK11000 104 gaKKEEINQrvNQVAEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQmrieISRLH 180
|
170 180 190
....*....|....*....|....*....|....*
gi 157427812 244 KSLaqgGRTIICTIH-QPSAklFEMFDKLYILSQG 277
Cdd:PRK11000 181 KRL---GRTMIYVTHdQVEA--MTLADKIVVLDAG 210
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
96-258 |
1.24e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 89.09 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTL---MNLLagyrKSGMKGQILVNGK----------------PRELRTFRKMSCYIMQEDILLPHL 156
Cdd:COG4598 35 DVISIIGSSGSGKSTFlrcINLL----ETPDSGEIRVGGEeirlkpdrdgelvpadRRQLQRIRTRLGMVFQSFNLWSHM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 157 TVLEAMM---ISAnLKLNeKQEVKkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:COG4598 111 TVLENVIeapVHV-LGRP-KAEAI-ERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP 187
|
170 180
....*....|....*....|....*
gi 157427812 234 ASSFQVASLMKSLAQGGRTIICTIH 258
Cdd:COG4598 188 ELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
96-283 |
1.60e-19 |
|
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: 86.60 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPREL--RTFRKMSCYIMQEdillPHLtvleammisanlklnek 173
Cdd:cd03247 29 EKIALLGRSGSGKSTLLQLLTGDLKP-QQGEITLDGVPVSDleKALSSLISVLNQR----PYL----------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 174 qevkkeLVTEILTALGllscshtrtALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQgGRTI 253
Cdd:cd03247 87 ------FDTTLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK-DKTL 150
|
170 180 190
....*....|....*....|....*....|
gi 157427812 254 ICTIHQPSAklFEMFDKLYILSQGQCIFKG 283
Cdd:cd03247 151 IWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
96-283 |
2.47e-19 |
|
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: 92.50 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRkSGMKGQILVNG------KPRELRtfRKMSCyIMQEDILL------------PHLT 157
Cdd:TIGR01846 484 EFIGIVGPSGSGKSTLTKLLQRLY-TPQHGQVLVDGvdlaiaDPAWLR--RQMGV-VLQENVLFsrsirdnialcnPGAP 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 158 VLEAMMISanlKLNEKQEVKKELVTEILTALGllscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSF 237
Cdd:TIGR01846 560 FEHVIHAA---KLAGAHDFISELPQGYNTEVG------EKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEA 630
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 157427812 238 QVASLMKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 283
Cdd:TIGR01846 631 LIMRNMREICR-GRTVIIIAHRLST--VRACDRIIVLEKGQIAESG 673
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
96-283 |
3.22e-19 |
|
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: 87.29 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSgmKGQILVNG------KPRELRtfRKMScyIMQEDILLPHLTVLEAMM----- 163
Cdd:cd03251 29 ETVALVGPSGSGKSTLVNLIPRfYDVD--SGRILIDGhdvrdyTLASLR--RQIG--LVSQDVFLFNDTVAENIAygrpg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 164 -----ISANLKLNEKQEVKKELVTEILTALGllscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQ 238
Cdd:cd03251 103 atreeVEEAARAANAHEFIMELPEGYDTVIG------ERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 157427812 239 VASLMKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 283
Cdd:cd03251 177 VQAALERLMK-NRTTFVIAHRLST--IENADRIVVLEDGKIVERG 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
99-254 |
3.41e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.23 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 99 GIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGKPRELRTFRK-------MscyIMQEDILLPHLTVLEAMMISANLK- 169
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGvYQPDS--GEILLDGEPVRFRSPRDaqaagiaI---IHQELNLVPNLSVAENIFLGREPRr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 ---LNEKQEVKKelVTEILTALGL-LScSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKS 245
Cdd:COG1129 109 gglIDWRAMRRR--ARELLARLGLdID-PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRR 185
|
....*....
gi 157427812 246 LAQGGRTII 254
Cdd:COG1129 186 LKAQGVAII 194
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
100-278 |
3.90e-19 |
|
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: 89.09 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGK-----PRELRTFRKMscyiMQEDILLPHLTVLEAmmISANLKLN-EK 173
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPD-SGSIMLDGEdvtnvPPHLRHINMV----FQSYALFPHMTVEEN--VAFGLKMRkVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 174 QEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLA-QGGRT 252
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQeQLGIT 153
|
170 180
....*....|....*....|....*.
gi 157427812 253 IICTIHQPSAKLfEMFDKLYILSQGQ 278
Cdd:TIGR01187 154 FVFVTHDQEEAM-TMSDRIAIMRKGK 178
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
96-283 |
4.45e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.98 E-value: 4.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKP-----RELRTFRKMSCYIMQE-DILLPHLTVLEAMMISA-NL 168
Cdd:PRK13636 33 EVTAILGGNGAGKSTLFQNLNGILKP-SSGRILFDGKPidysrKGLMKLRESVGMVFQDpDNQLFSASVYQDVSFGAvNL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 169 KLNEKqEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ 248
Cdd:PRK13636 112 KLPED-EVRKR-VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQK 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 157427812 249 G-GRTIICTIHQ-PSAKLFemFDKLYILSQGQCIFKG 283
Cdd:PRK13636 190 ElGLTIIIATHDiDIVPLY--CDNVFVMKEGRVILQG 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
78-280 |
5.75e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 87.13 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 78 KRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGK------PRELRTFRKMscyimqedi 151
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-SGEVRLNGRpladwsPAELARRRAV--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 152 lLPH-------LTVLE--AMMISANlkLNEKQEVkKELVTEILTALGLLSCSHTRTALLSGG--QRKRLAIAL----ELV 216
Cdd:PRK13548 81 -LPQhsslsfpFTVEEvvAMGRAPH--GLSRAED-DALVAAALAQVDLAHLAGRDYPQLSGGeqQRVQLARVLaqlwEPD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157427812 217 NNPPVMFFDEPTSGLDSASSFQVASLMKSLA-QGGRTIICTIHqpSAKLFEMF-DKLYILSQGQCI 280
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLH--DLNLAARYaDRIVLLHQGRLV 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
76-283 |
5.82e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.37 E-value: 5.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 76 WRKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTL-MNLLAGYRKSgmKGQILVNGKP-----RELRTFRKMSCYIMQE 149
Cdd:PRK13638 8 WFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLLRPQ--KGAVLWQGKPldyskRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 150 -DILLPHLTVLEAMMIS-ANLKLNEKQEVKKelVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEP 227
Cdd:PRK13638 86 pEQQIFYTDIDSDIAFSlRNLGVPEAEITRR--VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157427812 228 TSGLDSASSFQVASLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHG 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
96-233 |
6.88e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 88.67 E-value: 6.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGK-------PRElrtfRKMScYIMQEDILLPHLTVLEammisaN- 167
Cdd:COG1118 29 ELVALLGPSGSGKTTLLRIIAGLETPD-SGRIVLNGRdlftnlpPRE----RRVG-FVFQHYALFPHMTVAE------Ni 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157427812 168 ------LKLNEKQevKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:COG1118 97 afglrvRPPSKAE--IRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
96-283 |
1.15e-18 |
|
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: 85.62 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPR---ELRTFRKMSCYIMQEDILLpHLTVLE-------AM--- 162
Cdd:cd03252 29 EVVGIVGRSGSGKSTLTKLIQRFYVPE-NGRVLVDGHDLalaDPAWLRRQVGVVLQENVLF-NRSIRDnialadpGMsme 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 163 MISANLKLNEKQEVKKELVTEILTALGllscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASL 242
Cdd:cd03252 107 RVIEAAKLAGAHDFISELPEGYDTIVG------EQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157427812 243 MKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 283
Cdd:cd03252 181 MHDICA-GRTVIIIAHRLST--VKNADRIIVMEKGRIVEQG 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
82-260 |
1.42e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.87 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 82 KTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGY-----RKSGMKGQILVNGKPR---ELRTFRKMSCYIMQEDILL 153
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydSKIKVDGKVLYFGKDIfqiDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 154 PHLTVLEAmmISANLK---LNEKQEVKKeLVTEILTALGLLSCSHTR----TALLSGGQRKRLAIALELVNNPPVMFFDE 226
Cdd:PRK14246 103 PHLSIYDN--IAYPLKshgIKEKREIKK-IVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190
....*....|....*....|....*....|....
gi 157427812 227 PTSGLDSASSFQVASLMKSLaQGGRTIICTIHQP 260
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNP 212
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
61-283 |
1.45e-18 |
|
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: 85.28 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 61 IEF--VELSYSVREGpcwrkrgyKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRkSGMKGQILVNGKP-REL- 136
Cdd:cd03249 1 IEFknVSFRYPSRPD--------VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFY-DPTSGEILLDGVDiRDLn 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 137 -RTFRKMSCYIMQEDILLphltvleAMMISANLKL--------NEKQEVKKELVTEILTAL--GLLSCSHTRTALLSGGQ 205
Cdd:cd03249 72 lRWLRSQIGLVSQEPVLF-------DGTIAENIRYgkpdatdeEVEEAAKKANIHDFIMSLpdGYDTLVGERGSQLSGGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157427812 206 RKRLAIALELVNNPPVMFFDEPTSGLDSASSFQV-ASLMKslAQGGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 283
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVqEALDR--AMKGRTTIVIAHRLST--IRNADLIAVLQNGQVVEQG 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
100-260 |
1.80e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.82 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPRelrtfrkmSCYIMQ---EDILLPhLTVLEAMMISANLKLNEKQEV 176
Cdd:NF040873 23 VVGPNGSGKSTLLKVLAGVLRP-TSGTVRRAGGAR--------VAYVPQrseVPDSLP-LTVRDLVAMGRWARRGLWRRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 177 KKE---LVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTI 253
Cdd:NF040873 93 TRDdraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATV 172
|
....*..
gi 157427812 254 ICTIHQP 260
Cdd:NF040873 173 VVVTHDL 179
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
96-313 |
2.03e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.81 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNG----KPRELRTFRKMSCYIMQE-DILLPHLTVLEAMMISA-NLK 169
Cdd:PRK13644 29 EYIGIIGKNGSGKSTLALHLNGLLRP-QKGKVLVSGidtgDFSKLQGIRKLVGIVFQNpETQFVGRTVEEDLAFGPeNLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 LnEKQEVKKeLVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQG 249
Cdd:PRK13644 108 L-PPIEIRK-RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157427812 250 GRTIICTIHqpSAKLFEMFDKLYILSQGQCIFKGMVTNLI--PYLKGLGLHCPTyhnpadfIIEVA 313
Cdd:PRK13644 186 GKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEPENVLsdVSLQTLGLTPPS-------LIELA 242
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
96-260 |
2.15e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.45 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYrKSGMKGQILVNGKP---------RELRTfrKMSCYIMQEDILLPHLTVLEAMMISA 166
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGL-DDGSSGEVSLVGQPlhqmdeearAKLRA--KHVGFVFQSFMLIPTLNALENVELPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 167 NLKlNEKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL 246
Cdd:PRK10584 114 LLR-GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSL 192
|
170
....*....|....*
gi 157427812 247 AQG-GRTIICTIHQP 260
Cdd:PRK10584 193 NREhGTTLILVTHDL 207
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
80-283 |
2.25e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 80 GYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPRELRTFRKMSCYIMqediLLP-HLTV 158
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP-QSGTVFLGDKPISMLSSRQLARRLA----LLPqHHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 159 LEAMMI--------SANL----KLNEKQEvkkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDE 226
Cdd:PRK11231 88 PEGITVrelvaygrSPWLslwgRLSAEDN---ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 227 PTSGLDSASSFQVASLMKSLAQGGRTIICTIH---QPSaklfEMFDKLYILSQGQCIFKG 283
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVMAQG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
96-260 |
3.01e-18 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 88.19 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRkSGMKGQILVNGKP---RELRTFRKMSCYIMQEdillPHL---TVLEammisaNLK 169
Cdd:TIGR02868 362 ERVAILGPSGSGKSTLLATLAGLL-DPLQGEVTLDGVPvssLDQDEVRRRVSVCAQD----AHLfdtTVRE------NLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 LNeKQEVKKELVTEILTALGL----------LSCS-HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSfq 238
Cdd:TIGR02868 431 LA-RPDATDEELWAALERVGLadwlralpdgLDTVlGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETA-- 507
|
170 180
....*....|....*....|....
gi 157427812 239 vASLMKSLAQG--GRTIICTIHQP 260
Cdd:TIGR02868 508 -DELLEDLLAAlsGRTVVLITHHL 530
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
96-278 |
5.49e-18 |
|
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: 83.54 E-value: 5.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPRELRTFRKMSC-YIMQEDILLPHLTVLEAmmISANLKLNEKQ 174
Cdd:cd03296 29 ELVALLGPSGSGKTTLLRLIAGLERPD-SGTILFGGEDATDVPVQERNVgFVFQHYALFRHMTVFDN--VAFGLRVKPRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 175 EV-----KKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ- 248
Cdd:cd03296 106 ERppeaeIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDe 185
|
170 180 190
....*....|....*....|....*....|.
gi 157427812 249 -GGRTIICTIHQPSAklFEMFDKLYILSQGQ 278
Cdd:cd03296 186 lHVTTVFVTHDQEEA--LEVADRVVVMNKGR 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
42-283 |
5.55e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.57 E-value: 5.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 42 NHITEAQ---RFS--HLPKRSAVDIEF--VELSYSVREGPcwrkrgyktLLKCLSGKFCCREMIGIMGPSGSGKSTLMNL 114
Cdd:PRK11160 315 NEITEQKpevTFPttSTAAADQVSLTLnnVSFTYPDQPQP---------VLKGLSLQIKAGEKVALLGRTGCGKSTLLQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 115 LAGYRKSGmKGQILVNGKP----RElRTFRKMSCYIMQEdillPHL---TVLEammisaNLKLNEKQEVKKELvTEILTA 187
Cdd:PRK11160 386 LTRAWDPQ-QGEILLNGQPiadySE-AALRQAISVVSQR----VHLfsaTLRD------NLLLAAPNASDEAL-IEVLQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 188 LGLLSCSHTRTAL----------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQgGRTIICTI 257
Cdd:PRK11160 453 VGLEKLLEDDKGLnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMIT 531
|
250 260
....*....|....*....|....*.
gi 157427812 258 HQpsAKLFEMFDKLYILSQGQCIFKG 283
Cdd:PRK11160 532 HR--LTGLEQFDRICVMDNGQIIEQG 555
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
95-283 |
5.67e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 83.81 E-value: 5.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 95 REMIGIMGPSGSGKSTLMN----LLAGYRKSGMKGQILVNGK---PRELRTFRKMSCYIMQEDILLPHLTVLEAmmISAN 167
Cdd:PRK14247 29 NTITALMGPSGSGKSTLLRvfnrLIELYPEARVSGEVYLDGQdifKMDVIELRRRVQMVFQIPNPIPNLSIFEN--VALG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 LKLNEKQEVKKEL---VTEILTALGLLSCSHTR----TALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVA 240
Cdd:PRK14247 107 LKLNRLVKSKKELqerVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 157427812 241 SLMKSLAQgGRTIICTIHQPsAKLFEMFDKLYILSQGQCIFKG 283
Cdd:PRK14247 187 SLFLELKK-DMTIVLVTHFP-QQAARISDYVAFLYKGQIVEWG 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
96-278 |
7.56e-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: 85.55 E-value: 7.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNG-------KPRELRTFRKMSCYIMQEDILLPHLTVLEAMMISANL 168
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPD-EGEIVLNGrtlfdsrKGIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 169 KLNEKQEVKKELVTEILTALGLLScshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ 248
Cdd:TIGR02142 103 ARPSERRISFERVIELLGIGHLLG---RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHA 179
|
170 180 190
....*....|....*....|....*....|
gi 157427812 249 GGRTIICTIHQPSAKLFEMFDKLYILSQGQ 278
Cdd:TIGR02142 180 EFGIPILYVSHSLQEVLRLADRVVVLEDGR 209
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
96-283 |
8.41e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.40 E-value: 8.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGK-----PRELRTFRKMScYIMQEDILLPHLTVLEAMMISANLKL 170
Cdd:PRK10895 30 EIVGLLGPNGAGKTTTFYMVVGIVPRD-AGNIIIDDEdisllPLHARARRGIG-YLPQEASIFRRLSVYDNLMAVLQIRD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 171 NEKQEVKKELVTEILTALGLlscSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLA 247
Cdd:PRK10895 108 DLSAEQREDRANELMEEFHI---EHLRDSMgqsLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLR 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 157427812 248 QGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 283
Cdd:PRK10895 185 DSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHG 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
96-248 |
1.10e-17 |
|
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: 84.33 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTL----MNLLAGYRKSGmkGQILVNGK------PRELRTFR--KMScYIMQEDI--LLPHLTVLEA 161
Cdd:COG0444 32 ETLGLVGESGSGKSTLaraiLGLLPPPGITS--GEILFDGEdllklsEKELRKIRgrEIQ-MIFQDPMtsLNPVMTVGDQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 162 MM--ISANLKLNEKQevKKELVTEILTALGLlscSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:COG0444 109 IAepLRIHGGLSKAE--ARERAIELLERVGL---PDPERRLdrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDV 183
|
170
....*....|....*
gi 157427812 234 ASSFQVASLMKSLAQ 248
Cdd:COG0444 184 TIQAQILNLLKDLQR 198
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
77-289 |
1.10e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.09 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 77 RKR-GYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYrKSGMKGQILVNGK--PRELRTFRKMSCYIMQEDILL 153
Cdd:PRK13537 14 EKRyGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL-THPDAGSISLCGEpvPSRARHARQRVGVVPQFDNLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 154 PHLTVLEAMMISAN-LKLNEKQevKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK13537 93 PDFTVRENLLVFGRyFGLSAAA--ARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 157427812 233 SASSFQVASLMKSLAQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKGMVTNLI 289
Cdd:PRK13537 171 PQARHLMWERLRSLLARGKTILLTTHfmEEAERL---CDRLCVIEEGRKIAEGAPHALI 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
96-277 |
1.29e-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: 82.51 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRK--SG---MKGQILVNGKPRELRTFRKMScyimqediLLPHLTVLEAMMISANLKL 170
Cdd:TIGR01184 12 EFISLIGHSGCGKSTLLNLISGLAQptSGgviLEGKQITEPGPDRMVVFQNYS--------LLPWLTVRENIALAVDRVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 171 NE-KQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD--SASSFQvASLMKSLA 247
Cdd:TIGR01184 84 PDlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDalTRGNLQ-EELMQIWE 162
|
170 180 190
....*....|....*....|....*....|
gi 157427812 248 QGGRTIICTIHQPSAKLFeMFDKLYILSQG 277
Cdd:TIGR01184 163 EHRVTVLMVTHDVDEALL-LSDRVVMLTNG 191
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
92-283 |
1.43e-17 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 82.03 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 92 FCCR--EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNG-----KPRELRtfRKMScYIMQEDILLPHLTVLEAMMI 164
Cdd:cd03266 26 FTVKpgEVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDGfdvvkEPAEAR--RRLG-FVSDSTGLYDRLTARENLEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 165 SANLKLNEKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMK 244
Cdd:cd03266 102 FAGLYGLKGDELTAR-LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157427812 245 SLAQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKG 283
Cdd:cd03266 181 QLRALGKCILFSTHimQEVERL---CDRVVVLHRGRVVYEG 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
82-258 |
1.81e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.91 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 82 KTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLaGYRKSGMKGQILVNGKPREL---RTFRKMSCYIMQEdilLPH--- 155
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQPLESwssKAFARKVAYLPQQ---LPAaeg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 156 LTVLEAMMISA---NLKLNEKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK10575 100 MTVRELVAIGRypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180
....*....|....*....|....*..
gi 157427812 233 SASSFQVASLMKSLAQG-GRTIICTIH 258
Cdd:PRK10575 180 IAHQVDVLALVHRLSQErGLTVIAVLH 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-283 |
3.11e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 85.28 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 17 AVAMAVALEDGAEPPVLTTHLKKVEnhiteaqrfshLPKRSAVDIEFVELSYSVREGpcwrkrgyKTLLKCLSGKFCCRE 96
Cdd:PRK11174 317 AVGAAESLVTFLETPLAHPQQGEKE-----------LASNDPVTIEAEDLEILSPDG--------KTLAGPLNFTLPAGQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 97 MIGIMGPSGSGKSTLMNLLAG---YRksgmkGQILVNGkpRELR-----TFRKMSCYIMQEDiLLPHLTVLEAMMIsANL 168
Cdd:PRK11174 378 RIALVGPSGAGKTSLLNALLGflpYQ-----GSLKING--IELReldpeSWRKHLSWVGQNP-QLPHGTLRDNVLL-GNP 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 169 KLNE---KQEVKKELVTEILTAL--GLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLM 243
Cdd:PRK11174 449 DASDeqlQQALENAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAL 528
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 157427812 244 KSLAQGGRTIICTiHQPSAkLFEMfDKLYILSQGQCIFKG 283
Cdd:PRK11174 529 NAASRRQTTLMVT-HQLED-LAQW-DQIWVMQDGQIVQQG 565
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
100-233 |
3.46e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.83 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYrKSGMKGQILVNGKP-------RELrtfrkmscyIMQEDILLPHLTVLEAmmISANLKLN- 171
Cdd:COG4525 38 ALGASGCGKTTLLNLIAGF-LAPSSGEITLDGVPvtgpgadRGV---------VFQKDALLPWLNVLDN--VAFGLRLRg 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157427812 172 -EKQEvKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:COG4525 106 vPKAE-RRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
96-278 |
3.65e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.84 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGK-----PRELR---TfrkmscyIMQEDILLPHLTVLEAMMISAN 167
Cdd:PRK09452 41 EFLTLLGPSGCGKTTVLRLIAGFETPD-SGRIMLDGQdithvPAENRhvnT-------VFQSYALFPHMTVFENVAFGLR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 LKLNEKQEVKkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLA 247
Cdd:PRK09452 113 MQKTPAAEIT-PRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQ 191
|
170 180 190
....*....|....*....|....*....|...
gi 157427812 248 -QGGRTIICTIH-QPSAklFEMFDKLYILSQGQ 278
Cdd:PRK09452 192 rKLGITFVFVTHdQEEA--LTMSDRIVVMRDGR 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
96-283 |
3.84e-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: 86.22 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPRE--LRTFRKMSCYIMQEDILLPHLTVLEAMMISANLKLNEK 173
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPP-TSGTVLVGGKDIEtnLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 174 QEVKKELvTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTI 253
Cdd:TIGR01257 1036 EEAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTII 1114
|
170 180 190
....*....|....*....|....*....|
gi 157427812 254 ICTIHQPSAKLfeMFDKLYILSQGQCIFKG 283
Cdd:TIGR01257 1115 MSTHHMDEADL--LGDRIAIISQGRLYCSG 1142
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
98-283 |
1.21e-16 |
|
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: 79.58 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 98 IGIMGPSGSGKSTLMNLLagYR-KSGMKGQILVNGKP-RE--LRTFRKMSCYIMQeDILLPHLTVLEAMMIsANLKLNEK 173
Cdd:cd03253 30 VAIVGPSGSGKSTILRLL--FRfYDVSSGSILIDGQDiREvtLDSLRRAIGVVPQ-DTVLFNDTIGYNIRY-GRPDATDE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 174 Q--EVKK--ELVTEIL-------TALGllscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASL 242
Cdd:cd03253 106 EviEAAKaaQIHDKIMrfpdgydTIVG------ERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 157427812 243 MKSLAQgGRTIICTIHQPS----AklfemfDKLYILSQGQCIFKG 283
Cdd:cd03253 180 LRDVSK-GRTTIVIAHRLStivnA------DKIIVLKDGRIVERG 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
98-285 |
1.41e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 80.23 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 98 IGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKP---RELRTFRKMSCYIMQ---EDILLPhlTVLEAMMIS-ANLKL 170
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKP-TSGSVLIRGEPitkENIREVRKFVGLVFQnpdDQIFSP--TVEQDIAFGpINLGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 171 NEkqEVKKELVTEILTALGLlscSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLA 247
Cdd:PRK13652 110 DE--ETVAHRVSSALHMLGL---EELRDRVphhLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLP 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 157427812 248 QG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKGMV 285
Cdd:PRK13652 185 ETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTV 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
96-287 |
1.69e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.39 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTL---MNLLAgyRKSGmkGQILVNG------KPRELRTFRKMSCYIMQEDILLPHLTVLEAmmISA 166
Cdd:PRK11153 32 EIFGVIGASGAGKSTLircINLLE--RPTS--GRVLVDGqdltalSEKELRKARRQIGMIFQHFNLLSSRTVFDN--VAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 167 NLKLN--EKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMK 244
Cdd:PRK11153 106 PLELAgtPKAEIKAR-VTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 157427812 245 SL-AQGGRTIICTIHqpsaklfEM------FDKLYILSQGQCIFKGMVTN 287
Cdd:PRK11153 185 DInRELGLTIVLITH-------EMdvvkriCDRVAVIDAGRLVEQGTVSE 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
96-260 |
2.02e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.31 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRkSGMKGQILVNGKP-RELRT-FRKMSCYIMQEDILLPHLTVLEammisaNLKLNEK 173
Cdd:PRK13538 28 ELVQIEGPNGAGKTSLLRILAGLA-RPDAGEVLWQGEPiRRQRDeYHQDLLYLGHQPGIKTELTALE------NLRFYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 174 --QEVKKELVTEILTALGL-----LSCSHtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL 246
Cdd:PRK13538 101 lhGPGDDEALWEALAQVGLagfedVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQH 175
|
170
....*....|....
gi 157427812 247 AQGGRTIICTIHQP 260
Cdd:PRK13538 176 AEQGGMVILTTHQD 189
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
96-291 |
2.56e-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: 82.87 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPR---ELRTFRKMSCYIMQEDILLPHlTVLEAMMISANLKLNE 172
Cdd:TIGR01193 501 SKTTIVGMSGSGKSTLAKLLVGFFQAR-SGEILLNGFSLkdiDRHTLRQFINYLPQEPYIFSG-SILENLLLGAKENVSQ 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 173 kQEVKKEL-VTEILTALGLLSCS-HTRTAL----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL 246
Cdd:TIGR01193 579 -DEIWAACeIAEIKDDIENMPLGyQTELSEegssISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL 657
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 157427812 247 AQggRTIICTIHQPSakLFEMFDKLYILSQGQCIFKGMVTNLIPY 291
Cdd:TIGR01193 658 QD--KTIIFVAHRLS--VAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
61-239 |
2.66e-16 |
|
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: 78.28 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 61 IEFVELSYSvregpcWRKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKP---RELR 137
Cdd:cd03248 12 VKFQNVTFA------YPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQP-QGGQVLLDGKPisqYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 138 TFRKMSCYIMQEDILLPH---------LTVLEAMMISANLKLNEKQEVKKELVTEILTALGllscshTRTALLSGGQRKR 208
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARslqdniaygLQSCSFECVKEAAQKAHAHSFISELASGYDTEVG------EKGSQLSGGQKQR 158
|
170 180 190
....*....|....*....|....*....|.
gi 157427812 209 LAIALELVNNPPVMFFDEPTSGLDSASSFQV 239
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQV 189
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
95-248 |
2.73e-16 |
|
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: 80.92 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 95 REMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP---RELRTF-----RKMScYIMQEDILLPHLTVLEammisa 166
Cdd:COG4148 25 RGVTALFGPSGSGKTTLLRAIAGLERPD-SGRIRLGGEVlqdSARGIFlpphrRRIG-YVFQEARLFPHLSVRG------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 167 NLKLNEKQEVK---KELVTEILTALG---LLscsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVA 240
Cdd:COG4148 97 NLLYGRKRAPRaerRISFDEVVELLGighLL---DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
....*...
gi 157427812 241 SLMKSLAQ 248
Cdd:COG4148 174 PYLERLRD 181
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
96-277 |
2.87e-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: 82.70 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGMkGQILVNGKPRE---LRTFRKMSCYIMQEDILLPHlTVLEAMMISANLKLNE 172
Cdd:TIGR03797 480 EFVAIVGPSGSGKSTLLRLLLGFETPES-GSVFYDGQDLAgldVQAVRRQLGVVLQNGRLMSG-SIFENIAGGAPLTLDE 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 173 KQEVKKEL-VTEILTAL--GLlscsHTRTA----LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSfqvASLMKS 245
Cdd:TIGR03797 558 AWEAARMAgLAEDIRAMpmGM----HTVISegggTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQ---AIVSES 630
|
170 180 190
....*....|....*....|....*....|....*.
gi 157427812 246 LAQGGRTIICTIHQPS----AklfemfDKLYILSQG 277
Cdd:TIGR03797 631 LERLKVTRIVIAHRLStirnA------DRIYVLDAG 660
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
96-258 |
4.36e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.61 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNG------KPRELRTFRKMSCYIMQEDILLPHLTVLEAMMISANLK 169
Cdd:PRK10908 29 EMAFLTGHSGAGKSTLLKLICGIERPS-AGKIWFSGhditrlKNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 LNEKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQG 249
Cdd:PRK10908 108 GASGDDIRRR-VSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV 186
|
....*....
gi 157427812 250 GRTIICTIH 258
Cdd:PRK10908 187 GVTVLMATH 195
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
100-283 |
6.96e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.12 E-value: 6.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYRKSGmKGQILV----------------NGKPRELRTF---RKMSCYIMQ-EDILLPHLTVL 159
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSK-YGTIQVgdiyigdkknnhelitNPYSKKIKNFkelRRRVSMVFQfPEYQLFKDTIE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 160 EAMMISAnLKLNEKQEVKKELVTEILTALGLLSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQ 238
Cdd:PRK13631 136 KDIMFGP-VALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFgLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHE 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 157427812 239 VASLMKSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKG 283
Cdd:PRK13631 215 MMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTG 258
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
96-232 |
7.01e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.88 E-value: 7.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYrKSGMKGQILVNGK-----PRELRTFRKMscyiMQEDILLPHLTVLEAmmISANLKL 170
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGF-EQPTAGQIMLDGVdlshvPPYQRPINMM----FQSYALFPHMTVEQN--IAFGLKQ 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157427812 171 NE--KQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK11607 119 DKlpKAEIASR-VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
67-248 |
8.41e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 80.50 E-value: 8.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 67 SYSVREGPCWRKRGYKTLLKCLSgkFCCR--EMIGIMGPSGSGKSTL----MNLLAGyrksgmKGQILVNGKP------R 134
Cdd:COG4172 284 WFPIKRGLFRRTVGHVKAVDGVS--LTLRrgETLGLVGESGSGKSTLglalLRLIPS------EGEIRFDGQDldglsrR 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 135 ELRTFRKMscyiMQedI--------LLPHLTVLEamMISANLKLNEKQEVKKE---LVTEILTALGLlscshTRTAL--- 200
Cdd:COG4172 356 ALRPLRRR----MQ--VvfqdpfgsLSPRMTVGQ--IIAEGLRVHGPGLSAAErraRVAEALEEVGL-----DPAARhry 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 157427812 201 ---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ 248
Cdd:COG4172 423 pheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQR 473
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
96-277 |
8.90e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.43 E-value: 8.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPRELRTFRKmsCYIMQEDILLPHLTVLEAMMISANLKLNEKQE 175
Cdd:PRK11248 28 ELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPVEGPGAER--GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 176 vKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQG-GRTII 254
Cdd:PRK11248 105 -RLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVL 183
|
170 180
....*....|....*....|...
gi 157427812 255 CTIHQPSAKLFeMFDKLYILSQG 277
Cdd:PRK11248 184 LITHDIEEAVF-MATELVLLSPG 205
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
99-341 |
1.03e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.24 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 99 GIMGPSGSGKSTLMNLLAGYRKSGMK----GQILVNG--KPRELRTFRKMSCYIMQ--EDILLPHLTVLEAMMISANLKL 170
Cdd:PRK13643 36 ALIGHTGSGKSTLLQHLNGLLQPTEGkvtvGDIVVSStsKQKEIKPVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 171 NeKQEVKKeLVTEILTALGLLSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQG 249
Cdd:PRK13643 116 P-KEKAEK-IAAEKLEMVGLADEFWEKSPFeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 250 GRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKGMVTNL---IPYLKGLGLHCPTYHNPADFIIEVASGEYGDLnPLLFR 326
Cdd:PRK13643 194 GQTVVLVTHLMD-DVADYADYVYLLEKGHIISCGTPSDVfqeVDFLKAHELGVPKATHFADQLQKTGAVTFEKL-PITRA 271
|
250
....*....|....*
gi 157427812 327 AVQNGLCAMAEKNSG 341
Cdd:PRK13643 272 ELVTLLTSLSVNSGG 286
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
96-254 |
1.31e-15 |
|
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: 75.16 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPRELRTFRKMS----CYI---MQEDILLPHLTVLEAMMISAnl 168
Cdd:cd03215 27 EIVGIAGLVGNGQTELAEALFGLRPP-ASGEITLDGKPVTRRSPRDAIragiAYVpedRKREGLVLDLSVAENIALSS-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 169 klnekqevkkelvteiltalgllscshtrtaLLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ 248
Cdd:cd03215 104 -------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD 152
|
....*.
gi 157427812 249 GGRTII 254
Cdd:cd03215 153 AGKAVL 158
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
96-283 |
1.32e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.61 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGK------------------PRELRTFRKMScyiMQEDILLphlt 157
Cdd:COG1137 30 EIVGLLGPNGAGKTTTFYMIVGLVKPD-SGRIFLDGEdithlpmhkrarlgigylPQEASIFRKLT---VEDNILA---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 158 VLEAmmisanLKLNEKQevKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD--SAS 235
Cdd:COG1137 102 VLEL------RKLSKKE--REERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiAVA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 157427812 236 SFQvaSLMKSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 283
Cdd:COG1137 174 DIQ--KIIRHLKERGIGVLITDHNVRETL-GICDRAYIISEGKVLAEG 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
95-254 |
1.77e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.61 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 95 REMIGIMGPSGSGKSTL------MN-LLAGYRksgMKGQILVNGK--------PRELRT-----FRK-----MSCYimqE 149
Cdd:COG1117 37 NKVTALIGPSGCGKSTLlrclnrMNdLIPGAR---VEGEILLDGEdiydpdvdVVELRRrvgmvFQKpnpfpKSIY---D 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 150 DILLPhltvleammisanLKLNE--KQEVKKELVTEILTALGL-------LscsHTRTALLSGGQRKRLAIALELVNNPP 220
Cdd:COG1117 111 NVAYG-------------LRLHGikSKSELDEIVEESLRKAALwdevkdrL---KKSALGLSGGQQQRLCIARALAVEPE 174
|
170 180 190
....*....|....*....|....*....|....
gi 157427812 221 VMFFDEPTSGLDSASSFQVASLMKSLAQgGRTII 254
Cdd:COG1117 175 VLLMDEPTSALDPISTAKIEELILELKK-DYTIV 207
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
82-256 |
2.26e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.67 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 82 KTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLL-------AGYRKSGmkgQILVNGKP----RELRTFRKMSCYIMQED 150
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRYSG---DVLLGGRSifnyRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 151 ILLPhLTVLEAMMISANL-KLNEKQEVKKeLVTEILTALGLLSCSHTRTA----LLSGGQRKRLAIALELVNNPPVMFFD 225
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAhKLVPRKEFRG-VAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190
....*....|....*....|....*....|.
gi 157427812 226 EPTSGLDSASSFQVASLMKSLAQGGRTIICT 256
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVT 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
58-283 |
2.42e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 77.07 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 58 AVDiefvELSYSVREGpcwrkrgyktllkclsgkfccrEMIGIMGPSGSGKSTLM----NLLAGYrksgmKGQILVNGKP 133
Cdd:COG4152 16 AVD----DVSFTVPKG----------------------EIFGLLGPNGAGKTTTIriilGILAPD-----SGEVLWDGEP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 134 RELRTFRKMScYIMQEDILLPHLTVLEAMMISANLKLNEKQEVKKELvTEILTALGLLSCSHTRTALLSGGQRKRLAIAL 213
Cdd:COG4152 65 LDPEDRRRIG-YLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRA-DEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157427812 214 ELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQ-PSAKlfEMFDKLYILSQGQCIFKG 283
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQmELVE--ELCDRIVIINKGRKVLSG 211
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
92-278 |
2.54e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.18 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 92 FCCR--EMIGIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGKPRELRTFRKM----SCYIMQEDILLPHLTVLEAMMI 164
Cdd:PRK11288 25 FDCRagQVHALMGENGAGKSTLLKILSGnYQPDA--GSILIDGQEMRFASTTAAlaagVAIIYQELHLVPEMTVAENLYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 165 S---ANLKLNEKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVAS 241
Cdd:PRK11288 103 GqlpHKGGIVNRRLLNYE-AREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFR 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 157427812 242 LMKSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQ 278
Cdd:PRK11288 182 VIRELRAEGRVILYVSHR-MEEIFALCDAITVFKDGR 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
96-280 |
3.11e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 73.62 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPRELRTFRkmscyimqedillphltvlEAMmisanlklnekqe 175
Cdd:cd03216 27 EVHALLGENGAGKSTLMKILSGLYKPD-SGEILVDGKEVSFASPR-------------------DAR------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 176 vkkelvteiltALGLlSCSHTrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIIC 255
Cdd:cd03216 74 -----------RAGI-AMVYQ----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIF 137
|
170 180
....*....|....*....|....*...
gi 157427812 256 TIHqpsaKLFEMF---DKLYILSQGQCI 280
Cdd:cd03216 138 ISH----RLDEVFeiaDRVTVLRDGRVV 161
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
79-232 |
3.20e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 79 RGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVngkPRELRtfrkMScYIMQEDILLPHLTV 158
Cdd:COG0488 8 FGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD-SGEVSI---PKGLR----IG-YLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 159 LEAMMIS-------------ANLKLNEKQEVKKEL------------------VTEILTALGLLSCSHTR-TALLSGGQR 206
Cdd:COG0488 79 LDTVLDGdaelraleaeleeLEAKLAEPDEDLERLaelqeefealggweaearAEEILSGLGFPEEDLDRpVSELSGGWR 158
|
170 180
....*....|....*....|....*.
gi 157427812 207 KRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
95-302 |
3.81e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 76.24 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 95 REMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNG-----KPRELRTFRKMSCYIMQedilLPHLTVLEAMM---IS- 165
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKP-TSGKIIIDGvditdKKVKLSDIRKKVGLVFQ----YPEYQLFEETIekdIAf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 166 --ANLKLNEkQEVKKElVTEILTALGL-LSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVAS 241
Cdd:PRK13637 108 gpINLGLSE-EEIENR-VKRAMNIVGLdYEDYKDKSPFeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILN 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157427812 242 LMKSLAQG-GRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKGM---VTNLIPYLKGLGLHCP--TY 302
Cdd:PRK13637 186 KIKELHKEyNMTIILVSHsmEDVAKL---ADRIIVMNKGKCELQGTpreVFKEVETLESIGLAVPqvTY 251
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
96-283 |
4.50e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.77 E-value: 4.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNG---------KPRELRtfRKMSCYIMQEDILLPHLTVLEAMMISA 166
Cdd:PRK10070 55 EIFVIMGLSGSGKSTMVRLLNRLIEP-TRGQVLIDGvdiakisdaELREVR--RKKIAMVFQSFALMPHMTVLDNTAFGM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 167 NLKLNEKQEvKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVA-SLMKS 245
Cdd:PRK10070 132 ELAGINAEE-RREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKL 210
|
170 180 190
....*....|....*....|....*....|....*...
gi 157427812 246 LAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 283
Cdd:PRK10070 211 QAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVG 247
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
77-278 |
6.23e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.10 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 77 RKR-GYKTLLKCL-----SGKFccremIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPreLRTFRKMSCYIMQED 150
Cdd:PRK11247 19 SKRyGERTVLNQLdlhipAGQF-----VAVVGRSGCGKSTLLRLLAGLETPS-AGELLAGTAP--LAEAREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 151 ILLPHLTVLEammisaNLKLNEKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSG 230
Cdd:PRK11247 91 RLLPWKKVID------NVGLGLKGQWRDA-ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157427812 231 LDSASSFQVASLMKSL-AQGGRTIICTIHQPSAKLfEMFDKLYILSQGQ 278
Cdd:PRK11247 164 LDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAV-AMADRVLLIEEGK 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
96-233 |
6.78e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 76.68 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPRELRTFRKMS-CYIMQEDILLPHLTVLEAmmISANLK-LNEK 173
Cdd:PRK11432 33 TMVTLLGPSGCGKTTVLRLVAGLEKP-TEGQIFIDGEDVTHRSIQQRDiCMVFQSYALFPHMSLGEN--VGYGLKmLGVP 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 174 QEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:PRK11432 110 KEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
96-283 |
9.19e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 74.25 E-value: 9.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKP-RELRTFRKMS---CYIMQEDILLPHLTVLEammisaNLKL- 170
Cdd:COG0410 30 EIVALLGRNGAGKTTLLKAISGLLPP-RSGSIRFDGEDiTGLPPHRIARlgiGYVPEGRRIFPSLTVEE------NLLLg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 171 ----NEKQEVKK--ELVTEILTALGLLScsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLdsASSF--QVASL 242
Cdd:COG0410 103 ayarRDRAEVRAdlERVYELFPRLKERR--RQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL--APLIveEIFEI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157427812 243 MKSLAQGGRTIICtIHQPSAKLFEMFDKLYILSQGQCIFKG 283
Cdd:COG0410 179 IRRLNREGVTILL-VEQNARFALEIADRAYVLERGRIVLEG 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
61-288 |
9.73e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.20 E-value: 9.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 61 IEFVELSYSVREGPCWRKRGYKTL-LKCLSGKFccremIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNG-------K 132
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQAIHDVnTEFEQGKY-----YAIVGQTGSGKSTLIQNINALLKP-TTGTVTVDDitithktK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 133 PRELRTFRKMSCYIMQ--EDILLPHLTVLEAMMISANLKLNEKQevKKELVTEILTALG----LLSCSHTRtalLSGGQR 206
Cdd:PRK13646 77 DKYIRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDE--VKNYAHRLLMDLGfsrdVMSQSPFQ---MSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 207 KRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLA-QGGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKGMV 285
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMN-EVARYADEVIVMKEGSIVSQTSP 230
|
...
gi 157427812 286 TNL 288
Cdd:PRK13646 231 KEL 233
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
67-283 |
1.03e-14 |
|
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: 73.91 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 67 SYSVREGPCW----------RKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGK-P- 133
Cdd:cd03267 9 SYRVYSKEPGligslkslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPTS--GEVRVAGLvPw 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 134 -RELRTFRKMSCYIMQEDILLPHLTVLEAMMISANLKLNEKQEVKKEL--VTEILTALGLLscsHTRTALLSGGQRKRLA 210
Cdd:cd03267 87 kRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLdeLSELLDLEELL---DTPVRQLSLGQRMRAE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157427812 211 IALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL-AQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKG 283
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHymKDIEAL---ARRVLVIDKGRLLYDG 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
51-288 |
1.08e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.45 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 51 SHLPKRSAVDIEFVELSYSvregpcWRKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAG-YRKSGmkGQILV 129
Cdd:TIGR00958 469 TLAPLNLEGLIEFQDVSFS------YPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlYQPTG--GQVLL 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 130 NGKPreLRTFRkmSCYIMQEDILLPHLTVLEAMMISAN----LKLNEKQEVkkelvteilTALGLLSCSHT--------- 196
Cdd:TIGR00958 541 DGVP--LVQYD--HHYLHRQVALVGQEPVLFSGSVRENiaygLTDTPDEEI---------MAAAKAANAHDfimefpngy 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 197 ------RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKslaQGGRTIICTIHQPSakLFEMFDK 270
Cdd:TIGR00958 608 dtevgeKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS---RASRTVLLIAHRLS--TVERADQ 682
|
250
....*....|....*...
gi 157427812 271 LYILSQGQCIFKGMVTNL 288
Cdd:TIGR00958 683 ILVLKKGSVVEMGTHKQL 700
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
96-278 |
1.24e-14 |
|
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: 77.00 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNG---KPRELRTFRKMSCYIMQeDILLPHLTV----------LEAM 162
Cdd:TIGR01842 345 EALAIIGPSGSGKSTLARLIVGIWPP-TSGSVRLDGadlKQWDRETFGKHIGYLPQ-DVELFPGTVaeniarfgenADPE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 163 MISANLKLNEKQEVKKELVTEILTALGllscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASL 242
Cdd:TIGR01842 423 KIIEAAKLAGVHELILRLPDGYDTVIG------PGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANA 496
|
170 180 190
....*....|....*....|....*....|....*.
gi 157427812 243 MKSLAQGGRTIICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:TIGR01842 497 IKALKARGITVVVITHRPS--LLGCVDKILVLQDGR 530
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
96-278 |
1.45e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGK---PR-ELRTFRKMSCYIMQ---EDILLPHLTVLEAMMISANL 168
Cdd:PRK09700 290 EILGFAGLVGSGRTELMNCLFGVDKR-AGGEIRLNGKdisPRsPLDAVKKGMAYITEsrrDNGFFPNFSIAQNMAISRSL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 169 KL----------NEKQEVKkelVTEILTALGLLSCSHTRTAL--LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASS 236
Cdd:PRK09700 369 KDggykgamglfHEVDEQR---TAENQRELLALKCHSVNQNIteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAK 445
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 157427812 237 FQVASLMKSLAQGGRTIICTihqpSAKLFEMF---DKLYILSQGQ 278
Cdd:PRK09700 446 AEIYKVMRQLADDGKVILMV----SSELPEIItvcDRIAVFCEGR 486
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
96-258 |
1.60e-14 |
|
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: 73.35 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPRelRTFRKMSCYIMQED-------ILLPHlTVL--EAMMISA 166
Cdd:TIGR03771 7 ELLGLLGPNGAGKTTLLRAILGLIPPA-KGTVKVAGASP--GKGWRHIGYVPQRHefawdfpISVAH-TVMsgRTGHIGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 167 nlkLNEKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL 246
Cdd:TIGR03771 83 ---LRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIEL 159
|
170
....*....|..
gi 157427812 247 AQGGRTIICTIH 258
Cdd:TIGR03771 160 AGAGTAILMTTH 171
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
96-289 |
2.04e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.74 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG--YRKSGmkgQILVNGK-P-RELRTFRKMSCYIM-QEDILLPHLTVLEammisaNLKL 170
Cdd:COG4586 49 EIVGFIGPNGAGKSTTIKMLTGilVPTSG---EVRVLGYvPfKRRKEFARRIGVVFgQRSQLWWDLPAID------SFRL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 171 N------EKQEVKKEL--VTEILTALGLLScSHTRTalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASL 242
Cdd:COG4586 120 LkaiyriPDAEYKKRLdeLVELLDLGELLD-TPVRQ--LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREF 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 157427812 243 MKSL-AQGGRTIICTIHqpsaklfEMFD------KLYILSQGQCIFKGMVTNLI 289
Cdd:COG4586 197 LKEYnRERGTTILLTSH-------DMDDiealcdRVIVIDHGRIIYDGSLEELK 243
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
61-283 |
2.46e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.63 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 61 IEFVELSYSVREGPCWRKRG-YKTLLKCLSGKFccremIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNG-------K 132
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRAlFDVNLTIEDGSY-----TAFIGHTGSGKSTIMQLLNGLHVP-TQGSVRVDDtlitstsK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 133 PRELRTFRKMSCYIMQ--EDILLPHlTVLEAMMISA-NLKLNEKQEVKkeLVTEILTALGLLSCSHTRTAL-LSGGQRKR 208
Cdd:PRK13649 77 NKDIKQIRKKVGLVFQfpESQLFEE-TVLKDVAFGPqNFGVSQEEAEA--LAREKLALVGISESLFEKNPFeLSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157427812 209 LAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 283
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD-DVANYADFVYVLEKGKLVLSG 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
61-258 |
3.01e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.71 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 61 IEFVELSYSVREGPCWRKRGYKTL-LKCLSGKFccremIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP------ 133
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNIsFELEEGSF-----VALVGHTGSGKSTLMQHFNALLKPS-SGTITIAGYHitpetg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 134 -RELRTFRKMSCYIMQ--EDILLPHlTVLEAMMISA-NLKLNEKQevKKELVTEILTALGLLSCSHTRTAL-LSGGQRKR 208
Cdd:PRK13641 77 nKNLKKLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPkNFGFSEDE--AKEKALKWLKKVGLSEDLISKSPFeLSGGQMRR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 157427812 209 LAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIH 258
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
66-248 |
4.13e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.80 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 66 LSYSVREGPCWRKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP------RELRTF 139
Cdd:PRK10419 9 LSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPS-QGNVSWRGEPlaklnrAQRKAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 140 RKMSCYIMQEDI--LLPHLTVLEamMISANLK--LNEKQEVKKELVTEILTALGL-LSCSHTRTALLSGGQRKRLAIALE 214
Cdd:PRK10419 88 RRDIQMVFQDSIsaVNPRKTVRE--IIREPLRhlLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190
....*....|....*....|....*....|....
gi 157427812 215 LVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ 248
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQ 199
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
88-284 |
6.01e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 88 LSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgmKGQILVNGKPRE---LRTFRKMSCYIMQEDILLPHLTVLEAMMI 164
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG--SGSIQFAGQPLEawsAAELARHRAYLSQQQTPPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 165 SANLKLNEKQEVKkeLVTEILTALGLLSCSHTRTALLSGG--QRKRLAIALELV---NNP--PVMFFDEPTSGLDSASsf 237
Cdd:PRK03695 93 HQPDKTRTEAVAS--ALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQVwpdINPagQLLLLDEPMNSLDVAQ-- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157427812 238 QVA--SLMKSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKGM 284
Cdd:PRK03695 169 QAAldRLLSELCQQGIAVVMSSHDLNHTL-RHADRVWLLKQGKLLASGR 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
96-278 |
1.19e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 70.87 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG---YRKSGmkGQILVNGkprelrtfrkmscyimqEDIL-------------------- 152
Cdd:COG0396 27 EVHAIMGPNGSGKSTLAKVLMGhpkYEVTS--GSILLDG-----------------EDILelspderaragiflafqypv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 153 -LPHLTVLEAMMISANLKLNEKQEVKK--ELVTEILTALGlLSCSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFDE 226
Cdd:COG0396 88 eIPGVSVSNFLRTALNARRGEELSAREflKLLKEKMKELG-LDEDFLDRYVnegFSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 157427812 227 PTSGLDSASSFQVASLMKSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQ 278
Cdd:COG0396 167 TDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDGR 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
100-261 |
1.54e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.03 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMN----LLAGYRKSGMKGQILVNGK--------PRELRTFRKMscyIMQEDILLPHLTVLEAMMISan 167
Cdd:PRK14267 35 LMGPSGCGKSTLLRtfnrLLELNEEARVEGEVRLFGRniyspdvdPIEVRREVGM---VFQYPNPFPHLTIYDNVAIG-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 LKLNEKQEVKKELVTEILTAL---GLLSCSHTR----TALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVA 240
Cdd:PRK14267 110 VKLNGLVKSKKELDERVEWALkkaALWDEVKDRlndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIE 189
|
170 180
....*....|....*....|.
gi 157427812 241 SLMKSLAQgGRTIICTIHQPS 261
Cdd:PRK14267 190 ELLFELKK-EYTIVLVTHSPA 209
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
96-288 |
1.62e-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: 70.25 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKsGMKGQILVNGKPRE-LRTFRKMS---CYIMQEDILLPHLTVLEAMMISANLKLN 171
Cdd:TIGR03410 27 EVTCVLGRNGVGKTTLLKTLMGLLP-VKSGSIRLDGEDITkLPPHERARagiAYVPQGREIFPRLTVEENLLTGLAALPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 172 EKQEVKKELVT--EILTALgllscSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLA-Q 248
Cdd:TIGR03410 106 RSRKIPDEIYElfPVLKEM-----LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRaE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 157427812 249 GGRTIIcTIHQPSAKLFEMFDKLYILSQGQCIFKGMVTNL 288
Cdd:TIGR03410 181 GGMAIL-LVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
55-283 |
1.62e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 71.18 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 55 KRSAVDIEFVELSYSVREGPcwrkrgyktLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGK-- 132
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENN---------ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKP-QSGEIKIDGIti 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 133 PRE-LRTFRKMSCYIMQ------------EDILLPhltvLEAMMISanlklnekQEVKKELVTEILTALGLLSCSHTRTA 199
Cdd:PRK13632 74 SKEnLKEIRKKIGIIFQnpdnqfigatveDDIAFG----LENKKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 200 LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLA-QGGRTIICTIHQPSAKLfeMFDKLYILSQGQ 278
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRkTRKKTLISITHDMDEAI--LADKVIVFSEGK 219
|
....*
gi 157427812 279 CIFKG 283
Cdd:PRK13632 220 LIAQG 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
99-254 |
1.73e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.14 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 99 GIMGPSGSGKSTLMNLLAG-YRKSgmKGQILVNGKPRELRTFRK-MSCYI-M--QEDILLPHLTVLE----AMMISANLK 169
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGlYQPD--SGEILIDGKPVRIRSPRDaIALGIgMvhQHFMLVPNLTVAEnivlGLEPTKGGR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 LNEKQEVKKelVTEILTALGL---LscsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSASSFQVaslM 243
Cdd:COG3845 113 LDRKAARAR--IRELSERYGLdvdP---DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpqEADELFEI---L 184
|
170
....*....|.
gi 157427812 244 KSLAQGGRTII 254
Cdd:COG3845 185 RRLAAEGKSII 195
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
96-254 |
3.74e-13 |
|
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: 69.39 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGK----------PRE---LRtfRKMSCYIMQedIL--LPHLTVL 159
Cdd:COG4778 38 ECVALTGPSGAGKSTLLKCIYGnYLPDS--GSILVRHDggwvdlaqasPREilaLR--RRTIGYVSQ--FLrvIPRVSAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 160 EAMMISAnLKLNEKQEVKKELVTEILTALGL------LScshtrTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:COG4778 112 DVVAEPL-LERGVDREEARARARELLARLNLperlwdLP-----PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDA 185
|
170 180
....*....|....*....|.
gi 157427812 234 ASSFQVASLMKSLAQGGRTII 254
Cdd:COG4778 186 ANRAVVVELIEEAKARGTAII 206
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
45-289 |
5.18e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.97 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 45 TEAQRFSHLPKRSAVDIEF--VELSYSVREGPCWRKRGyktlLKCLSGKfccreMIGIMGPSGSGKSTLMNLLAGYRKSg 122
Cdd:PRK11176 326 QEKDEGKRVIERAKGDIEFrnVTFTYPGKEVPALRNIN----FKIPAGK-----TVALVGRSGSGKSTIANLLTRFYDI- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 123 MKGQILVNG---KPRELRTFRKmSCYIMQEDILLPHLTVLEAMMISANLKLNEKQ---EVKKELVTEILTAL--GLLSCS 194
Cdd:PRK11176 396 DEGEILLDGhdlRDYTLASLRN-QVALVSQNVHLFNDTIANNIAYARTEQYSREQieeAARMAYAMDFINKMdnGLDTVI 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 195 HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLaQGGRTIICTIHQPSAklFEMFDKLYIL 274
Cdd:PRK11176 475 GENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEKADEILVV 551
|
250
....*....|....*
gi 157427812 275 SQGQCIFKGMVTNLI 289
Cdd:PRK11176 552 EDGEIVERGTHAELL 566
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
61-283 |
5.60e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 69.76 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 61 IEFVELSYSVREGpcwrkrgyKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRkSGMKGQILVNGK---PRELR 137
Cdd:PRK13647 5 IEVEDLHFRYKDG--------TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-LPQRGRVKVMGRevnAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 138 TFRKMSCYIMQE-DILLPHLTVLEAMMISA-NLKLNeKQEVKkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALEL 215
Cdd:PRK13647 76 WVRSKVGLVFQDpDDQVFSSTVWDDVAFGPvNMGLD-KDEVE-RRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157427812 216 VNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 283
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEG 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
96-232 |
8.19e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 70.26 E-value: 8.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGY-RKSGmkGQILVNGK------PRElrtfrkmscyimqEDI--------LLPHLTVLE 160
Cdd:PRK11650 31 EFIVLVGPSGCGKSTLLRMVAGLeRITS--GEIWIGGRvvnelePAD-------------RDIamvfqnyaLYPHMSVRE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157427812 161 AMmiSANLKL--NEKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK11650 96 NM--AYGLKIrgMPKAEIEER-VAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
96-254 |
9.44e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.82 E-value: 9.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGKPRELRTFRKMscyiMQEDI-----------LLPHLTVLEAMM 163
Cdd:COG1129 279 EILGIAGLVGAGRTELARALFGaDPADS--GEIRLDGKPVRIRSPRDA----IRAGIayvpedrkgegLVLDLSIRENIT 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 164 IsANLK-------LNEKQEvkKELVTEILTALGL-LSCSHTRTALLSGG-QRKrLAIALELVNNPPVMFFDEPTSGLDSA 234
Cdd:COG1129 353 L-ASLDrlsrgglLDRRRE--RALAEEYIKRLRIkTPSPEQPVGNLSGGnQQK-VVLAKWLATDPKVLILDEPTRGIDVG 428
|
170 180
....*....|....*....|
gi 157427812 235 SSFQVASLMKSLAQGGRTII 254
Cdd:COG1129 429 AKAEIYRLIRELAAEGKAVI 448
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
100-258 |
9.53e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.76 E-value: 9.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPRELRTFRKMSCYIMQE---DILLPHLTVLEAMMISANLK--LNEKQ 174
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGFVRLA-SGKISILGQPTRQALQKNLVAYVPQSeevDWSFPVLVEDVVMMGRYGHMgwLRRAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 175 EVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTII 254
Cdd:PRK15056 117 KRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTML 196
|
....
gi 157427812 255 CTIH 258
Cdd:PRK15056 197 VSTH 200
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
96-309 |
2.95e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.57 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYrKSGMKGQILVNGK------PRElrtfRKMScYIMQEDILLPHLTVLEAmmISANLK 169
Cdd:PRK10851 29 QMVALLGPSGSGKTTLLRIIAGL-EHQTSGHIRFHGTdvsrlhARD----RKVG-FVFQHYALFRHMTVFDN--IAFGLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 LNEKQE-----VKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMK 244
Cdd:PRK10851 101 VLPRRErpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 245 SLAQGGR--TIICTIHQPSAklFEMFDKLYILSQGqCI--------------------FKGMVTNLIPYLKGLGLHCPTY 302
Cdd:PRK10851 181 QLHEELKftSVFVTHDQEEA--MEVADRVVVMSQG-NIeqagtpdqvwrepatrfvleFMGEVNRLQGTIRGGQFHVGAH 257
|
....*..
gi 157427812 303 HNPADFI 309
Cdd:PRK10851 258 RWPLGYT 264
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
96-283 |
3.16e-12 |
|
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: 66.90 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG---YRKSG----MKGQILVNGKPRElRTfRKMSCYIMQEDILLPHLTVLEAMMISANL 168
Cdd:TIGR01978 27 EIHAIMGPNGSGKSTLSKTIAGhpsYEVTSgtilFKGQDLLELEPDE-RA-RAGLFLAFQYPEEIPGVSNLEFLRSALNA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 169 KLNEKQEVK------KELVTEILTALGLLSCSHTRTAL--LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVA 240
Cdd:TIGR01978 105 RRSARGEEPldlldfEKLLKEKLALLDMDEEFLNRSVNegFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVA 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 157427812 241 SLMKSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQCIFKG 283
Cdd:TIGR01978 185 EGINRLREPDRSFLIITHYQ--RLLNYIkpDYVHVLLDGRIVKSG 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
82-242 |
3.25e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.03 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 82 KTLLKCLS-----GKFCCremigIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGK-----PRELRtfrkmSCYI---M 147
Cdd:COG1101 19 KRALDGLNltieeGDFVT-----VIGSNGAGKSTLLNAIAGsLPPDS--GSILIDGKdvtklPEYKR-----AKYIgrvF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 148 QeDILL---PHLTVLEAMMISAN------LKLNEKQEvKKELVTEILTALGL-----LscsHTRTALLSGGQRKRLAIAL 213
Cdd:COG1101 87 Q-DPMMgtaPSMTIEENLALAYRrgkrrgLRRGLTKK-RRELFRELLATLGLglenrL---DTKVGLLSGGQRQALSLLM 161
|
170 180
....*....|....*....|....*....
gi 157427812 214 ELVNNPPVMFFDEPTSGLDSASSFQVASL 242
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVLEL 190
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
96-278 |
3.60e-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: 69.39 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGkpRELRTFRKmscyimqeDILLPHL------------TVLE--A 161
Cdd:COG4618 359 EVLGVIGPSGSGKSTLARLLVGVWPP-TAGSVRLDG--ADLSQWDR--------EELGRHIgylpqdvelfdgTIAEniA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 162 MMisanlklnekQEVKKELVTE----------IL-------TALGllscshTRTALLSGGQRKRLAIALELVNNPPVMFF 224
Cdd:COG4618 428 RF----------GDADPEKVVAaaklagvhemILrlpdgydTRIG------EGGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 157427812 225 DEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQPSAkLFEMfDKLYILSQGQ 278
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSL-LAAV-DKLLVLRDGR 543
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
96-258 |
4.25e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.42 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTL---MNLL-------------------AGYRKSGMKGQILVnGKPR-----ELRTFRKMSCYIMQ 148
Cdd:PRK13651 34 EFIAIIGQTGSGKTTFiehLNALllpdtgtiewifkdeknkkKTKEKEKVLEKLVI-QKTRfkkikKIKEIRRRVGVVFQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 149 -EDILLPHLTVLEAMMISANLKLNEKQEVKKeLVTEILTALGLLSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDE 226
Cdd:PRK13651 113 fAEYQLFEQTIEKDIIFGPVSMGVSKEEAKK-RAAKYIELVGLDESYLQRSPFeLSGGQKRRVALAGILAMEPDFLVFDE 191
|
170 180 190
....*....|....*....|....*....|..
gi 157427812 227 PTSGLDSASSFQVASLMKSLAQGGRTIICTIH 258
Cdd:PRK13651 192 PTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
96-246 |
4.72e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.81 E-value: 4.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGK------PRELRTFRKMSCYIMQEDI--LLPHLTVLEamMISAN 167
Cdd:PRK15079 48 ETLGVVGESGCGKSTFARAIIGLVKA-TDGEVAWLGKdllgmkDDEWRAVRSDIQMIFQDPLasLNPRMTIGE--IIAEP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 LKLNE----KQEVKKElVTEILTALGLLSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASL 242
Cdd:PRK15079 125 LRTYHpklsRQEVKDR-VKAMMLKVGLLPNLINRYPHeFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNL 203
|
....
gi 157427812 243 MKSL 246
Cdd:PRK15079 204 LQQL 207
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
95-283 |
4.78e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.55 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 95 REMIGIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGKPRE------------LRTFrkmscyimQEDILLPHLTVLEA 161
Cdd:PRK11300 31 QEIVSLIGPNGAGKTTVFNCLTGfYKPTG--GTILLRGQHIEglpghqiarmgvVRTF--------QHVRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 162 MMISANLKLN--------------EKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEP 227
Cdd:PRK11300 101 LLVAQHQQLKtglfsgllktpafrRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157427812 228 TSGLDSASSFQVASLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 283
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
60-278 |
8.13e-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: 65.21 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 60 DIEFVELSYSVREGPcwrkrgyKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLagYR-KSGMKGQILVNGKP----- 133
Cdd:cd03244 2 DIEFKNVSLRYRPNL-------PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLAL--FRlVELSSGSILIDGVDiskig 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 134 -RELRtfRKMSCyIMQEDILL---------PHLTVLEAMMISAnLKlnekqEVK-KELVTEILTALGLLSCShtRTALLS 202
Cdd:cd03244 73 lHDLR--SRISI-IPQDPVLFsgtirsnldPFGEYSDEELWQA-LE-----RVGlKEFVESLPGGLDTVVEE--GGENLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 203 GGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSlAQGGRTIIC------TIHQpsaklfemFDKLYILSQ 276
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTiahrldTIID--------SDRILVLDK 212
|
..
gi 157427812 277 GQ 278
Cdd:cd03244 213 GR 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
54-278 |
1.03e-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: 67.54 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 54 PKRSAVDiefvELSYSVREGpcwrkrgyktllkclsgkfccrEMIGIMGPSGSGKSTLMNLLAGYRKSGMKGQILVNGKP 133
Cdd:TIGR02633 271 PHRKRVD----DVSFSLRRG----------------------EILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKP 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 134 RELRTFRKMscyIMQEDILLPH----LTVLEAMMISANLKLNEKQEVKKELVTEILTALGLLSCS----HTRTAL----- 200
Cdd:TIGR02633 325 VDIRNPAQA---IRAGIAMVPEdrkrHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAiqrlKVKTASpflpi 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 201 --LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIIcTIHQPSAKLFEMFDKLYILSQGQ 278
Cdd:TIGR02633 402 grLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAII-VVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
96-277 |
1.04e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.68 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLA-GYRKSGmkGQILVNG---KPRELRTFRKMSCYIMQEDILL------------PHLT-- 157
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLINLLQrVFDPQS--GRILIDGtdiRTVTRASLRRNIAVVFQDAGLFnrsiednirvgrPDATde 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 158 -VLEAMMISANLKLNEKQEVKKElvteilTALGllscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASS 236
Cdd:PRK13657 440 eMRAAAERAQAHDFIERKPDGYD------TVVG------ERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 157427812 237 FQVASLMKSLAQgGRTIICTIHQPS----AKLFEMFDKLYILSQG 277
Cdd:PRK13657 508 AKVKAALDELMK-GRTTFIIAHRLStvrnADRILVFDNGRVVESG 551
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
96-282 |
1.34e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKP-RELRTFRkmscyIMQEDI-LLPH-LTVLEAMMISANLKLN- 171
Cdd:PRK11614 32 EIVTLIGANGAGKTTLLGTLCGDPRA-TSGRIVFDGKDiTDWQTAK-----IMREAVaIVPEgRRVFSRMTVEENLAMGg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 172 ---EKQEVKK--ELVTEILTALglLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL 246
Cdd:PRK11614 106 ffaERDQFQEriKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 157427812 247 AQGGRTIIcTIHQPSAKLFEMFDKLYILSQGQCIFK 282
Cdd:PRK11614 184 REQGMTIF-LVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
96-283 |
2.47e-11 |
|
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: 63.31 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG---YRKSgmKGQILVNGK-----PRELRTfrKMSCYIM-QEDILLPHLTVLEAMMisa 166
Cdd:cd03217 27 EVHALMGPNGSGKSTLAKTIMGhpkYEVT--EGEILFKGEditdlPPEERA--RLGIFLAfQYPPEIPGVKNADFLR--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 167 nlKLNEKqevkkelvteiltalgllscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL 246
Cdd:cd03217 100 --YVNEG---------------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 157427812 247 AQGGRTIICTIHQpsAKLFEMF--DKLYILSQGQCIFKG 283
Cdd:cd03217 151 REEGKSVLIITHY--QRLLDYIkpDRVHVLYDGRIVKSG 187
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
81-278 |
2.68e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 66.37 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 81 YKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVngkPRELRTFrkmscyimqediLLPHltvlE 160
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG-SGRIAR---PAGARVL------------FLPQ----R 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 161 AMMISANLKL-----NEKQEVKKELVTEILTALGL------LSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 229
Cdd:COG4178 435 PYLPLGTLREallypATAEAFSDAELREALEAVGLghlaerLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157427812 230 GLDSASSFQVASLMKSLAQGGrTIICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:COG4178 515 ALDEENEAALYQLLREELPGT-TVISVGHRST--LAAFHDRVLELTGDG 560
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
95-258 |
2.73e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.36 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 95 REMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVN--------GKPREL---RTFRKMScYIMQEDILLPHLTVLEAMM 163
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGVLEP-TSGEVNVRvgdewvdmTKPGPDgrgRAKRYIG-ILHQEYDLYPHRTVLDNLT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 164 ISANLKLNEKQEVKKELVTeiLTALGLlSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSF 237
Cdd:TIGR03269 388 EAIGLELPDELARMKAVIT--LKMVGF-DEEKAEEILdkypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKV 464
|
170 180
....*....|....*....|..
gi 157427812 238 QVA-SLMKSLAQGGRTIICTIH 258
Cdd:TIGR03269 465 DVThSILKAREEMEQTFIIVSH 486
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
96-307 |
3.40e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.29 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAgyRKSGMKGQILVNGKPR-----------ELRTFRKMSCYIMQEDILLPhLTVLEAMMI 164
Cdd:PRK14258 34 KVTAIIGPSGCGKSTFLKCLN--RMNELESEVRVEGRVEffnqniyerrvNLNRLRRQVSMVHPKPNLFP-MSVYDNVAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 165 SANL-----KLN-----EKQEVKKELVTEILTALgllscsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 234
Cdd:PRK14258 111 GVKIvgwrpKLEiddivESALKDADLWDEIKHKI------HKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPI 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157427812 235 SSFQVASLMKSLA-QGGRTIICTIHQpsaklfemFDKLYILSQGQCIFKGMvTNLIPYLKGLGLHCPTYHNPAD 307
Cdd:PRK14258 185 ASMKVESLIQSLRlRSELTMVIVSHN--------LHQVSRLSDFTAFFKGN-ENRIGQLVEFGLTKKIFNSPHD 249
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
96-258 |
3.50e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 65.63 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPRELRTFRKMSCYIM---QEDIL--------------LPHLTV 158
Cdd:PRK09536 30 SLVGLVGPNGAGKTTLLRAINGTLTPT-AGTVLVAGDDVEALSARAASRRVAsvpQDTSLsfefdvrqvvemgrTPHRSR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 159 LEAMmisanlklnekQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQ 238
Cdd:PRK09536 109 FDTW-----------TETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVR 177
|
170 180
....*....|....*....|
gi 157427812 239 VASLMKSLAQGGRTIICTIH 258
Cdd:PRK09536 178 TLELVRRLVDDGKTAVAAIH 197
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
431-584 |
5.10e-11 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 62.52 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 431 ILFLMFAAMMPTVLTFplemaVFLREH--LNYWYSLKI----YFLAKTMADVPFQVICPAVYCSIMYWMTSQPAETSRFL 504
Cdd:COG0842 11 AMSLLFTALMLTALSI-----AREREQgtLERLLVTPVsrleILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 505 LFLALGASTALAAQSLGMLIGAASSSLQVATFLGPVTAIPVLLFSGFFVSFKAIPSYLQWSSYLSYVRYGFEGVILTIYG 584
Cdd:COG0842 86 LLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRALFLG 165
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
96-312 |
5.55e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSG-MKGQILVNGKPRELRTFR----KMSCYIMQEDILLPHLTVLEAMM----ISA 166
Cdd:PRK13549 32 EIVSLCGENGAGKSTLMKVLSGVYPHGtYEGEIIFEGEELQASNIRdterAGIAIIHQELALVKELSVLENIFlgneITP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 167 NLKLNEKQEVKKelVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL 246
Cdd:PRK13549 112 GGIMDYDAMYLR--AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 247 AQGGRTIICTIHqpsaKLFEMF---DKLYILSQGQC-------------IFKGMV----TNLIPYLKglglhcptyHNPA 306
Cdd:PRK13549 190 KAHGIACIYISH----KLNEVKaisDTICVIRDGRHigtrpaagmteddIITMMVgrelTALYPREP---------HTIG 256
|
....*.
gi 157427812 307 DFIIEV 312
Cdd:PRK13549 257 EVILEV 262
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
95-264 |
5.97e-11 |
|
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: 60.85 E-value: 5.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 95 REMIGIMGPSGSGKSTLMNLLAGYRKSGMKGQILVNGkprelrtfrkmscyimqedillphltvleammisanlklnekq 174
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 175 evkkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQV------ASLMKSLAQ 248
Cdd:smart00382 39 ----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleelRLLLLLKSE 114
|
170
....*....|....*.
gi 157427812 249 GGRTIICTIHQPSAKL 264
Cdd:smart00382 115 KNLTVILTTNDEKDLG 130
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
96-288 |
6.54e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 6.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSgmKGQILVNGKPRElRTFRKMSC-----YIMQEDILLPHLTVLEAMMISanlK 169
Cdd:PRK09700 32 EIHALLGENGAGKSTLMKVLSGiHEPT--KGTITINNINYN-KLDHKLAAqlgigIIYQELSVIDELTVLENLYIG---R 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 LNEKQ---------EVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVA 240
Cdd:PRK09700 106 HLTKKvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLF 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 157427812 241 SLMKSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKGMVTNL 288
Cdd:PRK09700 186 LIMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
100-258 |
6.63e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.18 E-value: 6.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAgyRKSGM-KGQILVNG------KPRELRtfRKMScyIM-QEDILLPHLTVLEammisanL--- 168
Cdd:COG4604 32 LIGPNGAGKSTLLSMIS--RLLPPdSGEVLVDGldvattPSRELA--KRLA--ILrQENHINSRLTVRE-------Lvaf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 169 --------KLNEKQEvkkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVA 240
Cdd:COG4604 99 grfpyskgRLTAEDR---EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMM 175
|
170
....*....|....*....
gi 157427812 241 SLMKSLAQG-GRTIICTIH 258
Cdd:COG4604 176 KLLRRLADElGKTVVIVLH 194
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
98-258 |
6.74e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 6.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 98 IGIMGPSGSGKSTLMNLLAGYRKSgmkgqilVNGKPRELRTFRkmSCYIMQEDILLPHLTVLEAMM-------------- 163
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDKD-------FNGEARPQPGIK--VGYLPQEPQLDPTKTVRENVEegvaeikdaldrfn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 164 -ISANL--------KLNEKQEvkkELvTEILTALGL-------------LSCS--HTRTALLSGGQRKRLAIALELVNNP 219
Cdd:TIGR03719 105 eISAKYaepdadfdKLAAEQA---EL-QEIIDAADAwdldsqleiamdaLRCPpwDADVTKLSGGERRRVALCRLLLSKP 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 157427812 220 PVMFFDEPTSGLDSASsfqVASLMKSLAQGGRTIICTIH 258
Cdd:TIGR03719 181 DMLLLDEPTNHLDAES---VAWLERHLQEYPGTVVAVTH 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
96-258 |
8.76e-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: 65.42 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGyRKSGMKGQILVNGKP--RELRTFRKMSCYIMQEDILLPHLTVLEAMMISANLKLNEK 173
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTG-DTTVTSGDATVAGKSilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 174 QEVKKeLVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTI 253
Cdd:TIGR01257 2045 EEIEK-VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAV 2123
|
....*
gi 157427812 254 ICTIH 258
Cdd:TIGR01257 2124 VLTSH 2128
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
100-300 |
9.65e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.85 E-value: 9.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP---RELRTFRKMSCYIMQEDillphltvlEAMMISANLKLN----- 171
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIEKVK-SGEIFYNNQAitdDNFEKLRKHIGIVFQNP---------DNQFVGSIVKYDvafgl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 172 EKQEVK----KELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLA 247
Cdd:PRK13648 110 ENHAVPydemHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVK 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157427812 248 QGGR-TIICTIHQPSAKLFEmfDKLYILSQGQCIFKGMVTNLIPYLKGL---GLHCP 300
Cdd:PRK13648 190 SEHNiTIISITHDLSEAMEA--DHVIVMNKGTVYKEGTPTEIFDHAEELtriGLDLP 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
96-295 |
1.64e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.11 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKS----TLMNLLAGYRKSGMKGQILVNGKPRELRTFRKMS------------CYIMQEDI--LLPHLT 157
Cdd:PRK10261 43 ETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSaaqmrhvrgadmAMIFQEPMtsLNPVFT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 158 VLEAMMISANLKLNEKQEvkkELVTEILTALGLLSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGL 231
Cdd:PRK10261 123 VGEQIAESIRLHQGASRE---EAMVEAKRMLDQVRIPEAQTILsryphqLSGGMRQRVMIAMALSCRPAVLIADEPTTAL 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157427812 232 DSASSFQVASLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGMVTNLI-----PYLKGL 295
Cdd:PRK10261 200 DVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFhapqhPYTRAL 268
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
100-288 |
1.65e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.09 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGK--P----RELRTFRKMSCYIMQEDILLPHLTVLEAMMISANLKLNEK 173
Cdd:PRK11831 38 IMGPSGIGKTTLLRLIGGQIAPD-HGEILFDGEniPamsrSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 174 QEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQG-GRT 252
Cdd:PRK11831 117 APLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVT 196
|
170 180 190
....*....|....*....|....*....|....*.
gi 157427812 253 IICTIHQpSAKLFEMFDKLYILSQGQCIFKGMVTNL 288
Cdd:PRK11831 197 CVVVSHD-VPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
54-278 |
2.02e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.41 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 54 PKRSAVDiefvELSYSVREGpcwrkrgyktllkclsgkfccrEMIGIMGPSGSGKSTLMNLLAGYRKSGMKGQILVNGKP 133
Cdd:PRK13549 273 PHIKRVD----DVSFSLRRG----------------------EILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKP 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 134 RELRTFRKMS----CY------------IM--QEDILLPHL-TVLEAMMISANLKLNEKQEVKKELvtEILTALGLLSCS 194
Cdd:PRK13549 327 VKIRNPQQAIaqgiAMvpedrkrdgivpVMgvGKNITLAALdRFTGGSRIDDAAELKTILESIQRL--KVKTASPELAIA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 195 HtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTihqpSAKLFE---MFDKL 271
Cdd:PRK13549 405 R-----LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI----SSELPEvlgLSDRV 475
|
....*..
gi 157427812 272 YILSQGQ 278
Cdd:PRK13549 476 LVMHEGK 482
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
85-247 |
2.15e-10 |
|
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: 61.27 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 85 LKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNG-----KPRELRTFRKMSCYIMQEDILLPHLTvl 159
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPD-EGDIEIELdtvsyKPQYIKADYEGTVRDLLSSITKDFYT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 160 eammisanlklnekqevKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQV 239
Cdd:cd03237 92 -----------------HPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
....*...
gi 157427812 240 ASLMKSLA 247
Cdd:cd03237 155 SKVIRRFA 162
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
96-280 |
2.21e-10 |
|
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: 63.31 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSGMKGQILVNGKPRELR----TFRKMSCYIMQEDILLPHLTVLEAMMISANLKL 170
Cdd:TIGR02633 28 ECVGLCGENGAGKSTLMKILSGvYPHGTWDGEIYWSGSPLKASnirdTERAGIVIIHQELTLVPELSVAENIFLGNEITL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 171 NEKQEVKKELV---TEILTALGLLSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL 246
Cdd:TIGR02633 108 PGGRMAYNAMYlraKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 157427812 247 AQGGRTIICTIHqpsaKLFE---MFDKLYILSQGQCI 280
Cdd:TIGR02633 188 KAHGVACVYISH----KLNEvkaVCDTICVIRDGQHV 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
80-256 |
2.27e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.33 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 80 GYKTLLKCLSGKFCCREMIGIMGPSGSGKSTL------MNLLAgyRKSGMKGQILVNGK----PR----ELRTFRKMscy 145
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsinrMNDLN--PEVTITGSIVYNGHniysPRtdtvDLRKEIGM--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 146 IMQEDILLPhLTVLEAMMISANLKLNEKQEVKKELVTEILTALGLLSCSHTR---TAL-LSGGQRKRLAIALELVNNPPV 221
Cdd:PRK14239 91 VFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRlhdSALgLSGGQQQRVCIARVLATSPKI 169
|
170 180 190
....*....|....*....|....*....|....*
gi 157427812 222 MFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICT 256
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT 204
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
96-232 |
2.30e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.48 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGyRKSGMKGQILVNGKPRELRTFRKMSC----YIMQEDILLPHLTVLEA--MMISA--N 167
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSA-RLAPDAGEVHYRMRDGQLRDLYALSEaerrRLLRTEWGFVHQHPRDGlrMQVSAggN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 lklnekqevkkelVTEILTALGLLSCSHTR-TAL-------------------LSGGQRKRLAIALELVNNPPVMFFDEP 227
Cdd:PRK11701 112 -------------IGERLMAVGARHYGDIRaTAGdwlerveidaariddlpttFSGGMQQRLQIARNLVTHPRLVFMDEP 178
|
....*
gi 157427812 228 TSGLD 232
Cdd:PRK11701 179 TGGLD 183
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
98-232 |
2.68e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.16 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 98 IGIMGPSGSGKSTLMNLLAGYRK--SGmkgqilvngkprelrTFR-----KMScYIMQE-DILLPHLTVLEAMmisanlk 169
Cdd:COG0488 344 IGLIGPNGAGKSTLLKLLAGELEpdSG---------------TVKlgetvKIG-YFDQHqEELDPDKTVLDEL------- 400
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 lnekQEVKKELvTEIlTALGLLSC-------SHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:COG0488 401 ----RDGAPGG-TEQ-EVRGYLGRflfsgddAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
96-232 |
3.09e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPRELRTFRKMSCYIMQEDILLPHLTVLEAMMISANLKLNEKQE 175
Cdd:PRK13543 38 EALLVQGDNGAGKTTLLRVLAGLLHVE-SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQ 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 157427812 176 VKkelvTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK13543 117 MP----GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
82-286 |
3.64e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.81 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 82 KTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRK-SGMKGQILVNGK-----PRELRTfrKMSCYI-MQEDILLP 154
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAyKILEGDILFKGEsildlEPEERA--HLGIFLaFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 155 HLTVLEAMMISAN--LKLNEKQEVKK----ELVTEILTALGLLSCSHTRTAL--LSGGQRKRLAIALELVNNPPVMFFDE 226
Cdd:CHL00131 98 GVSNADFLRLAYNskRKFQGLPELDPleflEIINEKLKLVGMDPSFLSRNVNegFSGGEKKRNEILQMALLDSELAILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157427812 227 PTSGLDSASSFQVASLMKSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQCIFKGMVT 286
Cdd:CHL00131 178 TDSGLDIDALKIIAEGINKLMTSENSIILITHYQ--RLLDYIkpDYVHVMQNGKIIKTGDAE 237
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
96-260 |
3.74e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.36 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKsgmkgqilvnGKPRElrtfrkmSCYIMQEDILLPHLTVLEAMMISANLKLnekqe 175
Cdd:COG2401 57 EIVLIVGASGSGKSTLLRLLAGALK----------GTPVA-------GCVDVPDNQFGREASLIDAIGRKGDFKD----- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 176 vkkelVTEILTALGLLSCS--HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ-GGRT 252
Cdd:COG2401 115 -----AVELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARrAGIT 189
|
....*...
gi 157427812 253 IICTIHQP 260
Cdd:COG2401 190 LVVATHHY 197
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
100-259 |
5.13e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.80 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYRKSgMKGQI------LVNGK-PRELRTFRKMSCYIMQ--EDILLPHlTVLEAMMISAnLKL 170
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQP-TSGTVtigervITAGKkNKKLKPLRKKVGIVFQfpEHQLFEE-TVEKDICFGP-MNF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 171 NEKQEVKKELVTEILTALGLLSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ- 248
Cdd:PRK13634 115 GVSEEDAKQKAREMIELVGLPEELLARSPFeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKe 194
|
170
....*....|.
gi 157427812 249 GGRTIICTIHQ 259
Cdd:PRK13634 195 KGLTTVLVTHS 205
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
96-226 |
5.37e-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: 62.12 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGKP---RELRTFRKMSCYIMQEDILLPHLtvleammisanlkLN 171
Cdd:COG4615 359 ELVFIVGGNGSGKSTLAKLLTGlYRPES--GEILLDGQPvtaDNREAYRQLFSAVFSDFHLFDRL-------------LG 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157427812 172 EKQEVKKELVTEILTALGLlscSH---------TRTAlLSGGQRKRLAIALELVNNPPVMFFDE 226
Cdd:COG4615 424 LDGEADPARARELLERLEL---DHkvsvedgrfSTTD-LSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
96-257 |
5.46e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 61.28 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKS----TLMNLLAGYRKSG----MKGQILVNGKPRELRTFR--KMScYIMQEDI--LLPHLTVLEAMM 163
Cdd:PRK09473 43 ETLGIVGESGSGKSqtafALMGLLAANGRIGgsatFNGREILNLPEKELNKLRaeQIS-MIFQDPMtsLNPYMRVGEQLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 164 isANLKLNeKQEVKKELVTEILTALGLLSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSF 237
Cdd:PRK09473 122 --EVLMLH-KGMSKAEAFEESVRMLDAVKMPEARKRMkmypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQA 198
|
170 180
....*....|....*....|
gi 157427812 238 QVASLMKSLAQGGRTIICTI 257
Cdd:PRK09473 199 QIMTLLNELKREFNTAIIMI 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
96-283 |
6.11e-10 |
|
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: 62.13 E-value: 6.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG---YRKSgmKGQILVN----------------GKP--------------------REL 136
Cdd:TIGR03269 27 EVLGILGRSGAGKSVLMHVLRGmdqYEPT--SGRIIYHvalcekcgyverpskvGEPcpvcggtlepeevdfwnlsdKLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 137 RTFRKMSCYIMQEDI-LLPHLTVLEAMMISanlkLNEKQEVKKELVTEILTALGLLSCSHTRTAL---LSGGQRKRLAIA 212
Cdd:TIGR03269 105 RRIRKRIAIMLQRTFaLYGDDTVLDNVLEA----LEEIGYEGKEAVGRAVDLIEMVQLSHRITHIardLSGGEKQRVVLA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157427812 213 LELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:TIGR03269 181 RQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEV-IEDLSDKAIWLENGEIKEEG 251
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
58-233 |
6.87e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.04 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 58 AVDIEFVELSYsvregpcwrkRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRkSGMKGQILVNGKPREL- 136
Cdd:PRK10790 340 RIDIDNVSFAY----------RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYY-PLTEGEIRLDGRPLSSl 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 137 --RTFRKmSCYIMQEDillphlTVLEAMMISANLKLNekQEVKKELVTEILTALGLLSCS-------HTRTA----LLSG 203
Cdd:PRK10790 409 shSVLRQ-GVAMVQQD------PVVLADTFLANVTLG--RDISEEQVWQALETVQLAELArslpdglYTPLGeqgnNLSV 479
|
170 180 190
....*....|....*....|....*....|
gi 157427812 204 GQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDS 509
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
94-258 |
7.19e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.07 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 94 CREMIGIMGPSGSGKSTLMNLLAGyrksGMKGQILVNGKPRE----LRTFR--KMSCYI--MQEDILLPHLTVLEAMMIS 165
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAG----KLKPNLGKFDDPPDwdeiLDEFRgsELQNYFtkLLEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 166 ANLK------LNEKQEV-KKELVTEILTALGLLScshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQ 238
Cdd:cd03236 101 KAVKgkvgelLKKKDERgKLDELVDQLELRHVLD---RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180
....*....|....*....|
gi 157427812 239 VASLMKSLAQGGRTIICTIH 258
Cdd:cd03236 178 AARLIRELAEDDNYVLVVEH 197
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
173-300 |
7.22e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.58 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 173 KQEVKKeLVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLA-QGGR 251
Cdd:PRK13640 117 RPEMIK-IVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNL 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 157427812 252 TIICTIHQPSAKlfEMFDKLYILSQGQCIFKGMVTNLIP---YLKGLGLHCP 300
Cdd:PRK13640 196 TVISITHDIDEA--NMADQVLVLDDGKLLAQGSPVEIFSkveMLKEIGLDIP 245
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
100-248 |
8.18e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.75 E-value: 8.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYRK--SG---MKGQILVNGKPRELRTFRKMSCYIMQEDI--LLPHLTV---LEAMMIsANLK 169
Cdd:PRK11308 46 VVGESGCGKSTLARLLTMIETptGGelyYQGQDLLKADPEAQKLLRQKIQIVFQNPYgsLNPRKKVgqiLEEPLL-INTS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 LNEKQevKKELVTEILTALGLLSCSHTRTA-LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ 248
Cdd:PRK11308 125 LSAAE--RREKALAMMAKVGLRPEHYDRYPhMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
98-254 |
9.35e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 61.72 E-value: 9.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 98 IGIMGPSGSGKSTLMNLLAG---------------------YRKSGMKG--QILVNGkprELRTFRKmscyIMQEDiLLP 154
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGelkpnlgdydeepswdevlkrFRGTELQDyfKKLANG---EIKVAHK----PQYVD-LIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 155 HL---TVLEAMMisanlKLNEKQEVKkelvtEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 231
Cdd:COG1245 174 KVfkgTVRELLE-----KVDERGKLD-----ELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180
....*....|....*....|...
gi 157427812 232 DSASSFQVASLMKSLAQGGRTII 254
Cdd:COG1245 244 DIYQRLNVARLIRELAEEGKYVL 266
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
84-278 |
9.48e-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: 58.63 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 84 LLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAG-YRKsgMKGQILVNGKprelrtfrkMScYIMQEdillphltvleAM 162
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEK--LSGSVSVPGS---------IA-YVSQE-----------PW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 163 MISANLKLN-------EKQEVKK-----ELVT--EILTAlGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPT 228
Cdd:cd03250 77 IQNGTIRENilfgkpfDEERYEKvikacALEPdlEILPD-GDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157427812 229 SGLDSassfQVAS-LMKSLAQG----GRTIICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:cd03250 156 SAVDA----HVGRhIFENCILGlllnNKTRILVTHQLQ--LLPHADQIVVLDNGR 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
96-248 |
9.99e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 61.24 E-value: 9.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKS----TLMNLLAgYRKSGMKGQILVNGK------PRELRTFR--KMSCyIMQEDI--LLPHLTVlea 161
Cdd:COG4172 37 ETLALVGESGSGKSvtalSILRLLP-DPAAHPSGSILFDGQdllglsERELRRIRgnRIAM-IFQEPMtsLNPLHTI--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 162 mmisanlklnEKQevkkelVTEILT-------------ALGLLscshTRTAL-------------LSGGQRKRLAIALEL 215
Cdd:COG4172 112 ----------GKQ------IAEVLRlhrglsgaaararALELL----ERVGIpdperrldayphqLSGGQRQRVMIAMAL 171
|
170 180 190
....*....|....*....|....*....|...
gi 157427812 216 VNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ 248
Cdd:COG4172 172 ANEPDLLIADEPTTALDVTVQAQILDLLKDLQR 204
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
163-303 |
1.03e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.52 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 163 MISANLKLNEKQevKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASL 242
Cdd:NF000106 109 MIGR*LDLSRKD--ARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157427812 243 MKSLAQGGRTIICTIhQPSAKLFEMFDKLYILSQGQCIFKGMVTNLIPYLKGLGLHCPTYH 303
Cdd:NF000106 187 VRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAH 246
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
100-259 |
1.27e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPRELRT---FRKMSCYIM-QEDILLPHLTVLEAMMisanLKLNEKQE 175
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGIVPPD-SGTLEIGGNPCARLTpakAHQLGIYLVpQEPLLFPNLSVKENIL----FGLPKRQA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 176 VKKELvTEILTALGllsCS---HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRT 252
Cdd:PRK15439 117 SMQKM-KQLLAALG---CQldlDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVG 192
|
....*..
gi 157427812 253 IICTIHQ 259
Cdd:PRK15439 193 IVFISHK 199
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
100-279 |
1.37e-09 |
|
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: 57.55 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYRKSGmKGQIlvnGKPRELRTFrkmscYIMQEdillPHLTVleammisANLKlnekqevkke 179
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWG-SGRI---GMPEGEDLL-----FLPQR----PYLPL-------GTLR---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 180 lvtEILtalgllscSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLaqgGRTIICTIHQ 259
Cdd:cd03223 82 ---EQL--------IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHR 147
|
170 180
....*....|....*....|.
gi 157427812 260 PS-AKLFEMfdKLYILSQGQC 279
Cdd:cd03223 148 PSlWKFHDR--VLDLDGEGGW 166
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
96-254 |
1.87e-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: 60.60 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGkpRELRTFRKMScyiMQEDI-LLPHLTVLEAMMISANL---KL 170
Cdd:COG5265 385 KTVAIVGPSGAGKSTLARLLFRfYDVTS--GRILIDG--QDIRDVTQAS---LRAAIgIVPQDTVLFNDTIAYNIaygRP 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 171 NEKQEvkkelvtEILTALGLLSCSHTRTAL--------------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASS 236
Cdd:COG5265 458 DASEE-------EVEAAARAAQIHDFIESLpdgydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTE 530
|
170
....*....|....*...
gi 157427812 237 FQVASLMKSLAQGGRTII 254
Cdd:COG5265 531 RAIQAALREVARGRTTLV 548
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
96-248 |
2.03e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.49 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKS----TLMNLLAGYRKSGMKGQILVNGKP------RELRTFR--KMScYIMQEDillphltvleamM 163
Cdd:PRK15134 36 ETLALVGESGSGKSvtalSILRLLPSPPVVYPSGDIRFHGESllhaseQTLRGVRgnKIA-MIFQEP------------M 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 164 ISAN-LKLNEKQ--EV--------KKELVTEILTALGLLSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDE 226
Cdd:PRK15134 103 VSLNpLHTLEKQlyEVlslhrgmrREAARGEILNCLDRVGIRQAAKRLtdyphqLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180
....*....|....*....|..
gi 157427812 227 PTSGLDSASSFQVASLMKSLAQ 248
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQ 204
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
80-258 |
2.27e-09 |
|
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: 56.30 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 80 GYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPRelrtfrkmSCYIMQedillphltvl 159
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD-EGIVTWGSTVK--------IGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 160 eammisanlklnekqevkkelvteiltalgllscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASsfqV 239
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES---I 106
|
170
....*....|....*....
gi 157427812 240 ASLMKSLAQGGRTIICTIH 258
Cdd:cd03221 107 EALEEALKEYPGTVILVSH 125
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
91-283 |
2.50e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.87 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 91 KFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNG--------KPRELRTFRKMSCYIMQEDILLPHLTVLEAM 162
Cdd:PRK13645 33 TFKKNKVTCVIGTTGSGKSTMIQLTNGLIIS-ETGQTIVGDyaipanlkKIKEVKRLRKEIGLVFQFPEYQLFQETIEKD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 163 MISANLKLNE-KQEVKKElVTEILTALGLLSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVA 240
Cdd:PRK13645 112 IAFGPVNLGEnKQEAYKK-VPELLKLVQLPEDYVKRSPFeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 157427812 241 SLMKSLAQG-GRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 283
Cdd:PRK13645 191 NLFERLNKEyKKRIIMVTHNMD-QVLRIADEVIVMHEGKVISIG 233
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
99-288 |
2.94e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 99 GIMGPSGSGKSTLMNLLAG-YRKSGmkGQILVNGKPRelrTFR--KMS-----CYIMQEDILLPHLTVLEammisaNLKL 170
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGiYTRDA--GSILYLGKEV---TFNgpKSSqeagiGIIHQELNLIPQLTIAE------NIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 171 NekQEVK--------KELVTE---ILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSASS 236
Cdd:PRK10762 103 G--REFVnrfgridwKKMYAEadkLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtdtETESL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 157427812 237 FQVaslMKSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKGMVTNL 288
Cdd:PRK10762 181 FRV---IRELKSQGRGIVYISHR-LKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
96-278 |
4.05e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.60 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSgmKGQILVNGKP---RELRTFRKMSCYIMQEDILLPHLTVleammisanlklN 171
Cdd:PRK10522 350 ELLFLIGGNGSGKSTLAMLLTGlYQPQ--SGEILLDGKPvtaEQPEDYRKLFSAVFTDFHLFDQLLG------------P 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 172 EKQEVKKELVTEILTALGL---LSCSHTRTAL--LSGGQRKRLAIALELVNNPPVMFFDEPTSglDSASSF-----QVas 241
Cdd:PRK10522 416 EGKPANPALVEKWLERLKMahkLELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAA--DQDPHFrrefyQV-- 491
|
170 180 190
....*....|....*....|....*....|....*..
gi 157427812 242 LMKSLAQGGRTIICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:PRK10522 492 LLPLLQEMGKTIFAISHDDH--YFIHADRLLEMRNGQ 526
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
98-249 |
4.79e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 98 IGIMGPSGSGKSTLMNLLAG---------------------YRKSGMKG--QILVNGKpreLRTFRKMScYImqeDiLLP 154
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGelipnlgdyeeepswdevlkrFRGTELQNyfKKLYNGE---IKVVHKPQ-YV---D-LIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 155 HL---TVLEAmmisanLKLNEKQEVKKELVTEiltaLGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 231
Cdd:PRK13409 174 KVfkgKVREL------LKKVDERGKLDEVVER----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170
....*....|....*...
gi 157427812 232 DSASSFQVASLMKSLAQG 249
Cdd:PRK13409 244 DIRQRLNVARLIRELAEG 261
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
96-278 |
4.79e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSgmKGQILVNGKPRELRT----FRKMSCYIMQE---DILLPHLTVLEAMMISA- 166
Cdd:PRK10762 279 EILGVSGLMGAGRTELMKVLYGaLPRT--SGYVTLDGHEVVTRSpqdgLANGIVYISEDrkrDGLVLGMSVKENMSLTAl 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 167 ------NLKLNEKQEvkKELVTEILTALGLLSCSHTRT-ALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQV 239
Cdd:PRK10762 357 ryfsraGGSLKHADE--QQAVSDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEI 434
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 157427812 240 ASLMKSLAQGGRTIICTihqpSAKLFE---MFDKLYILSQGQ 278
Cdd:PRK10762 435 YQLINQFKAEGLSIILV----SSEMPEvlgMSDRILVMHEGR 472
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
60-278 |
5.25e-09 |
|
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: 56.65 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 60 DIEFVELSysVREGPcwrkrGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLmnLLAGYRKS-GMKGQILVNGKP----- 133
Cdd:cd03369 6 EIEVENLS--VRYAP-----DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLeAEEGKIEIDGIDistip 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 134 -RELRtfRKMSCyIMQEDILLphltvleAMMISANL-KLNEKQEVkkelvtEILTALGLLSCSHTrtalLSGGQRKRLAI 211
Cdd:cd03369 77 lEDLR--SSLTI-IPQDPTLF-------SGTIRSNLdPFDEYSDE------EIYGALRVSEGGLN----LSQGQRQLLCL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157427812 212 ALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGrTIICTIHQPSAKLfeMFDKLYILSQGQ 278
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNS-TILTIAHRLRTII--DYDKILVMDAGE 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
96-254 |
6.11e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.03 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRK--SG-MKGQILVNGKPRELRTFRKMscyimqedillphlTVlEAMMISANlklNE 172
Cdd:COG1245 367 EVLGIVGPNGIGKTTFAKILAGVLKpdEGeVDEDLKISYKPQYISPDYDG--------------TV-EEFLRSAN---TD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 173 KQEVKKeLVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQG-GR 251
Cdd:COG1245 429 DFGSSY-YKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGK 507
|
...
gi 157427812 252 TII 254
Cdd:COG1245 508 TAM 510
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
96-283 |
8.34e-09 |
|
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: 56.39 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSgmKGQILVNGKPR---ELRTFrkmscyimqediLLPHLTVLEAMMISANLkLN 171
Cdd:cd03220 49 ERIGLIGRNGAGKSTLLRLLAGiYPPD--SGTVTVRGRVSsllGLGGG------------FNPELTGRENIYLNGRL-LG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 172 EKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAssFQ--VASLMKSLAQG 249
Cdd:cd03220 114 LSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA--FQekCQRRLRELLKQ 191
|
170 180 190
....*....|....*....|....*....|....
gi 157427812 250 GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03220 192 GKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
96-283 |
1.33e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.86 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAG-YRKSgmKGQILVNGK---PRELRTfrkmscyimqedILLPHLTVLEammisaNLKLN 171
Cdd:COG1134 53 ESVGIIGRNGAGKSTLLKLIAGiLEPT--SGRVEVNGRvsaLLELGA------------GFHPELTGRE------NIYLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 172 ------EKQEVkKELVTEIL--TALG--LlscsHT--RTalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAssFQ- 238
Cdd:COG1134 113 grllglSRKEI-DEKFDEIVefAELGdfI----DQpvKT--YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA--FQk 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 157427812 239 -VASLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:COG1134 184 kCLARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMDG 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
95-267 |
1.36e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 56.33 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 95 REMIGIMGPSGSGKSTLM-------NLLAGYRksgMKGQILVNGK--------PRELRTFRKMscyIMQEDILLPHlTVL 159
Cdd:PRK14243 36 NQITAFIGPSGCGKSTILrcfnrlnDLIPGFR---VEGKVTFHGKnlyapdvdPVEVRRRIGM---VFQKPNPFPK-SIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 160 EAmmISANLKLNEKQEVKKELVTEILTALGLLScsHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:PRK14243 109 DN--IAYGARINGYKGDMDELVERSLRQAALWD--EVKDKLkqsglsLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 157427812 234 ASSFQVASLMKSLAQgGRTIICTIH--QPSAKLFEM 267
Cdd:PRK14243 185 ISTLRIEELMHELKE-QYTIIIVTHnmQQAARVSDM 219
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
61-283 |
1.55e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.34 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 61 IEFVELSYSVREGPCWRKRGYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPRELRTFR 140
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-SGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 141 KMSCYIMQedILLPHLTVLE-----AMMISANLKLNEK--QEVKKELVTEILTALGLLScSHTR--TALLSGGQRKRLAI 211
Cdd:PRK15112 84 YRSQRIRM--IFQDPSTSLNprqriSQILDFPLRLNTDlePEQREKQIIETLRQVGLLP-DHASyyPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157427812 212 ALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL--AQGGRTIICTIHQPSAKlfEMFDKLYILSQGQCIFKG 283
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMK--HISDQVLVMHQGEVVERG 232
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
96-289 |
1.94e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 57.41 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPrelrtfrkmsCYIMQEDILLPHLTVLEAM------MISANLK 169
Cdd:PRK10789 342 QMLGICGPTGSGKSTLLSLIQRHFDVS-EGDIRFHDIP----------LTKLQLDSWRSRLAVVSQTpflfsdTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 LNEKQEVKKELvteilTALGLLSCSH---------------TRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 234
Cdd:PRK10789 411 LGRPDATQQEI-----EHVARLASVHddilrlpqgydtevgERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGR 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157427812 235 SSFQVaslMKSLAQGG--RTIICTIHQPSAkLFEMfDKLYILSQGQCIFKGMVTNLI 289
Cdd:PRK10789 486 TEHQI---LHNLRQWGegRTVIISAHRLSA-LTEA-SEILVMQHGHIAQRGNHDQLA 537
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
100-232 |
2.02e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.42 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYrKSGMKGQILVNGK---PRELRTF-----RKMScYIMQEDILLPHLTVleammiSANLKLN 171
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGL-TRPQKGRIVLNGRvlfDAEKGIClppekRRIG-YVFQDARLFPHYKV------RGNLRYG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157427812 172 ekqeVKKELVTEILTALGLLSCSH--TRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK11144 101 ----MAKSMVAQFDKIVALLGIEPllDRYPGsLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
96-300 |
2.03e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 55.86 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTL---MNLLAgyrkSGMKGQILVNG----KPRELRTFRKMSCYIMQE-DILLPHLTVLEAMMISA- 166
Cdd:PRK13633 37 EFLVILGRNGSGKSTIakhMNALL----IPSEGKVYVDGldtsDEENLWDIRNKAGMVFQNpDNQIVATIVEEDVAFGPe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 167 NLKLnEKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL 246
Cdd:PRK13633 113 NLGI-PPEEIRER-VDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKEL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 247 -AQGGRTIICTIH--QPSAKLfemfDKLYILSQGQCIFKGMVTNL---IPYLKGLGLHCP 300
Cdd:PRK13633 191 nKKYGITIILITHymEEAVEA----DRIIVMDSGKVVMEGTPKEIfkeVEMMKKIGLDVP 246
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
201-274 |
2.43e-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: 53.90 E-value: 2.43e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157427812 201 LSGGQRKRLAIALEL----VNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQPsaKLFEMFDKLYIL 274
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLIHI 153
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
97-259 |
3.85e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.80 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 97 MIGIMGPSGSGKSTLMNLLAG-YRKSgmKGQILVNGK--PRELRTFRKMSCYIMQEDILLPHLTVLEAMMI-----SANL 168
Cdd:PRK13540 29 LLHLKGSNGAGKTTLLKLIAGlLNPE--KGEILFERQsiKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYdihfsPGAV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 169 KlnekqevkkelVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ 248
Cdd:PRK13540 107 G-----------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRA 175
|
170
....*....|.
gi 157427812 249 GGRTIICTIHQ 259
Cdd:PRK13540 176 KGGAVLLTSHQ 186
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
98-258 |
4.25e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 98 IGIMGPSGSGKSTLMNLLAGYRKSgmkgqilVNGKPRELRTFRkmSCYIMQEDILLPHLTVLEAMM-------------- 163
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKE-------FEGEARPAPGIK--VGYLPQEPQLDPEKTVRENVEegvaevkaaldrfn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 164 -ISANL--------KLNEKQEvkkELvTEILTALGL-------------LSC--SHTRTALLSGGQRKRLAIALELVNNP 219
Cdd:PRK11819 107 eIYAAYaepdadfdALAAEQG---EL-QEIIDAADAwdldsqleiamdaLRCppWDAKVTKLSGGERRRVALCRLLLEKP 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 157427812 220 PVMFFDEPTSGLDSASsfqVASLMKSLAQGGRTIICTIH 258
Cdd:PRK11819 183 DMLLLDEPTNHLDAES---VAWLEQFLHDYPGTVVAVTH 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
96-248 |
6.10e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.32 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKS-----TLMNLLAGYRKSGmkGQILVNGKPRELRTFR-KMSCYIMQ--EDILLPHLTVleAMMISAN 167
Cdd:PRK10418 30 RVLALVGGSGSGKSltcaaALGILPAGVRQTA--GRVLLDGKPVAPCALRgRKIATIMQnpRSAFNPLHTM--HTHARET 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 LKLNEKQEVKKELVtEILTALGLlscSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVAS 241
Cdd:PRK10418 106 CLALGKPADDATLT-AALEAVGL---ENAARVLklypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILD 181
|
....*..
gi 157427812 242 LMKSLAQ 248
Cdd:PRK10418 182 LLESIVQ 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
96-246 |
1.63e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGK------PRELRTFRKMSCYIMQEDI--LLPHLTVLEAMMISAN 167
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVES-QGGEIIFNGQridtlsPGKLQALRRDIQFIFQDPYasLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 LKLNEKQEVKKELVTEILTALGLLSCSHTRTA-LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL 246
Cdd:PRK10261 430 VHGLLPGKAAAARVAWLLERVGLLPEHAWRYPhEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
96-254 |
2.01e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGK------PRELRTfRKMScYIMQE---DILLPHLTVLEAMM--- 163
Cdd:COG3845 285 EILGIAGVAGNGQSELAEALAGLRPPA-SGSIRLDGEditglsPRERRR-LGVA-YIPEDrlgRGLVPDMSVAENLIlgr 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 164 -----ISANLKLNEK--QEVKKELVTE--ILTAlGLlscsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 234
Cdd:COG3845 362 yrrppFSRGGFLDRKaiRAFAEELIEEfdVRTP-GP----DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVG 436
|
170 180
....*....|....*....|
gi 157427812 235 SSFQVASLMKSLAQGGRTII 254
Cdd:COG3845 437 AIEFIHQRLLELRDAGAAVL 456
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
96-278 |
2.69e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.43 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPR------ELRtfRKMSCYIMQEDILLPHLTVLEAMMISANLK 169
Cdd:PRK13650 34 EWLSIIGHNGSGKSTTVRLIDGLLEAE-SGQIIIDGDLLteenvwDIR--HKIGMVFQNPDNQFVGATVEDDVAFGLENK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 170 LNEKQEVKkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQG 249
Cdd:PRK13650 111 GIPHEEMK-ERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDD 189
|
170 180 190
....*....|....*....|....*....|..
gi 157427812 250 -GRTIICTIHQpsakLFE--MFDKLYILSQGQ 278
Cdd:PRK13650 190 yQMTVISITHD----LDEvaLSDRVLVMKNGQ 217
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
80-258 |
3.05e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.30 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 80 GYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRkSGMKGQILVNGKPRELRTFRKMSCYI--MQEDILLPHLT 157
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-TPAHGHVWLDGEHIQHYASKEVARRIglLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 158 VLEAMMISANLK----LNEKQEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:PRK10253 97 TVQELVARGRYPhqplFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180
....*....|....*....|....*.
gi 157427812 234 ASSFQVASLMKSL-AQGGRTIICTIH 258
Cdd:PRK10253 177 SHQIDLLELLSELnREKGYTLAAVLH 202
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
100-285 |
3.97e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAG-YRKSGMKGQILVNGKPRELRTFR----KMSCYIMQEDILLPHLTVLEammisaNLKL-NEK 173
Cdd:NF040905 32 LCGENGAGKSTLMKVLSGvYPHGSYEGEILFDGEVCRFKDIRdseaLGIVIIHQELALIPYLSIAE------NIFLgNER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 174 --------QEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKS 245
Cdd:NF040905 106 akrgvidwNETNRR-ARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 157427812 246 L-AQGGRTIIctIhqpSAKLFEMF---DKLYILSQGQC---------------IFKGMV 285
Cdd:NF040905 185 LkAQGITSII--I---SHKLNEIRrvaDSITVLRDGRTietldcradevtedrIIRGMV 238
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
96-258 |
7.67e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 51.17 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPRELRT---FRKMSCYIMQ-------------------EDILL 153
Cdd:PRK13635 34 EWVAIVGHNGSGKSTLAKLLNGLLLPE-AGTITVGGMVLSEETvwdVRRQVGMVFQnpdnqfvgatvqddvafglENIGV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 154 PHLTvleamMIsanlklnekqevkkELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:PRK13635 113 PREE-----MV--------------ERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDP 173
|
170 180
....*....|....*....|....*.
gi 157427812 234 ASSFQVASLMKSL-AQGGRTIICTIH 258
Cdd:PRK13635 174 RGRREVLETVRQLkEQKGITVLSITH 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
96-254 |
7.70e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGY-RKSGmkGQILVNGKPRELRTFRK-MSCYIM------QEDILLPHLTVLEAMMISA- 166
Cdd:PRK11288 280 EIVGLFGLVGAGRSELMKLLYGAtRRTA--GQVYLDGKPIDIRSPRDaIRAGIMlcpedrKAEGIIPVHSVADNINISAr 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 167 ------NLKLNEKQEvkKELVTEILTALGLLSCS-HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQV 239
Cdd:PRK11288 358 rhhlraGCLINNRWE--AENADRFIRSLNIKTPSrEQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEI 435
|
170
....*....|....*
gi 157427812 240 ASLMKSLAQGGRTII 254
Cdd:PRK11288 436 YNVIYELAAQGVAVL 450
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
96-246 |
1.12e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.48 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPRELRTF----RKMSCYIMQEDILLPHLTVLEAMMISANLKLN 171
Cdd:PRK13642 34 EWVSIIGQNGSGKSTTARLIDGLFEE-FEGKVKIDGELLTAENVwnlrRKIGMVFQNPDNQFVGATVEDDVAFGMENQGI 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157427812 172 EKQEVKKElVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL 246
Cdd:PRK13642 113 PREEMIKR-VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI 186
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
63-278 |
1.18e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.59 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 63 FVELSYSVREGpcwrkrgyktllkclsgkfccrEMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGkprelRTFRKM 142
Cdd:PRK15439 279 FRNISLEVRAG----------------------EILGLAGVVGAGRTELAETLYGLRPA-RGGRIMLNG-----KEINAL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 143 SCYI-MQEDIL-LP-----HLTVLEAMmISAN---LKLNEK---QEVKKE--LVTEILTALGLlSCSHTRTAL--LSGGQ 205
Cdd:PRK15439 331 STAQrLARGLVyLPedrqsSGLYLDAP-LAWNvcaLTHNRRgfwIKPAREnaVLERYRRALNI-KFNHAEQAArtLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157427812 206 RKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTihqpSAKLFE---MFDKLYILSQGQ 278
Cdd:PRK15439 409 QQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFI----SSDLEEieqMADRVLVMHQGE 480
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
95-261 |
1.51e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 95 REMIGIMGPSGSGKSTLmnLLAGYRKSGmkgqilvngkprELRTFRKMSCYIMQEDILLPHLTVLEAMMISAnLKLNEKq 174
Cdd:cd03238 21 NVLVVVTGVSGSGKSTL--VNEGLYASG------------KARLISFLPKFSRNKLIFIDQLQFLIDVGLGY-LTLGQK- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 175 evkkelvteiltalgllscshtrTALLSGGQRKRLAIALEL-VNNPPVMF-FDEPTSGLDSASSFQVASLMKSLAQGGRT 252
Cdd:cd03238 85 -----------------------LSTLSGGELQRVKLASELfSEPPGTLFiLDEPSTGLHQQDINQLLEVIKGLIDLGNT 141
|
....*....
gi 157427812 253 IICTIHQPS 261
Cdd:cd03238 142 VILIEHNLD 150
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
96-251 |
1.54e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.72 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKsgmkgqilvngkPRElrtfrkmscyimqEDILLPHLTVLeammisanlklnekqe 175
Cdd:cd03222 26 EVIGIVGPNGTGKTTAVKILAGQLI------------PNG-------------DNDEWDGITPV---------------- 64
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157427812 176 VKKELVTeiltalgllscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGR 251
Cdd:cd03222 65 YKPQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
96-232 |
2.15e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGyrksgmkGQILVNGK----------------PRE-------------------LRTFR 140
Cdd:PRK11147 30 ERVCLVGRNGAGKSTLMKILNG-------EVLLDDGRiiyeqdlivarlqqdpPRNvegtvydfvaegieeqaeyLKRYH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 141 KMSCYIMQE--DILLPHLTVLEAMMISANLKLNEKQevkkelVTEILTALGLlsCSHTRTALLSGGQRKRLAIALELVNN 218
Cdd:PRK11147 103 DISHLVETDpsEKNLNELAKLQEQLDHHNLWQLENR------INEVLAQLGL--DPDAALSSLSGGWLRKAALGRALVSN 174
|
170
....*....|....
gi 157427812 219 PPVMFFDEPTSGLD 232
Cdd:PRK11147 175 PDVLLLDEPTNHLD 188
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
195-278 |
2.57e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 195 HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIIcTIHQPSAKLFEMFDKLYIL 274
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII-IISSEMPELLGITDRILVM 464
|
....
gi 157427812 275 SQGQ 278
Cdd:PRK10982 465 SNGL 468
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
97-232 |
2.77e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.51 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 97 MIGIMGPSGSGKSTLMNLLAGYRKsGMKGQILVNGKPRELRTFRKMSCYimqeDI----------LLPHLTVLEAMMISA 166
Cdd:NF033858 29 MVGLIGPDGVGKSSLLSLIAGARK-IQQGRVEVLGGDMADARHRRAVCP----RIaympqglgknLYPTLSVFENLDFFG 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157427812 167 NLKLNEKQEvKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:NF033858 104 RLFGQDAAE-RRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
92-259 |
3.76e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 92 FCC--REMIGIMGPSGSGKSTLMNLLAGY------------------------------RKSGMK--------------- 124
Cdd:PTZ00265 1189 FSCdsKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgdeeQNVGMKnvnefsltkeggsge 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 125 --------GQILVNGK---PRELRTFRKMSCYIMQEDILLphltvleAMMISANLKLNE----KQEVKK----------- 178
Cdd:PTZ00265 1269 dstvfknsGKILLDGVdicDYNLKDLRNLFSIVSQEPMLF-------NMSIYENIKFGKedatREDVKRackfaaidefi 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 179 -ELVTEILTALGLLSCShtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLA-QGGRTIICT 256
Cdd:PTZ00265 1342 eSLPNKYDTNVGPYGKS------LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITI 1415
|
...
gi 157427812 257 IHQ 259
Cdd:PTZ00265 1416 AHR 1418
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
100-248 |
4.93e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.17 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYRkSGMKGQILVNGKP-REL--RTFRKMSCYIMQEDILLPHlTVLEAMMISANLKlNEKQEV 176
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLI-SPTSGTLLFEGEDiSTLkpEIYRQQVSYCAQTPTLFGD-TVYDNLIFPWQIR-NQQPDP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 177 KK--------ELVTEILTalgllscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQ 248
Cdd:PRK10247 115 AIflddlerfALPDTILT---------KNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVR 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
100-232 |
5.27e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.19 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGYRKSGmKGQILvngKPRELRTfrkmsCYIMQE---DILLPhLTVLEAMMISANlklnekqeV 176
Cdd:PRK09544 35 LLGPNGAGKSTLVRVVLGLVAPD-EGVIK---RNGKLRI-----GYVPQKlylDTTLP-LTVNRFLRLRPG--------T 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 157427812 177 KKElvtEILTALGLLSCSHTRTA---LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK09544 97 KKE---DILPALKRVQAGHLIDApmqKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
96-278 |
7.88e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTL-MNLLAGYRKSGMKGQILVNGKPRELRTF--------------RKMSCYIMQEDIL----LPHL 156
Cdd:NF040905 287 EIVGIAGLMGAGRTELaMSVFGRSYGRNISGTVFKDGKEVDVSTVsdaidaglayvtedRKGYGLNLIDDIKrnitLANL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 157 TvleamMISANLKLNEKQEVKkeLVTEILTALGLLSCS-HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 235
Cdd:NF040905 367 G-----KVSRRGVIDENEEIK--VAEEYRKKMNIKTPSvFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGA 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 157427812 236 SFQVASLMKSLAQGGRTIIcTIhqpSAKLFE---MFDKLYILSQGQ 278
Cdd:NF040905 440 KYEIYTIINELAAEGKGVI-VI---SSELPEllgMCDRIYVMNEGR 481
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
96-261 |
1.49e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKprelrtfrkmSCYIMQEDILLPHLTVLEAMMISAnLKLNEKQE 175
Cdd:PRK13545 51 EIVGIIGLNGSGKSTLSNLIAGVTMPN-KGTVDIKGS----------AALIAISSGLNGQLTGIENIELKG-LMMGLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 176 VKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIIC 255
Cdd:PRK13545 119 KIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFF 198
|
....*.
gi 157427812 256 TIHQPS 261
Cdd:PRK13545 199 ISHSLS 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
201-261 |
1.73e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 1.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157427812 201 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL-AQGGRTIICTIHQPS 261
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLS 641
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
96-259 |
2.17e-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: 46.17 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPRELRTF-------RKMSCYIMQEDILLpHLTVLEAMMISANL 168
Cdd:cd03290 28 QLTMIVGQVGCGKSSLLLAILGEMQT-LEGKVHWSNKNESEPSFeatrsrnRYSVAYAAQKPWLL-NATVEENITFGSPF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 169 KlneKQEVKkeLVTEI--------LTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASS--FQ 238
Cdd:cd03290 106 N---KQRYK--AVTDAcslqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSdhLM 180
|
170 180
....*....|....*....|.
gi 157427812 239 VASLMKSLAQGGRTIICTIHQ 259
Cdd:cd03290 181 QEGILKFLQDDKRTLVLVTHK 201
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
58-295 |
5.06e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.89 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 58 AVDiefvELSYSVREGpcwrkrgyktllkclsgkfccrEMIGIMGPSGSGKS----TLMNLLaGYRKSGMKGQILVNGkp 133
Cdd:PRK11022 22 AVD----RISYSVKQG----------------------EVVGIVGESGSGKSvsslAIMGLI-DYPGRVMAEKLEFNG-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 134 RELRTF-----RKMS----CYIMQEDI--LLPHLTVleAMMISANLKLNE--KQEVKKELVTEILTALGL---LSCSHTR 197
Cdd:PRK11022 73 QDLQRIsekerRNLVgaevAMIFQDPMtsLNPCYTV--GFQIMEAIKVHQggNKKTRRQRAIDLLNQVGIpdpASRLDVY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 198 TALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQG 277
Cdd:PRK11022 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAG 230
|
250 260
....*....|....*....|...
gi 157427812 278 QCIFKGMVTNLI-----PYLKGL 295
Cdd:PRK11022 231 QVVETGKAHDIFraprhPYTQAL 253
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
406-564 |
5.30e-05 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 45.84 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 406 IGLLYLQTGNDANKVLNNTGCLFFSILFLMFAAMMPTVLTFPLEMAVFLReHLNYWYSLKIYFLAKTMADVPFQVICPAV 485
Cdd:pfam12698 145 IPVESTPLFNPQSGYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKER-LLVSGVSPLQYWLGKILGDFLVGLLQLLI 223
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157427812 486 YCSIMYWMTSQPAETSRFLLFLALGAstaLAAQSLGMLIGAASSSLQVATFLGPVTAIPVLLFSGFFVSFKAIPSYLQW 564
Cdd:pfam12698 224 ILLLLFGIGIPFGNLGLLLLLFLLYG---LAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQW 299
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
96-232 |
6.02e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKP---RELRTFRK---MScyimQEDILLPHLTVLEammisaNLK 169
Cdd:NF033858 293 EIFGFLGSNGCGKSTTMKMLTGLLPAS-EGEAWLFGQPvdaGDIATRRRvgyMS----QAFSLYGELTVRQ------NLE 361
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157427812 170 LNEK-----QEVKKELVTEILTALGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:NF033858 362 LHARlfhlpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
97-277 |
1.17e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 97 MIGIMGPSGSGKSTLMNLLAGYRKSGMKGQILVNGKprelrtfrkmSCYIMQEDILLpHLTVLEAMMISANLklnEKQEV 176
Cdd:PLN03232 645 LVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGS----------VAYVPQVSWIF-NATVRENILFGSDF---ESERY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 177 KKEL-VTEILTALGLLScSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQV-ASLMKSLAQ 248
Cdd:PLN03232 711 WRAIdVTALQHDLDLLP-GRDLTEIgergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELK 789
|
170 180 190
....*....|....*....|....*....|.
gi 157427812 249 GGRTIICT--IHqpsakLFEMFDKLYILSQG 277
Cdd:PLN03232 790 GKTRVLVTnqLH-----FLPLMDRIILVSEG 815
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
100-254 |
1.22e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 100 IMGPSGSGKSTLMNLLAGyRKSGMKGQiLVNGKPRELR-TFRKMSCYIMQE------DILLPH-----LTVLEamMIsan 167
Cdd:PRK10938 34 FVGANGSGKSALARALAG-ELPLLSGE-RQSQFSHITRlSFEQLQKLVSDEwqrnntDMLSPGeddtgRTTAE--II--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 168 lklneKQEVKKELVTEILTA-LGLLSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSL 246
Cdd:PRK10938 107 -----QDEVKDPARCEQLAQqFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASL 181
|
....*...
gi 157427812 247 AQGGRTII 254
Cdd:PRK10938 182 HQSGITLV 189
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
258-315 |
1.51e-04 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 44.51 E-value: 1.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 157427812 258 HQPSAKLFEMFDKLYILSQGQCI-FKGMVTNLIPYLKGLGLHCPTYHNPADFIIEVASG 315
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTvYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEG 59
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
96-288 |
1.59e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 44.08 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 96 EMIGIMGPSGSGKSTLMNLLAGYRKSGmKGQILVNGKPrelrTFRKMSCYIM----QEDILL-------PHLTVLEAMMI 164
Cdd:cd03291 64 EMLAITGSTGSGKTSLLMLILGELEPS-EGKIKHSGRI----SFSSQFSWIMpgtiKENIIFgvsydeyRYKSVVKACQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 165 SANL-KLNEKQEVkkelvteILTALGLLscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQV--AS 241
Cdd:cd03291 139 EEDItKFPEKDNT-------VLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfeSC 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157427812 242 LMKSLAQGGRTIIctihqpSAKL--FEMFDKLYILSQGQCIFKGMVTNL 288
Cdd:cd03291 203 VCKLMANKTRILV------TSKMehLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
61-278 |
2.45e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 61 IEFVELSYSVREGPcwrkrgykTLLKCLSGKFCCREMIGIMGPSGSGKSTLMNLLAGYRKSgMKGQILVNGKPReLRTFR 140
Cdd:PLN03073 509 ISFSDASFGYPGGP--------LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQP-SSGTVFRSAKVR-MAVFS 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 141 K----------------MSCYI-MQEDILLPHLTvleAMMISANLKLnekqevkKELVTeiltalgllscshtrtalLSG 203
Cdd:PLN03073 579 QhhvdgldlssnpllymMRCFPgVPEQKLRAHLG---SFGVTGNLAL-------QPMYT------------------LSG 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157427812 204 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASsfqVASLMKSLA--QGGrtiICTIHQPSAKLFEMFDKLYILSQGQ 278
Cdd:PLN03073 631 GQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVlfQGG---VLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
146-261 |
2.51e-04 |
|
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: 43.53 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 146 IMQEDILLPHLTVLEAMMISANLKLNEKQEVKKELVTEILTALGLLscsHTRTA-LLSGGQRK---RLAIALELVNNPPV 221
Cdd:pfam13304 184 LLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGG---GELPAfELSDGTKRllaLLAALLSALPKGGL 260
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 157427812 222 MFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQPS 261
Cdd:pfam13304 261 LLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
201-276 |
2.91e-04 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 43.02 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 201 LSGGQRKRLAIALEL----VNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRtIICTIHQPsaKLFEMFDKLYILSQ 276
Cdd:cd03272 159 LSGGQKSLVALALIFaiqkCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQ-FITTTFRP--ELLEVADKFYGVKF 235
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
201-295 |
3.96e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.87 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 201 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCI 280
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90 100
....*....|....*....|
gi 157427812 281 FKGMVTNLI-----PYLKGL 295
Cdd:PRK15093 239 ETAPSKELVttphhPYTQAL 258
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
97-233 |
6.19e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 43.01 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 97 MIGIMGPSGSGKSTLMN-LLAGYRKsgMKGQILVNGKPRELRTFRKMSCYIMQEDILLPHL-------TVLEAMMISANL 168
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSaLLAEMDK--VEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKAlnekyyqQVLEACALLPDL 743
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157427812 169 KL---NEKQEVKKELVTeiltalgllscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:TIGR00957 744 EIlpsGDRTEIGEKGVN------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
201-272 |
1.53e-03 |
|
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: 40.28 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 201 LSGGQRK------RLAIALELVNNPPVMFFDEPTSGLDSAS-SFQVASLMKS-LAQGGRTIICTIHQPsaKLFEMFDKLY 272
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEErKSQKNFQLIVITHDE--ELVDAADHIY 193
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
201-258 |
2.12e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 2.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157427812 201 LSGGQRKRLAIALELVN---NPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIH 258
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
80-117 |
2.78e-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: 39.69 E-value: 2.78e-03
10 20 30
....*....|....*....|....*....|....*...
gi 157427812 80 GYKTLLKCLSGKFCCremigIMGPSGSGKSTLMNLLAG 117
Cdd:cd01854 75 GLDELRELLKGKTSV-----LVGQSGVGKSTLLNALLP 107
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
70-288 |
5.99e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 70 VREGPCWRKR-GYKTLLKCLSGKFCCREMIGIMGPSGSGKSTLmnLLAGYRKSGM-KGQILVNGKP------RELRtfRK 141
Cdd:PTZ00243 1310 VFEGVQMRYReGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTL--LLTFMRMVEVcGGEIRVNGREigayglRELR--RQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 142 MScYIMQEDILL---------PHLTVLEAMMISANLKLNEKQEVKKElvteiltALGLLSCSHTRTALLSGGQRKRLAIA 212
Cdd:PTZ00243 1386 FS-MIPQDPVLFdgtvrqnvdPFLEASSAEVWAALELVGLRERVASE-------SEGIDSRVLEGGSNYSVGQRQLMCMA 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157427812 213 LELVN-NPPVMFFDEPTSGLDSASSFQV-ASLMKSLAqgGRTIICTIHQpsAKLFEMFDKLYILSQG------------- 277
Cdd:PTZ00243 1458 RALLKkGSGFILMDEATANIDPALDRQIqATVMSAFS--AYTVITIAHR--LHTVAQYDKIIVMDHGavaemgsprelvm 1533
|
250
....*....|...
gi 157427812 278 --QCIFKGMVTNL 288
Cdd:PTZ00243 1534 nrQSIFHSMVEAL 1546
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
100-124 |
6.48e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 39.55 E-value: 6.48e-03
10 20
....*....|....*....|....*.
gi 157427812 100 IMGPSGSGKSTLMN-LLAGYRKSGMK 124
Cdd:COG3451 209 ILGPSGSGKSFLLKlLLLQLLRYGAR 234
|
|
| GBP |
cd01851 |
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
98-121 |
7.20e-03 |
|
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.
Pssm-ID: 206650 Cd Length: 224 Bit Score: 38.46 E-value: 7.20e-03
10 20
....*....|....*....|....
gi 157427812 98 IGIMGPSGSGKSTLMNLLAGYRKS 121
Cdd:cd01851 10 VSVFGSQSSGKSFLLNHLFGTSDG 33
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
201-258 |
7.93e-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: 39.61 E-value: 7.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157427812 201 LSGGQRKRLAIALEL---VNNPPVMFFDEPTSGLDSASSFQVASLMKSLAQGGRTIICTIH 258
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
80-117 |
9.17e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.52 E-value: 9.17e-03
10 20 30
....*....|....*....|....*....|....*...
gi 157427812 80 GYKTLLKCLSGKFCCremigIMGPSGSGKSTLMNLLAG 117
Cdd:pfam03193 96 GIEALKELLKGKTTV-----LAGQSGVGKSTLLNALLP 128
|
|
| |
